209 results on '"Josef R. Patsch"'
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152. Structure and Metabolism of Low Density Lipoproteins from Normal and Hypertriglyceridemic Subjects
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Henry J. Pownall, Josef R. Patsch, and Barry J. McKeone
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Very low-density lipoprotein ,biology ,Chemistry ,Phosphatidylcholine transfer protein ,Metabolism ,Sphingolipid ,chemistry.chemical_compound ,Biochemistry ,Cholesterylester transfer protein ,biology.protein ,Cholesteryl ester ,lipids (amino acids, peptides, and proteins) ,Plant lipid transfer proteins ,Lipoprotein - Abstract
Human plasma lipoproteins are complex assemblies of lipids and proteins whose identities are operationally defined by the densities at which they are isolated as the high, low, and very low density lipoproteins, HDL, LDL and VLDL, respectively. Lipoproteins transport glycerol and sphingolipids as well as free and esterified cholesterol along with apoproteins which may, depending on their identity, activate lipolytic enzymes or serve as ligands for receptor-mediated endocytosis. In addition to these important proteins, human plasma also contains a number of proteins that transport monomeric lipids between lipoprotein classes. Most notable among these are cholesterol ester transfer protein and phosphatidylcholine transfer protein. Lipolytic enzymes, lipoprotein receptors, and lipid transfer protein are the major endogenous factors that modify the concentration, composition, and structure of plasma lipoproteins. The major exogenous factors are found in the diet and include the amount and kinds of fatty acids that are consumed. more...
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- 1990
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153. What Factors Regulate the Action of Lipoprotein Lipase?
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Magnus Hultin, Gunilla Bengtsson-Olivecrona, Senén Vilaró, Jonas Peterson, Thomas Olivecrona, Josef R. Patsch, Richard J. Deckelbaum, and Yvon Carpentier
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medicine.medical_specialty ,Lipoprotein lipase ,Endothelium ,Chemistry ,Triglyceride transport ,Hydrolysis ,Endocrinology ,medicine.anatomical_structure ,Biochemistry ,Plasma triglyceride ,Internal medicine ,medicine ,Tissue distribution ,Lipoprotein - Abstract
Triglyceride transport is an efficient process. Meals containing as much as 100 g triglycerides are usually absorbed and disposed within a few hours with only a moderate rise in the plasma triglyceride concentration.1 Most of the lipoprotein triglycerides are unloaded through hydrolysis by lipoprotein lipase at endothelial sites in extra-hepatic tissues.2 It is often stated that this step is rate-limiting for triglyceride transport, and that it directs the tissue distribution of lipid uptake.3 Inherent in this concept are two assumptions that we will discuss in this paper. more...
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- 1990
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154. Effect of alcohol dose on plasma lipoprotein subfractions and lipolytic enzyme activity in active and inactive men
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John P. Foreyt, Antonio M. Gotto, Larry P. Kroch, G. Harley Hartung, Josef R. Patsch, Rebecca S. Reeves, and Wolfgang Patsch
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Adult ,Male ,medicine.medical_specialty ,Apolipoprotein B ,Alcohol Drinking ,Endocrinology, Diabetes and Metabolism ,media_common.quotation_subject ,Lipoproteins ,Alcohol ,chemistry.chemical_compound ,Endocrinology ,Internal medicine ,medicine ,Humans ,Exercise ,Apolipoproteins A ,Triglycerides ,media_common ,Lipoprotein lipase ,Ethanol ,biology ,Apolipoprotein A-I ,Dose-Response Relationship, Drug ,Cholesterol ,Cholesterol, HDL ,Lipoproteins, HDL3 ,Lipase ,Abstinence ,Middle Aged ,Lipoproteins, HDL2 ,Diet ,Jogging ,Lipoprotein Lipase ,chemistry ,Liver ,biology.protein ,lipids (amino acids, peptides, and proteins) ,Hepatic lipase ,Lipoproteins, HDL ,Lipoprotein - Abstract
Controversy as to which lipoprotein subfraction of high-density lipoprotein (HDL) increases during alcohol consumption prompted the current study of the effects of two alcohol doses over varying time intervals on plasma lipoproteins and lipolytic enzymes. Measurements were made in 49 healthy men before and after three weeks of abstinence from alcohol and after consumption of one or three 12-ounce cans of beer per day. We found that HDL (10%), HDL2 (14%), and HDL3 (9%) cholesterol, and apolipoprotein A-I (7%) decreased with abstinence from alcohol and then increased with its consumption. These increases were not significant until after 3 weeks of daily alcohol intake, but they were significant in both the one-can and three-cans of beer per day groups. In the 23 inactive subjects HDL and HDL2 cholesterol decreased with abstinence but did not increase significantly with alcohol intake. Lipolytic enzymes were not changed by alcohol manipulation, but the level of lipoprotein lipase was higher and that of hepatic lipase was lower at each measurement point in the 26 habitually active versus the 23 inactive subjects. Adjustment for weight or skinfold thickness did not affect lipoprotein changes over time within groups but did eliminate many of the differences between activity groups. Alcohol consumption seems to be related to possibly beneficial influences on plasma HDL and HDL2 cholesterol, and may thus impact the risk of heart disease. more...
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- 1990
155. Regulation of hepatic lipoprotein biosynthesis by hormones
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Wolfgang Patsch, Yen-Chiu Lin-Lee, N. L. Gorder, Josef R. Patsch, W. Strobl, and Antonio M. Gotto
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medicine.medical_specialty ,Very low-density lipoprotein ,Messenger RNA ,Apolipoprotein B ,biology ,Chemistry ,Endoplasmic reticulum ,nutritional and metabolic diseases ,Endocrinology ,Transcription (biology) ,Internal medicine ,Gene expression ,polycyclic compounds ,medicine ,biology.protein ,lipids (amino acids, peptides, and proteins) ,Lipoprotein ,Hormone - Abstract
To identify key regulatory processes of hepatic lipoprotein production, we studied the effects of hormonal perturbations on lipoprotein biosynthesis in the rat. Insulin administration to cultured hepatocytes inhibits the secretion of triglycerides, and apolipoproteins B and E, but does not alter secretory rates of apoproteins A-I and C-III. Net synthesis of apoB and E is not reduced by the hormone, but the rate of transport of apoB from the endoplasmic reticulum to the Golgi is diminished, and the association of apoB with triglyceride declines, resulting in reduced formation of nascent VLDL. Thus, intracellular transport of individual apoproteins is a specific process that can be selectively regulated by physiologic stimuli and that can affect net hepatic lipoprotein production. Thyroid hormones enhance hepatic net production of apoA-I in the rat. Twenty minutes after injection of a receptor saturating dose of T3 into euthyroid rats, apoA-I gene transcription increases, reaches a maximum of 179% of control at 3.5 hours, and remains elevated for 48 hours. Levels of nuclear and cytoplasmic apoA-I mRNA increase at 1 hour and 2 hours, respectively, and exceed the levels expected from enhanced transcription more than twofold at 24 h. Daily administration of 35 ug T3/1OO g body weight s.c. for 1 week increases the abundance of nuclear and cytoplasmic apoA-I mRNA more than threefold, but reduces the transcription of the apoA-I gene to 42% of control injected animals. Thus, thyorid hormone rapidly stimulates apoA-I gene transcription, but posttranscriptional events enhancing the stability of nuclear apoA-I RNA contribute to the acute effect of T3 on apoA-I mRNA levels. In chronic hyperthyroidism, stabilization of nuclear apoA-I RNA precursors is the principal mechanism for enhanced apoA-I gene expression and may cause feedback inhibition of apoA-I gene transcription. Our studies also imply that in euthyroid rats the majority of nuclear apoA-I mRNA precursors is degraded. more...
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- 1990
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156. Peripheral infusion of rat bone marrow derived endothelial progenitor cells leads to homing in acute lung injury
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Wolfgang Hilbe, Eberhard Gunsilius, Daniela Colleselli, Gilbert Spizzo, Andreas Gschwendtner, Christian M. Kähler, Albrecht Wendel, Harald Niederegger, Jürg Hamacher, Jutta Wechselberger, Eva-Maria Boneberg, and Josef R. Patsch more...
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Pulmonary and Respiratory Medicine ,Pathology ,medicine.medical_specialty ,Neovascularization, Physiologic ,Bone Marrow Cells ,Lung injury ,Mesenchymal Stem Cell Transplantation ,Rats, Sprague-Dawley ,Vasculogenesis ,ddc:570 ,medicine ,Animals ,Infusions, Parenteral ,Progenitor cell ,Bone Marrow Transplantation ,lcsh:RC705-779 ,Matrigel ,Respiratory Distress Syndrome ,business.industry ,Research ,Mesenchymal Stem Cells ,lcsh:Diseases of the respiratory system ,Rats ,Transplantation ,medicine.anatomical_structure ,embryonic structures ,cardiovascular system ,Female ,Bone marrow ,Wound healing ,business ,Homing (hematopoietic) ,circulatory and respiratory physiology - Abstract
BackgroundBone marrow-derived progenitors for both epithelial and endothelial cells have been observed in the lung. Besides mature endothelial cells (EC) that compose the adult vasculature, endothelial progenitor cells (EPC) are supposed to be released from the bone marrow into the peripheral blood after stimulation by distinct inflammatory injuries. Homing of ex vivo generated bone marrow-derived EPC into the injured lung has not been investigated so far. We therefore tested the hypothesis whether homing of EPC in damaged lung tissue occurs after intravenous administration.MethodsEx vivo generated, characterized and cultivated rat bone marrow-derived EPC were investigated for proliferation and vasculogenic properties in vitro. EPC were tested for their homing in a left-sided rat lung transplant model mimicking a severe acute lung injury. EPC were transplanted into the host animal by peripheral administration into the femoral vein (106 cells). Rats were sacrificed 1, 4 or 9 days after lung transplantation and homing of EPC was evaluated by fluorescence microscopy. EPC were tested further for their involvement in vasculogenesis processes occurring in subcutaneously applied Matrigel in transplanted animals.ResultsWe demonstrate the integration of intravenously injected EPC into the tissue of the transplanted left lung suffering from acute lung injury. EPC were localized in vessel walls as well as in destructed lung tissue. Virtually no cells were found in the right lung or in other organs. However, few EPC were found in subcutaneous Matrigel in transplanted rats.ConclusionTransplanted EPC may play an important role in reestablishing the endothelial integrity in vessels after severe injury or at inflamatory sites and might further contribute to vascular repair or wound healing processes in severely damaged tissue. Therapeutic applications of EPC transplantation may ensue. more...
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- 2007
157. Generalized Large Vessel Arteritis Visualized by 18 Fluorodeoxyglucose-Positron Emission Tomography
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R. W. Gasser, Hartmut Glossmann, Michael Schirmer, Roy Moncayo, Josef R. Patsch, H Erler, Eveline Donnemiller, and Martin Wenger
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Hyperparathyroidism ,medicine.medical_specialty ,endocrine system diseases ,medicine.diagnostic_test ,business.industry ,Thyroid ,Colonoscopy ,medicine.disease ,Scintigraphy ,medicine.anatomical_structure ,Positron emission tomography ,Physiology (medical) ,Erythrocyte sedimentation rate ,medicine ,Radiology ,Arteritis ,Bone marrow ,Cardiology and Cardiovascular Medicine ,business - Abstract
This previously healthy 81-year-old man with recurrent fever up to 38.8°C and an erythrocyte sedimentation rate of more than 85 mm/h had no pain and did not respond to empirical treatment with antibiotics. Imaging by computerized tomography, thyroid and whole body 99mTc-MIBI scintigraphy (because of pre-diagnosed hyperparathyroidism), gastroscopy, colonoscopy, and bone marrow aspiration were … more...
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- 2003
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158. Wolfram syndrome: a clinical and molecular genetic analysis
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Philipp Eller, Monika Lechleitner, Bernhard Föger, Gerd Finkenstedt, Roland Gander, Teresa Sauper, and Josef R. Patsch
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Male ,medicine.medical_specialty ,Pituitary disorder ,Ataxia ,Wolfram syndrome ,DNA Mutational Analysis ,Biology ,Electronic Letter ,Genetic Heterogeneity ,Atrophy ,Internal medicine ,otorhinolaryngologic diseases ,Genetics ,medicine ,Humans ,RNA, Messenger ,Genetics (clinical) ,Polymorphism, Genetic ,Base Sequence ,Genetic heterogeneity ,Wolfram Syndrome ,DNA ,medicine.disease ,Peripheral neuropathy ,Endocrinology ,Mutation ,Diabetes insipidus ,Female ,medicine.symptom ,Myoclonus - Abstract
Editor—Wolfram syndrome (OMIM 222300) is a progressive neurodegenerative disorder characterised by the association of juvenile, non-autoimmune, insulin dependent diabetes mellitus and optic atrophy. The physician D J Wolfram, who reported four cases in 1938, is credited with the first description.1 With the identification of other clinical features, Wolfram syndrome was also referred to as DIDMOAD syndrome (diabetesinsipidus, diabetes mellitus,optic atrophy and deafness). The initial manifestation of Wolfram syndrome is typically, but not invariably, insulin deficient diabetes mellitus at a median age of 6 years, followed by optic atrophy at 11 years.2 In the second decade, many patients develop central diabetes insipidus and sensorineural deafness. Additional, but less frequent neurological and endocrinological abnormalities are atonic bladder, ataxia, myoclonus, peripheral neuropathy, hypogonadism, and a relatively high incidence of depression and psychotic behaviour.3-5 Death occurs between 25 and 49 years (median 30 years). The prevalence of Wolfram syndrome was estimated at 1/100 000 in a North American population and 1/770 000 in the United Kingdom.2 6 Family studies indicate autosomal recessive inheritance. Genetic linkage analysis has localised Wolfram syndrome to the short arm of chromosome 4 (4p16),7 8 and the primary genetic defect of the syndrome was attributed to the WFS1 gene, which consists of eight exons encoding a 890 amino acid polypeptide with an apparent molecular weight of 100 kDa.9 10 Hydrophobicity analysis suggested a transmembrane protein comprising three structural domains: a hydrophilic amino terminus separated from a hydrophilic carboxy-terminal tail by a hydrophobic region containing nine predicted transmembrane segments. Homologous genes in Mus musculus , Rattus norvegicus , and Drosophila melanogaster have been described (GenBank AF084482/AJ011971, AF136378; FlyBase FBgn0039003). The majority of patients with Wolfram syndrome carry loss of function mutations … more...
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- 2001
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159. Interferon-alpha decreases leptin synthesis in murine adipocytes
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Susanne Kaser, Arthur Kaser, Wolfgang Vogel, Herbert Tilg, and Josef R. Patsch
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medicine.medical_specialty ,Endocrinology ,Hepatology ,Chemistry ,Internal medicine ,Leptin ,medicine ,Gastroenterology ,Alpha interferon - Published
- 2001
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160. IFN-alpha therapy increases circulating leptin levels in hepatitis C patients: A possible link to IFN-induced cachexia
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Susanne Kaser, Wolfgang Vogel, Arthur Kaser, Herbert Tilg, and Josef R. Patsch
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Ifn alpha ,medicine.medical_specialty ,Endocrinology ,Hepatology ,business.industry ,Leptin ,Internal medicine ,Gastroenterology ,medicine ,Hepatitis C ,medicine.disease ,business ,Cachexia - Published
- 2000
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161. 4.P.156 Oral intake of diatomaceous earth lowers blood cholesterol
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Dietmar Fuchs, A. Hausen, Elmar Jarosch, B. Widner, E. Artner-Dworzak, Karl P. Pfeiffer, Josef R. Patsch, Monika Lechleitner, and Helmut Wachter
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Chemistry ,Blood cholesterol ,Earth (chemistry) ,Food science ,Cardiology and Cardiovascular Medicine - Published
- 1997
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162. Unusual presentation of cholesteryl ester storage disease (CESD): report on a new family
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Alfred Doblinger, B. Fo¨ger, Andreas Ritsch, F. Hoppichler, W. Sperl, Y. Shin, Josef R. Patsch, and Monika Lechleitner
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medicine.medical_specialty ,Endocrinology ,Cholesteryl ester storage disease ,business.industry ,Internal medicine ,medicine ,Presentation (obstetrics) ,Cardiology and Cardiovascular Medicine ,medicine.disease ,business - Published
- 1994
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163. Treatment of primary mixed hyperlipidemia with etophylline clofibrate: effects on lipoprotein composition, lipoprotein-modifying enzymes and postprandial lipoprotein metabolism
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Thomas Hopferwieser, G. Tro¨binger, B. Fo¨ger, Karl P. Pfeiffer, Josef R. Patsch, Andreas Ritsch, and Monika Lechleitner
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chemistry.chemical_classification ,medicine.medical_specialty ,Very low-density lipoprotein ,Low-density lipoprotein receptor-related protein 8 ,Primary mixed hyperlipidemia ,Enzyme ,Endocrinology ,Postprandial ,chemistry ,Internal medicine ,medicine ,Composition (visual arts) ,Lipoprotein metabolism ,Cardiology and Cardiovascular Medicine ,Lipoprotein - Published
- 1994
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164. 89 TANGIER DISEASE IN A BLACKMALE: AN UNUSUAL CLINICAL PRESENTATION
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Jane F. Donat, B Fahey, W. Strobl, Josef R. Patsch, Warren D. Lo, W. Patsch, Antonio M. Gotto, and Howard R. Sloan
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Apolipoprotein E ,medicine.medical_specialty ,Apolipoprotein B ,biology ,business.industry ,Interstitial keratitis ,nutritional and metabolic diseases ,medicine.disease ,Peripheral neuropathy ,Endocrinology ,Tangier disease ,Internal medicine ,Pediatrics, Perinatology and Child Health ,medicine ,biology.protein ,lipids (amino acids, peptides, and proteins) ,business ,Nerve conduction ,Lumbosacral plexopathy ,Lipoprotein - Abstract
Tangier disease is a rare autosomal recessive disorder characterized by very low plasma apolipoprotein (apo) A-I and high-density lipoprotein (HDL), by tissue accuiulation of cholesteryl esters, and by peripheral neuropathy. The disease has been describedin Caucasians only. We report on a case of Tangier disease in a black boy. He presented with symptoms of progressive lumbosacral plexopathy. Electromyography and nerve conduction studies, however, indicated an unusal form of diffuse sensorimotor polyneuropathy. Additicnally, deep interstitial keratitis of the cornea was diagnosed. This feature has not been previously reported in Tangier disease. Plasma cholesterol was reduced to 25ng/dl, HDL-cholesterol and apoA-I to more...
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- 1990
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165. Effect of cholesterol feeding on the distribution of plasma lipoproteins and on the metabolism of apolipoprotein E in the rabbit
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R. I. Roth, Josef R. Patsch, John W. Gaubatz, and Antonio M. Gotto
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Apolipoprotein E ,medicine.medical_specialty ,Very low-density lipoprotein ,Chemistry ,Catabolism ,Cholesterol ,Cell Biology ,Metabolism ,QD415-436 ,Biochemistry ,Apolipoproteins E ,chemistry.chemical_compound ,Endocrinology ,Internal medicine ,medicine ,Centrifugation ,lipids (amino acids, peptides, and proteins) ,Lipoprotein - Abstract
Changes in lipoprotein distribution and in apolipoprotein E metabolism were studied in rabbits fed a diet containing 1% cholesterol. Lipoprotein distribution was monitored by rate zonal ultracentrifugation, gel filtration chromatography, and electrophoretic techniques. Normolipidemic rabbit plasma contained VLDL, IDL, LDL, and HDL. Within 1 week on the 1% cholesterol diet, the d less than 1.006 g/ml material was greatly elevated, and the lipoproteins of higher density (LDL and HDL) decreased below levels of detection. Cholesteremic d less than 1.006 g/ml material was cholesteryl ester-rich, triglyceride-poor, and contained particles of Sf 20 to greater than 400. Upon diet normalization, the LDL and HDL reappeared within 2-4 weeks accompanied by a decrease in the d less than 1.006 g/ml material. The metabolism of apoE was studied by injecting purified and 125I-labeled apoE into rabbits and following the clearance of the tracer. ApoE in the normolipemic rabbit demonstrated a fractional catabolic rate (FCR) of 0.132 hr-1 and a half-life (t1/2) of 10.3 hr. ApoE in the hypercholesterolemic rabbit demonstrated an FCR of 0.055 hr-1 and a t1/2 of 49.5 hr. ApoE concentrations in the plasma as estimated by electroimmunoassay were 19.5 mg/dl in the control rabbit and 199 mg/dl in the hypercholesterolemic rabbit. From these data, absolute synthetic rates of 20.3 mg/kg per day and 86.1 mg/kg per day were calculated for the control and the hypercholesterolemic rabbit, respectively. We conclude that the cholesterol-supplemented diet caused pronounced elevation of apoE in the plasma due to overproduction of the protein. more...
- Published
- 1983
166. Genetic susceptibility and resistance to diet-induced atherosclerosis and hyperlipoproteinemia
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Josef R. Patsch, Joel D. Morrisett, Surjit K. Datta, Han-Seob Kim, and John J. Trentin
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Apolipoprotein E ,Hyperlipoproteinemias ,medicine.medical_specialty ,Normal diet ,Arteriosclerosis ,Alpha (ethology) ,Biology ,Mice ,chemistry.chemical_compound ,Apolipoproteins E ,Internal medicine ,medicine ,Genetic predisposition ,Animals ,Apolipoproteins A ,Triglycerides ,Aortic atherosclerosis ,Strain (chemistry) ,Cholesterol ,Body Weight ,Sinus of Valsalva ,Lipoproteins, LDL ,Mice, Inbred C57BL ,Apolipoproteins ,Endocrinology ,chemistry ,Immunology ,Mice, Inbred CBA ,Diet, Atherogenic ,Female ,lipids (amino acids, peptides, and proteins) ,Disease Susceptibility ,Lipoproteins, HDL ,Cardiology and Cardiovascular Medicine ,Lipoprotein - Abstract
To test the hypothesis that genetic susceptibility or resistance to diet-induced atherosclerosis is correlated with serum levels of specific lipids, lipoproteins, or apoproteins, male mice of a genetically susceptible and a genetically resistant strain were fed either a normal or an atherogenic diet. After 20 weeks on a normal diet, neither the resistant nor the susceptible strain mice had atherosclerosis; resistant strain mice had serum cholesterol of 66 +/- 11 while the susceptible strain mice had 90 +/- 1 mg/dl serum cholesterol, and lipoproteins were dominated by a single alpha-migrating HDL. After 20 weeks on an atherogenic diet, resistant strain mice had 185 +/- 55 mg/dl cholesterol, their lipoproteins remained dominated by alpha-migrating HDL, and two of eight mice had mild atherosclerotic lesions; susceptible strain mice had 510 +/- 94 mg/dl cholesterol, multiple alpha- and pre-beta-migrating lipoprotein species, and all 13 had advanced aortic atherosclerosis. The resistant strain mice had an apolipoprotein E/total lipoprotein protein ratio of 0.42 on the normal diet and 0.53 on the atherogenic diet, while the susceptible strain mice had the significantly lower ratios of 0.07 and 0.31, respectively. These data indicate that genetic resistance to diet-induced aortic atherosclerosis in mice is correlated with capacity to prevent large increases in serum cholesterol, to suppress abnormal alpha- and pre-beta-migrating lipoproteins, and to maintain elevated serum apolipoprotein E/total lipoprotein protein ratios. Our data do not preclude the possibility of additional gene control at the level of arterial end organ response. more...
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- 1982
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167. Isolation and partial characterization of two abnormal human plasma lipoproteins: LP-X1 and LP-X2
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Josef R. Patsch, Wolfgang Patsch, Herbert Braunsteiner, and S. Sailer
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Adult ,Immunodiffusion ,medicine.medical_specialty ,Very low-density lipoprotein ,Apolipoprotein B ,Biliary Tract Diseases ,Lipoproteins ,Phospholipid ,Jaundice ,Blood lipids ,Biochemistry, Genetics and Molecular Biology (miscellaneous) ,chemistry.chemical_compound ,Internal medicine ,medicine ,Humans ,Aged ,Intermediate-density lipoprotein ,biology ,Chemistry ,Liver Diseases ,Middle Aged ,Blood Protein Electrophoresis ,Ouchterlony double immunodiffusion ,Molecular Weight ,Endocrinology ,biology.protein ,lipids (amino acids, peptides, and proteins) ,Lipoprotein - Abstract
Two abnormal lipoproteins (LP-X1 and LP-X2) rich in free cholesterol and phospholipid have been isolated from the plasma of nine different patients with obstructive jaundice. As isolated, both lipoproteins were devoid of low density lipoproteins as judged by agar electrophoresis. In addition, they were free of apoB as judged by double immunodiffusion. However, LP-X1 exhibited a higher phospholipid to protein ratio and a lower hydrated density than LP-X2. The levels of LP-X1 and LP-X2 in plasma were measured in three patients studied for 14 days after corrective surgery for obstructive liver disease. The level of both these abnormal lipoproteins decreased after surgery until the twelfth day when they were completely absent from the plasma of these patients. The rates of this decrease for the two particles are significantly different. These differences in metabolic, chemical, and physical properties of LP-X1 and LP-X2, establish their identity as two distinct and unique lipoprotein particles. more...
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- 1976
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168. Comparison of the effects of halofenate (MK-185) and clofibrate on plasma lipid and uric acid concentration in hyperlipoproteinemic patients
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Lisch Hj, Herbert Braunsteiner, Josef R. Patsch, and S. Sailer
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Adult ,Electrophoresis ,medicine.medical_specialty ,Hyperlipidemias ,chemistry.chemical_compound ,HALOFENATE ,Internal medicine ,Hyperlipidemia ,Plasma lipids ,medicine ,Humans ,Clofibrate ,Triglycerides ,Aged ,Triglyceride ,Cholesterol ,Sepharose ,Serum uric acid ,Middle Aged ,medicine.disease ,Lipids ,Glycolates ,Uric Acid ,Endocrinology ,chemistry ,Uric acid ,Cardiology and Cardiovascular Medicine ,Halofenate ,medicine.drug - Abstract
The plasma lipid and serum uric acid lowering effect of halofenate (MK-185, 1 g/day) was compared with the action of clofibrate (2 g/day) in a double-blind 1-yr study in 23 patients with Type 2, 3, 4, and 5 hyperlipoproteinemia. It could be demonstrated that clofibrate decreased the plasma cholesterol concentration significantly to 75% and the triglyceride concentration to 49% of the placebo period level. Halofenate produced no consistent effect on plasma cholesterol but ther was an average reduction of the plasma triglyceride concentration to 84%, which was, however, not significant. If only the Type 4 patients were taken into account, a mean significant decrease to 47% of the triglyceride concentration was observed during the second 24-week period of treatment. In contrast, halofenate lowered the serum uric acid concentration significatnly to 77% of the placebo period level, whereas the decreasing action of clofibrate was weaker (88%) and of lesser significance. more...
- Published
- 1975
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169. Isolation of subfractions of human very low density lipoproteins by zonal ultracentrifugation
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S Sailer, Josef R. Patsch, H Braunsteiner, Gert M. Kostner, and Wolfgang Patsch
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Very low-density lipoprotein ,Chromatography ,Cholesterol ,Size-exclusion chromatography ,Analytical chemistry ,Fraction (chemistry) ,Cell Biology ,Biochemistry ,Analytical Ultracentrifugation ,chemistry.chemical_compound ,chemistry ,lipids (amino acids, peptides, and proteins) ,Centrifugation ,Ultracentrifuge ,Inverse correlation ,Molecular Biology - Abstract
Very low density lipoproteins (VLDL) have been isolated and subfractionated on the basis of their differing flotation rates. The procedure consists of a single 45-min zonal ultracentrifugation step using a linear density gradient of d = 1.00 to 1.15 g/ml. Appropriate fractions of the zonal rotor effluent containing the entire VLDL spectrum were characterized by analytical ultracentrifugation, gel filtration chromatography, and complete chemical analysis. Flotation rates of VLDL subspecies from hypertriglyceridemic and normolipemic plasmas correlated directly with their Stokes radii and triglyceride content and inversely with their proportion of cholesterol, cholesteryl esters, phospholipids, and total protein. There was also an inverse correlation of flotation rate with the fraction of tetramethylurea-insoluble protein. This procedure provides a reliable methodology for a rapid isolation of VLDL subfractions and the accurate determination of their flotation rates. more...
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- 1978
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170. Lipoprotein-X: a substrate for lecithin: cholesterol acyltransferase
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Joel D. Morrisett, Josef R. Patsch, Anne K. Soutar, Louis C. Smith, and Antonio M. Gotto
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food.ingredient ,Clinical Biochemistry ,Sterol O-acyltransferase ,In Vitro Techniques ,Tritium ,Biochemistry ,Lecithin ,Phosphatidylcholine-Sterol O-Acyltransferase ,chemistry.chemical_compound ,food ,Phosphatidylcholine ,Humans ,Electrophoresis, Agar Gel ,Intermediate-density lipoprotein ,Lipoprotein-X ,Cholestasis ,Chromatography ,Cholesterol ,Reverse cholesterol transport ,General Medicine ,Clinical Enzyme Tests ,Lipoproteins, LDL ,chemistry ,Isotope Labeling ,Chromatography, Gel ,lipids (amino acids, peptides, and proteins) ,Cholesterol Esters ,Acyltransferases ,Lipoprotein - Abstract
The action of lecithin:cholesterol acyltransferase (LCAT) was studied on an abnormal lipoprotein (LP-X) rich in phosphatidylcholine and cholesterol from the plasma of patients with obstructive liver disease. 60 mg LP-X isolated free of other lipoproteins and subsequently labelled with 3H-cholesterol were incubated with 1 mg highly purified enzyme in the presence of albumin. After 45 h at 37 degrees C, the incubation mixture was subjected to zonal ultracentrifugation. 3H-cholesterol and 3H-cholesteryl esters were quantified in each fraction of the zonal gradient. More than 95% of the lipoproteins in this mixture banded in the density range of LP-X with no change in size distribution, but did contain 593 nmoles of newly formed cholesteryl esters. Agarose electrophoresis revealed an alpha-migrating band in addition to the original beta-band. Also on agar, the typically cathode migrating LP-X was changed to anode moving material. These studies indicate that LP-X can serve as a substrate for LCAT. more...
- Published
- 1977
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171. The Effects of Lipid Lowering Drugs on the Concentration and Composition of Plasma Lipoproteins in Hyperlipoproteinemias
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Josef R. Patsch, Yuichiro Goto, Antonio M. Gotto, and Tsutomu Hara
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Plasma lipoprotein ,Very low-density lipoprotein ,medicine.medical_specialty ,Endocrinology ,Chemistry ,Internal medicine ,medicine ,Composition (visual arts) ,Lipid lowering - Published
- 1979
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172. Formation of high density lipoprotein2-like particles during lipolysis of very low density lipoproteins in vitro
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S. Eisenberg, Antonio M. Gotto, T Olivercrona, and Josef R. Patsch
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Intermediate-density lipoprotein ,Very low-density lipoprotein ,Lipoprotein lipase ,Multidisciplinary ,Cholesterol ,Phospholipid ,Lipoproteins, VLDL ,Molecular Weight ,Lipoprotein Lipase ,chemistry.chemical_compound ,Apolipoproteins ,Biochemistry ,chemistry ,In vivo ,Biophysics ,Humans ,Lipolysis ,lipids (amino acids, peptides, and proteins) ,Ultracentrifuge ,Lipoproteins, HDL ,Research Article - Abstract
The effects of lipolysis of human plasma very low density lipoprotein (VLDL) on the structure and composition of high density lipoproteins (HDL) have been investigated. Lipolysis was performed in a controlled system in vitro containing VLDL (d less than 1.006 g/ml) and HDL3 (d = 1.125-1.210 g/ml) from human plasma and lipoprotein lipase (EC 3.1.1.34) purified from bovine milk. Lipolysis of VLDL caused profound changes in HDL3. Protein, phospholipid, and cholesterol liberated from VLDL during its lipolysis were transferred to the HDL3 particles. As a consequence of this in vitro transfer, the chemical composition and biophysical properties of HDL3 were substantially altered. The newly formed particles exhibited a flotation rate (F01.20) of 6.7 and a hydrated density of 1.110 g/ml. The chemical composition closely resembled that of native HDL2, and their size was slightly larger than that of the precursor HDL3. When HDL3 and postlipolysis HDL2 were subjected to ultracentrifugation under flotation velocity and equilibrium conditions, both proved to be stable particles. These results, when extrapolated to in vivo conditions, suggest an important metabolic relationship between the levels of circulating VLDL and HDL2 in plasma. This relationship now permits a reasonable explanation for numerous in vivo observations in which the levels of VLDL and HDL2 change reciprocally. more...
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- 1978
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173. Lipoprotein-X: proton and phosphorus-31 nuclear magnetic resonance studies on native, reconstituted, and model systems
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J. D. Morrisett, James R. Brainard, Josef R. Patsch, Antonio M. Gotto, and Eugene H. Cordes
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Magnetic Resonance Spectroscopy ,Proton ,Protein Conformation ,Chemistry ,Vesicle ,Bilayer ,Temperature ,Resonance ,Lipoprotein-X ,Biochemistry ,Lipoproteins, LDL ,Paramagnetism ,Cholesterol ,Nuclear magnetic resonance ,Permeability (electromagnetism) ,Humans ,lipids (amino acids, peptides, and proteins) ,Phosphorus-31 NMR spectroscopy ,Titration ,Phospholipids ,Protein Binding - Abstract
LP-X, a lipoprotein present in the low-density range (d 1.006--1.063 g/mL) of cholestatic human plasma, has been studied with its normal counterpart (LDL) by 1H and 31P nuclear magnetic resonance. The 220-MHz 1H spectrum of LP-X contains four major lines: the choline CH2N and N+(CH3)3 resonances and the cholesteryl--acyl CH2 and CH3 envelopes. The widths of these four lines at 37 degrees C are approximately 24, 10, 124, and 48 Hz, respectively. The latter two line widths are much greater than the corresponding ones of LDL (28 and 20 Hz), suggesting the much more restricted motion of acyl chains and/or cholesteryl rings in LP-X. This difference persists over the temperature range 15--52.5 degrees C. The microscopic fluidity of LP-X and LDL was compared by titration with 2,2,6,6-tetramethylpiperidinyl-1-oxy (Tempo), a paramagnetic amphiphile which distributes between the bulk aqueous phase and the fluid lipid phase of lipoproteins. Tempo is much less effective in broadening the 1H resonances of LP-X than of LDL, indicating the lower permeability/fluidity of the former. The 40.5-MHz 31P spectrum of LP-X consists of a single resonance whose line width is approximately 20 Hz and whose spin--lattice relaxation time is 2.23 +/- 0.15 s. Titration of LP-X with Pr3+ ions splits this resonance into two lines, one remaining at the chemical shift of the original resonance and the other paramagnetically shifting downfield. The ratio of integrated areas for these two lines was 1:1.72. Titration of phosphatidylcholine--cholesterol vesicles alone, vesicles containing apolipoprotein-C and albumin, or vesicles containing apolipoprotein-X gave results similar to those obtained with native LP-X, suggesting the presence of a single bilayer structure in all of these systems. more...
- Published
- 1980
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174. Lipoprotein-X: carbon-13 nuclear magnetic resonance studies on native, reconstituted, and model systems
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James R. Brainard, Antonio M. Gotto, James A. Hamilton, Eugene H. Cordes, Josef R. Patsch, and J. D. Morrisett
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Lipoprotein-X ,Magnetic Resonance Spectroscopy ,Protein Conformation ,Chemistry ,Cholesterol ,Bilayer ,Vesicle ,Glyceride ,Phospholipid ,Carbon-13 NMR ,Biochemistry ,Centrifugation, Zonal ,Lipoproteins, LDL ,chemistry.chemical_compound ,Nuclear magnetic resonance ,Humans ,lipids (amino acids, peptides, and proteins) ,Lipoproteins, HDL ,Phospholipids ,Lipoprotein - Abstract
Lipoprotein-X (LP-X), a lipoprotein isolated from human cholestatic plasma by ethanol--acetate precipitation and zonal ultracentrifugation, has been studied by 13C NMR at 67.9 MHz. Spectra of LP-X and its three subfractions are markedly different from those of normal human high-density lipoprotein3 (HDL3) or low-density lipoprotein (LDL). Spectra of LP-X are characterized by the presence of unusually broad resonance lines, especially those attributable to C6 of unesterified cholesterol (160--260 Hz) and to C beta of phospholipid glyceride (240--290 Hz). In contrast, the CH2O, CH2N, and N(CH3)3 choline resonances have line widths comparable to those of normal LDL and HDL3. For the subfraction LP-X1, spin--lattice relaxation times (T1) of the fatty acyl olefin resonances at 129.8 and 128.0 ppm and of the unesterified cholesterol C6 at 120.1 ppm were measured to be 675, 766, and 162 ms, respectively. These times are comparable to those measured for the corresponding resonances in single bilayer vesicles whose lipid composition approximates that of LP-X. The three LP-X subfractions isolated by zonal ultracentrifugation gave spectra which are identical, within experimental error, as judged qualitatively from their appearance and quantitatively from the line widths of selected resonances. In addition, 13C NMR spectra of sonicated total LP-X lipids are similar to spectra of the intact native lipoprotein. This study suggests (a) that motions of lipids in LP-X as probed by 13C NMR are similar to the motions of lipids found in model vesicular systems, (b) that the motions of the cholesterol rings and phospholipid fatty acyl chains are significantly more restricted in LP-X than in HDL3 and LDL, and (c) that the motions of the phosphoryl moieties in all three systems are similar. more...
- Published
- 1980
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175. Very low density lipoprotein. Removal of Apolipoproteins C-II and C-III-1 during lipolysis in vitro
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Thomas Olivecrona, Josef R. Patsch, James T. Sparrow, S. Eisenberg, and Antonio M. Gotto
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Lipoprotein lipase ,Very low-density lipoprotein ,Chromatography ,Triglyceride ,Apolipoprotein B ,biology ,nutritional and metabolic diseases ,Cell Biology ,Biochemistry ,chemistry.chemical_compound ,High-density lipoprotein ,chemistry ,biology.protein ,Lipolysis ,Agarose ,lipids (amino acids, peptides, and proteins) ,Centrifugation ,Molecular Biology - Abstract
In this study we have investigated the effects of very low density lipoprotein (VLDL) lipolysis on the removal of radiolabeled apolipoprotein C-II and apolipoprotein C-III-1 from in vitro lipolyzed lipoproteins. Lipolysis was carried out in vitro using lipoprotein lipase purified from bovine milk, and mixtures with or without plasma. Lipoproteins were isolated by ultracentrifugation and by gel filtration. Labeled apo-C-II and apo-C-III-1 distributed among plasma lipoproteins, predominantly VLDL and high density lipoprotein (HDL). Lipolysis induced transfer of apo-C-II and apo-C-III-1 from VLDL to HDL. The transfer was proportional to the extent of triglyceride hydrolysis, and similar for the two apoproteins. The apo-C-II/apo-C-III-1 radioactivity ratio did not change in either VLDL or the fraction of d greater than 1.006 g/ml during the progression of the lipolytic process. Similar observations were recorded while using plasma-devoid lipolytic systems. Gel filtration of incubation mixtures, on 6% agarose, revealed that the removal of labeled apo-C molecules from VLDL is not a consequence of either centrifugation or high salt concentration. These results suggest that there is no preferential removal of apo-C-II or apo-C-III-1 from lipolyzed VLDL particles. They further indicate that the ratio of apo-C-II to apo-C-III-1 does not regulate the extent of lipolysis of different VLDL particles, at least in VLDL isolated from normolipidemic humans. more...
- Published
- 1979
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176. Studies on the degradation of lipoprotein-X
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F. Kunz, Josef R. Patsch, Herbert Braunsteiner, S. Sailer, and Wolfgang Patsch
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Male ,Time Factors ,food.ingredient ,Lipoproteins ,Clinical Biochemistry ,Sterol O-acyltransferase ,In Vitro Techniques ,Biochemistry ,Lecithin ,Phosphatidylcholine-Sterol O-Acyltransferase ,chemistry.chemical_compound ,food ,Humans ,Incubation ,Lipoprotein-X ,Cholestasis ,Chromatography ,Cholesterol ,Reverse cholesterol transport ,General Medicine ,Lysophosphatidylcholine ,chemistry ,lipids (amino acids, peptides, and proteins) ,Cholesterol Esters ,Lipoproteins, HDL ,Lipoprotein - Abstract
Three patients suffering from prolonged obstructive jaundice were studied after surgical removal of biliary obstruction. Four days after surgery the initial cholesterol esterification rate in the plasma rose from very low activities to values three to four times higher than those found in normal subjects. During this time lipoprotein-X decreased in concentration. The initial cholesterol esterification rate returned to normal values when plasma lipids and lipoproteins reached normal levels. During incubation of normal plasma with lipoprotein-X, changes in the lipid composition of the incubation mixture were observed which appeared to be catalysed by lecithin:cholesterol acyltransferase. The formation of esterified cholesterol and lysophosphatidylcholine exceeded that of control experiments when lipoprotein-X was replaced by buffer solution in the incubation mixture. Lipoprotein-X disappeared as monitored by electrophoresis on agar and measured after zonal ultracentrifugation, and lipoproteins with flotation behaviour of high density lipoprotein2, enriched in polar lipids, appeared. When plasma was incubated separately with lipoprotein-X1 and lipoprotein-X2in vitro, the T1/2 of these lipoproteins were 24 h and 9 1/2 h, respectively. Addition of lipoprotein-X2 to normal plasma resulted in an increased initial cholesterol esterification rate with a sigmoidal response curve. Lipoprotein-X1 increased the initial cholesterol esterification rate also but to a lesser extent. Our findings indicate that incubation of normal plasma with lipoprotein-X results in the disappearance of this abnormal lipoprotein and the appearance of a high density lipoprotein2-like particle mediated by enzymic cholesterol acyltransfer. more...
- Published
- 1977
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177. Dynamic properties of human high density lipoprotein apoproteins
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Antonio M. Gotto, O. D. Taunton, James Shepherd, Christopher J. Packard, and Josef R. Patsch
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Very low-density lipoprotein ,nutritional and metabolic diseases ,QD415-436 ,Cell Biology ,Metabolism ,Biochemistry ,In vitro ,chemistry.chemical_compound ,Endocrinology ,High-density lipoprotein ,chemistry ,High density lipoprotein subfraction ,polycyclic compounds ,lipids (amino acids, peptides, and proteins) ,Specific activity ,Incubation - Abstract
This study was designed to identify a method for the measurement of human high density lipoprotein subfraction (HDL2 and HDL3) metabolism. Apolipoproteins A-I, A-II, and C, the major HDL apoproteins, were radioiodinated and incorporated individually into HDL2 and HDL3 in vitro. Using a double label technique, the turnover of apoA-I in HDL2 and HDL3 was measured simultaneously in a normal male. The apoprotein exchanged rapidly between the two subfractions, evidenced by equilibration of their apoA-I specific activity. Radiolabeled apoA-II, incorporated into the subfractions, showed a similar exchange in vitro. Incubation of 131I-labeled very low density lipoproteins (VLDL) with HDL or its subfractions resulted in transfer of C proteins from VLDL to the HDL moiety. The extent of transfer was dependent on the HDL subfraction present; 50% of the VLDL apoC was transferred to HDL3, while the transfer to total HDL and HDL2 was 69% and 78%, respectively. ApoC also exchanged between HDL2 and HDL3, again showing a preference for the former and suggesting a primary metabolic relationship between VLDL and HDL2. Overall, the study indicates that apoA-I, apoA-II, and the C proteins exist in equilibrium between HDL2 and HDL3. This phenomenon precludes their use as probes for HDL subfraction metabolism in humans. more...
- Published
- 1978
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178. 3 Postprandial lipaemia
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Josef R. Patsch
- Subjects
medicine.medical_specialty ,Endocrinology ,Postprandial ,Chemistry ,Internal medicine ,medicine ,Biochemistry - Published
- 1987
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179. Effects of insulin on lipoprotein secretion in rat hepatocyte cultures. The role of the insulin receptor
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Wolfgang Patsch, Antonio M. Gotto, and Josef R. Patsch
- Subjects
medicine.medical_specialty ,biology ,Apolipoprotein B ,Insulin ,medicine.medical_treatment ,Cell Biology ,Biochemistry ,Apolipoproteins E ,Insulin receptor ,Endocrinology ,Internal medicine ,Insulin receptor substrate ,biology.protein ,medicine ,Receptor ,Molecular Biology ,Insulin-like growth factor 1 receptor ,Lipoprotein - Abstract
Insulin inhibits the secretion of lipoprotein components such as triglyceride, phospholipid, and apolipoproteins B and E in primary rat hepatocyte cultures. The aim of this study was to determine whether these hormonal effects are related to the interaction of insulin with its receptor on the surface of cultured hepatocytes. Half-maximal inhibition of secretion of apolipoprotein E and triglyceride occurred at 6 ng/ml porcine insulin, equivalent to a 20% receptor occupancy. When compared to porcine insulin, both guinea pig insulin and desoctapeptide insulin were 60 times less inhibitory on triglyceride and apolipoprotein secretion. These analogs were also 60 times less effective in competing with porcine 125I-insulin for receptor binding. Anti-insulin receptor IgG inhibited binding of porcine insulin to cells in a dose-dependent fashion. However, similar to the hormone itself, it reduced the secretion of triglyceride and apolipoproteins E and B. Preincubation of cells with 200 ng/ml porcine insulin for 15 h caused a 2.5-fold reduction of surface receptor number. These cells were less sensitive to the inhibitory effect of porcine insulin on secretion of triglyceride and apolipoproteins B and E. We conclude that the effects of insulin on lipoprotein processing by hepatocytes in culture are receptor-mediated, can be imitated by antibodies, to the insulin receptor, and are subject to control by receptor down-regulation. more...
- Published
- 1986
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180. Prevention of Perinatal Morbidity by Tight Metabolic Control in Gestational Diabetes Mellitus
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H.-J. Lisch, Alfred Bichler, Christoph Breier, Josef R. Patsch, Herbert Braunsteiner, H. Drexel, and S. Sailer
- Subjects
Blood Glucose ,medicine.medical_specialty ,endocrine system diseases ,Endocrinology, Diabetes and Metabolism ,medicine.medical_treatment ,Birth weight ,Pregnancy in Diabetics ,Hypoglycemia ,Pre-Eclampsia ,Pregnancy ,Reference Values ,Diabetes mellitus ,Diet, Diabetic ,Internal Medicine ,medicine ,Birth Weight ,Humans ,Insulin ,Advanced and Specialized Nursing ,Glucose tolerance test ,medicine.diagnostic_test ,Obstetrics ,business.industry ,Infant, Newborn ,Pregnancy Outcome ,nutritional and metabolic diseases ,Glucose Tolerance Test ,medicine.disease ,female genital diseases and pregnancy complications ,Gestational diabetes ,Metabolic control analysis ,Female ,business - Abstract
In a prospective controlled trial, we studied the effect of tight metabolic control on the outcomes of 102 gestational diabetes mellitus (GDM) pregnancies compared with outcomes of 102 matched nondiabetic control pregnancies. Women with GDM were treated to achieve and maintain a blood glucose concentration of less than 130 mg/dl at 1 h after breakfast. Treatment consisted of a diet low in oligosaccharides and fat and, if necessary, once daily insulin. By the end of gestation, 88 of the 102 women with GDM received insulin at a mean dose of 18 U/day. Duration of insulin therapy ranged from 3 to 32 wk with a median of 11 wk. Perinatal outcome of GDM pregnancies under this management equaled that of control pregnancies. The full spectrum of excess morbidity from GDM was prevented, and normal distribution of birth weight and normal rates of macrosomia, dystrophy, hypoglycemia, hypocalcemia, hyperbilirubinemia, fetal acidosis, and low Apgar scores were achieved. No mortality was observed. In addition to the two main study groups, we also studied a third group of 24 women with GDM whose treatment lasted less than or equal to 5 wk due to late diagnosis. This suboptimally treated group demonstrated a significant (P less than .05) increase of macrosomia and umbilical artery acidosis compared with the well-treated GDM group. The study reported herein demonstrates that excess mortality and morbidity typically observed in GDM can be prevented by early institution of tight metabolic control, which required insulin in 86% of our patients. more...
- Published
- 1988
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181. Effects of clofibrate, nicotinic acid and diet on the properties of the plasma lipoproteins in a subject with type III hyperlipoproteinemia
- Author
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Richard L Jackson, Antonio M. Gotto, Daniel Yeshurun, and Josef R. Patsch
- Subjects
Male ,medicine.medical_specialty ,Very low-density lipoprotein ,Apolipoprotein B ,Familial dysbetalipoproteinemia ,Lipoproteins ,Hyperlipidemias ,Lipoproteins, VLDL ,chemistry.chemical_compound ,High-density lipoprotein ,Internal medicine ,Dietary Carbohydrates ,medicine ,Humans ,Clofibrate ,Triglycerides ,biology ,Triglyceride ,business.industry ,Cholesterol ,Nicotinic Acids ,General Medicine ,Middle Aged ,Carbohydrate ,medicine.disease ,Lipoproteins, LDL ,Endocrinology ,chemistry ,biology.protein ,lipids (amino acids, peptides, and proteins) ,Lipoproteins, HDL ,business ,medicine.drug - Abstract
A patient with familial type III hyperlipoproteinemia (HLP) was subjected to a clinical trial in which the effects of different diet regimens and drugs on all plasma lipoprotein density classes were studied. In this patient, whose plasma cholesterol and triglyceride were within normal limits under clofibrate treatment, medication was discontinued in favor of a diet enriched in carbohydrate. This management resulted, within eight days, in the development of a type III phenotype featuring all of the most widely used criteria typical for this form of lipid disorder. Very low density lipoproteins contained an increased amount of cholesterol and the "arginine-rich" apolipoprotein at both the beginning of the trial and at the eighth day. When the carbohydrate-enriched diet was replaced by a diet commonly used in type III hyperlipoproteinemia, the plasma cholesterol and triglyceride values were lowered to upper normal limits. However, after zonal ultracentrifugation, a lipoprotein profile typical for a type III subject without treatment was observed. Administration of either clofibrate or nicotinic acid to the type III diet resulted in a further decrease of the plasma levels of cholesterol and triglyceride. Zonal ultracentrifugation indicated that these decreases were caused by lowering the plasma concentrations of very low density, intermediate density, and low density lipoproteins. Furthermore, both drugs raised the two high density lipoprotein classes from their initially decreased levels to normal plasma values. These results suggest that drug and diet treatment of a type III hyperlipoproteinemic not only lowers the amount of very low, intermediate, and low density lipoproteins but also increases the high density lipoproteins which are considered protective against atherosclerosis. more...
- Published
- 1977
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182. Risk factors for coronary artery disease: a study comparing hypercholesterolaemia and hypertriglyceridaemia in angiographically characterized patients
- Author
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E. Knapp, Josef R. Patsch, Herbert Braunsteiner, V. Mühlberger, Ch. Breier, and H. Drexel
- Subjects
Adult ,Male ,medicine.medical_specialty ,Hypercholesterolemia ,Clinical Biochemistry ,Group ii ,Coronary Disease ,Biochemistry ,Coronary artery disease ,Lipoprotein lipase deficiency ,chemistry.chemical_compound ,Plasma cholesterol ,Risk Factors ,Internal medicine ,Humans ,Medicine ,Triglycerides ,Aged ,Hypertriglyceridemia ,Lipoprotein lipase ,business.industry ,Cholesterol ,Catabolism ,Angiocardiography ,General Medicine ,Middle Aged ,medicine.disease ,Lipids ,chemistry ,Cardiology ,lipids (amino acids, peptides, and proteins) ,business ,Lipoprotein lipase activity - Abstract
Fifty-two male patients undergoing coronary angiography were allocated to four groups each consisting of 13 subjects: group I had normal coronary arteries and patients in groups II-IV exhibited coronary artery disease. In group II, plasma cholesterol was below 250 mg dl-1 and triglycerides below 160 mg dl-1; in group III, cholesterol was above 270 mg dl-1 and triglycerides under 160 mg dl-1; and in group IV, cholesterol was under 270 mg dl-1 and triglycerides above 180mgdl-1. The hypertriglyceridaemic group IV had the highest coronary score. In addition, it had lowest lipoprotein lipase activity, lowest HDL-cholesterol and lowest high-density lipoproteins-2 (HDL-2) levels, suggesting that this type of hypertriglyceridaemia is caused—at least, in part—by lipoprotein lipase deficiency with impaired removal of the triglyceride-rich lipoproteins and increased catabolism of HDL-2. Our findings point towards a type of hypertriglyceridaemia strongly associated with coronary artery disease which should therefore be treated accordingly. more...
- Published
- 1989
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183. Leoligin, the major lignan from Edelweiss, activates cholesteryl ester transfer protein
- Author
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Kathrin Eller, Daniela Schuster, David Bernhard, Philipp Eller, Ursula Stanzl, Hermann Stuppner, Ivan Tancevski, Tobias Linder, Andreas Ritsch, Stefan Schwaiger, Josef R. Patsch, Miranda Van Eck, Kristina Duwensee, and Patrick Markt more...
- Subjects
Transgene ,Sterol O-acyltransferase ,Mice, Transgenic ,EDELWEISS ,Molecular Dynamics Simulation ,Article ,Lignans ,chemistry.chemical_compound ,Mice ,Cholesterylester transfer protein ,Animals ,Humans ,Cholesterol metabolism ,High-density lipoproteins ,Lignan ,biology ,Metabolism ,Cholesteryl ester transfer protein ,Cholesterol Ester Transfer Proteins ,carbohydrates (lipids) ,Biochemistry ,chemistry ,biology.protein ,lipids (amino acids, peptides, and proteins) ,Rabbits ,Cardiology and Cardiovascular Medicine ,Lipoprotein - Abstract
Highlights ► Leoligin significantly activated CETP in human plasma at 100 pM. ► Leoligin concentrations of 1 mM inhibited CETP activity. ► There was no short-term toxicity apparent in mice treated with leoligin., Objective Cholesteryl ester transfer protein (CETP) plays a central role in the metabolism of high-density lipoprotein particles. Therefore, we searched for new drugs that bind to CETP and modulate its activity. Methods A preliminary pharmacophore-based parallel screening approach indicated that leoligin, a major lignan of Edelweiss (Leontopodium alpinum Cass.), might bind to CETP. Therefore we incubated leoligin ex vivo at different concentrations with human (n = 20) and rabbit plasma (n = 3), and quantified the CETP activity by fluorimeter. Probucol served as positive control. Furthermore, we dosed CETP transgenic mice with leoligin and vehicle control by oral gavage for 7 days and measured subsequently the in vivo modulation of CETP activity (n = 5 for each treatment group). Results In vitro, leoligin significantly activated CETP in human plasma at 100 pM (p = 0.023) and 1 nM (p = 0.042), respectively, whereas leoligin concentrations of 1 mM inhibited CETP activity (p = 0.012). The observed CETP activation was not species specific, as it was similar in magnitude for rabbit CETP. In vivo, there was also a higher CETP activity after oral dosage of CETP transgenic mice with leoligin (p = 0.015). There was no short-term toxicity apparent in mice treated with leoligin. Conclusion CETP agonism by leoligin appears to be safe and effective, and may prove to be a useful modality to alter high-density lipoprotein metabolism. more...
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184. Hyperlipoprotein�mie Typ III: Diagnose und quantitative Isolierung des charakteristischen Lipoproteins
- Author
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S. Sailer, Herbert Braunsteiner, Josef R. Patsch, and Wolfgang Patsch
- Subjects
Chemistry ,Drug Discovery ,Molecular Medicine ,General Medicine ,Molecular biology ,Genetics (clinical) ,Lipoprotein - Abstract
Mit Hilfe einer zonalen Ultrazentrifugationstechnik wurde bei Patienten mit Typ III-Hyperlipoproteinamie ein zusatzliches Lipoprotein (Lp III) quantitativ isoliert. Dieses Lp III ist hinsichtlich seiner hydrierten Dichte (Sf 15–20), seines Gehalts an Protein (20%), Gesamtcholesterin (36%) und Triglyceriden (19%), sowie hinsichtlich seiner elektrophoretischen Wanderungsgeschwindigkeit zwischen VLDL (Sf>20) und LDL (Sf 6–8) einzuordnen. Immunologisch konnte wie in den VLDL Apo-Lp B und Apo-Lp C nachgewiesen werden. more...
- Published
- 1974
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185. Apoprotein Exchange between Human High-Density-Lipoprotein Subfractions (High-Density-Lipoprotein Subfractions 2 and 3)
- Author
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Gemmell Morgan, Josef R. Patsch, Christopher J. Packard, Antonio M. Gotto, and James Shepherd
- Subjects
chemistry.chemical_classification ,Lipoprotein lipase ,Chemistry ,Adipose tissue ,Heparin ,Biochemistry ,Centrifugation, Zonal ,In vitro ,chemistry.chemical_compound ,Apolipoproteins ,High-density lipoprotein ,Enzyme ,medicine ,Humans ,lipids (amino acids, peptides, and proteins) ,Centrifugation ,Lipoproteins, HDL ,Protein Binding ,medicine.drug - Abstract
centrifugation restored these increases when included in the heparin-containing medium at concentrations of 10-8Opg of protein/ml. The ability of heparin to stimulate the release of lipoprotein lipase from human adipose tissue in vitro has been demonstrated by several groups of workers (Elkeles, 1974). That this release can be closely correlated with triacylglycerol clearance provided further evidence of the central role played by this enzyme in the transfer of triacylglycerol from blood to peripheral tissues. Serum lipoproteins appear to have a role in potentiating the release of the enzyme from the tissue. more...
- Published
- 1978
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186. Dynamics of lipid motions in high-density lipoprotein subfractions HDL2 and HDL3: magnetic resonance studies
- Author
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J. D. Morrisett, James R. Brainard, Josef R. Patsch, Antonio M. Gotto, and Roger D. Knapp
- Subjects
Male ,Magnetic Resonance Spectroscopy ,medicine.diagnostic_test ,Chemical Phenomena ,Chemistry ,Chemistry, Physical ,General Neuroscience ,Dynamics (mechanics) ,Fatty Acids ,Electron Spin Resonance Spectroscopy ,Magnetic resonance imaging ,General Biochemistry, Genetics and Molecular Biology ,chemistry.chemical_compound ,Nuclear magnetic resonance ,High-density lipoprotein ,History and Philosophy of Science ,Models, Chemical ,medicine ,Centrifugation, Density Gradient ,Humans ,Lipoproteins, HDL - Published
- 1980
187. High density lipoprotein2. Relationship of the plasma levels of this lipoprotein species to its composition, to the magnitude of postprandial lipemia, and to the activities of lipoprotein lipase and hepatic lipase
- Author
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Wolfgang Patsch, Josef R. Patsch, Antonio M. Gotto, and Sarada Prasad
- Subjects
medicine.medical_specialty ,Apolipoprotein B ,Triacylglycerol lipase ,Coronary Disease ,Apolipoproteins A ,chemistry.chemical_compound ,Eating ,Internal medicine ,medicine ,Humans ,Triglycerides ,Lipoprotein lipase ,biology ,Cholesterol ,digestive, oral, and skin physiology ,Cholesterol, HDL ,General Medicine ,Lipoprotein Lipase ,Endocrinology ,Postprandial ,chemistry ,Liver ,biology.protein ,lipids (amino acids, peptides, and proteins) ,Hepatic lipase ,Cholesterol Esters ,Lipoproteins, HDL ,Lipoprotein ,Research Article - Abstract
Lipoprotein lipase (LPL) activity in postheparin plasma of 38 normolipidemic volunteers was related to the magnitude of postprandial lipemia after a fat meal, to triglyceride content of high density lipoprotein2 (HDL2), to hepatic lipase (HL) activity, and to HDL2 levels. LPL activity correlated indirectly with lipemia, triglyceride content of HDL2, HL activity, and levels of HDL2 but not of HDL3. HL activity correlated directly with lipemia and indirectly with HDL2 levels. Triglyceride content of HDL2 correlated directly with lipemia and indirectly with HDL2 levels. In HDL2, abundance of apolipoprotein (apo) A-II and the apoA-I/apoA-II ratio varied widely. The latter correlated positively with LPL activity and HDL2 levels, and, inversely, with HL activity, lipemia, and triglyceride content of HDL2. The study suggests that HDL-cholesterol is not an independent parameter of lipid transport, but is strongly affected by triglyceride metabolism through lipolytic enzymes, as exemplified by postprandial lipemia that affect both composition and plasma levels of HDL2. more...
- Published
- 1987
188. Type III Hyperlipoproteinemia
- Author
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Josef R. Patsch
- Subjects
Intermediate-density lipoprotein ,medicine.medical_specialty ,Very low-density lipoprotein ,Triglyceride ,Familial dysbetalipoproteinemia ,Chemistry ,Cholesterol ,medicine.disease ,chemistry.chemical_compound ,Endocrinology ,High-density lipoprotein ,Internal medicine ,medicine ,lipids (amino acids, peptides, and proteins) ,Lipoprotein disorder ,Chylomicron - Abstract
Several synonyms for familial type III hyperlipoproteinemia are often used. These include familial “broad-β” disease, “floating-β” disorder, dysbetalipoproteinemia, xanthoma tuberosum, and idiopathic hypercholesterolemic xanthomatosis with hyperlipemia. Type III hyperlipoproteinemia is a genetically determined lipoprotein disorder manifested by an increased concentration of both cholesterol and triglyceride in the plasma. It is characterized by the presence of a lipoprotein that floats between density 1.006–1.019 in the postabsorptive state. Moreover, the concentration of VLDL (d < 1.006) is increased, and, frequently, chylomicrons are present in the fasting plasma. Often, the plasma lipoprotein electrophoresis pattern is characterized by a “broad-β” band. more...
- Published
- 1976
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189. Metabolism of apolipoproteins A-I and A-II and its influence on the high density lipoprotein subfraction distribution in males and females
- Author
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Christopher J. Packard, O. David Taunton, Josef R. Patsch, James Shepherd, and Antonio M. Gotto
- Subjects
Adult ,Male ,medicine.medical_specialty ,Clinical Biochemistry ,Apolipoproteins A ,Biochemistry ,Sex Factors ,Internal medicine ,High density lipoprotein subfraction ,polycyclic compounds ,medicine ,Distribution (pharmacology) ,Humans ,Triglycerides ,Plasma samples ,Chemistry ,Catabolism ,General Medicine ,Metabolism ,Endocrinology ,Apolipoproteins ,Cholesterol ,lipids (amino acids, peptides, and proteins) ,Female ,Lipoproteins, HDL ,Ultracentrifugation - Abstract
Rate zonal ultracentrifugation of plasma samples from ten healthy age-matched volunteers (five males, five females) indicated that the high density lipoprotein subfraction ratio (HDL2:HDL3) in females was significantly higher than in males. The cause of this phenomenon was investigated by simultaneous examination of the metabolism of the major HDL apoproteins (apoA-I and apoA-II) in both groups. The results show that there is no significant sex-related difference in the plasma pool size, fractional catabolic rate, or synthetic rate of either apoprotein. We conclude that the increased HDL2:HDL3 ratio in females versus males does not derive from measurable differences in the metabolic handling of either apoprotein. more...
- Published
- 1978
190. Treatment of severe cancer pain by low-dose continuous subcutaneous morphine
- Author
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Alexander Dzien, Klaus Abbrederis, Josef R. Patsch, H. Drexel, Christoph Breier, Alois Lang, Herbert Braunsteiner, and Robert W. Spiegel
- Subjects
medicine.medical_specialty ,Palliative care ,Nausea ,medicine.medical_treatment ,Sedation ,Drug Administration Schedule ,Drug tolerance ,Neoplasms ,medicine ,Humans ,Infusion Pumps ,Pain Measurement ,Chemotherapy ,Clinical Trials as Topic ,Morphine ,business.industry ,Palliative Care ,Drug Tolerance ,Surgery ,Anesthesiology and Pain Medicine ,Neurology ,Anesthesia ,Neurology (clinical) ,medicine.symptom ,Cancer pain ,business ,medicine.drug ,Methadone - Abstract
In a prospective and intraindividually controlled trial, we have compared the efficacy and safety of a continuous subcutaneous morphine infusion with conventional intermittent oral or subcutaneous morphine application. Twenty-eight in-patients with cancer pain received a short-term infusion lasting 2-42 days, and 8 out-patients underwent long-term infusion from 49 to 197 days during the terminal stage of their disease. Continuous subcutaneous morphine infusion significantly (P less than 0.001) improved both pain and quality of life when compared to conventional morphine application. With continuous infusion, 5-48 mg (median 19 mg) of morphine was required daily, significantly (P less than 0.001) less than the 10-90 mg (median 50 mg) necessary with conventional use. As a result of lower dosage, side effects under continuous infusion were infrequent and mild. Constipation occurred in 3 of the 36 patients and was always controlled by the addition of laxatives; no nausea, sedation or respiratory depression were observed. Signs of tolerance developed in 2 patients on long-term infusion, but the use of continuous subcutaneous methadone for 2 weeks reversed the tolerance. The study presented indicates that low-dose continuous subcutaneous morphine provides a valuable treatment modality for severe terminal cancer pain exhibiting a high degree of both efficacy and safety. more...
- Published
- 1989
191. Control of 3-Hydroxy-3-Methylglutaryl-CoA Reductase Activity in Cultured Human Fibroblasts by Very Low Density Lipoproteins of Subjects with Hypertriglyceridemia
- Author
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Richard L. Jackson, Josef R. Patsch, Louis C. Smith, Daniel Yeshurun, Sandra H. Gianturco, Antonio M. Gotto, O. David Taunton, and Harley D. Sybers
- Subjects
Adult ,Male ,Very low-density lipoprotein ,medicine.medical_specialty ,Hyperlipidemias ,Familial hypercholesterolemia ,Reductase ,Lipoproteins, VLDL ,chemistry.chemical_compound ,Internal medicine ,Hyperlipidemia ,medicine ,polycyclic compounds ,Humans ,Cells, Cultured ,Triglycerides ,Intermediate-density lipoprotein ,Triglyceride ,Chemistry ,Hypertriglyceridemia ,nutritional and metabolic diseases ,General Medicine ,Articles ,Fibroblasts ,Middle Aged ,medicine.disease ,Hydroxymethylglutaryl-CoA reductase ,Lipoproteins, LDL ,Endocrinology ,lipids (amino acids, peptides, and proteins) ,Hydroxymethylglutaryl CoA Reductases ,Ultracentrifugation - Abstract
Very low density lipoproteins (VLDL) and low density lipoproteins (LDL) from human normolipemic plasma, and the VLDL, the intermediate density lipoprotein (IDL), and LDL from patients with Type III hyperlipoproteinemic plasma were tested for their abilities to suppress the activity of 3-hydroxy-3-methylglutaryl-Coenzyme A (HMG-CoA) reductase in cultured human fibroblasts from normal subjects and a Type III patient. Regulation of cholesterol synthesis in the fibroblasts of a patient with Type III hyperlipoproteinemia appears to be normal. VLDL from normal subjects, isolated by angle head ultracentrifugation (d < 1.006) or by gel filtration on BioGel A-5m, were about 5 times less effective than LDL in suppressing HMG-CoA reductase activity, based on protein content, in agreement with previous reports with normal fibroblasts. Zonal centrifugation of normal VLDL isolated by both methods showed that the VLDL contained IDL. Normal VLDL from the angle head rotor, refractionated by the zonal method, had little, if any, ability to suppress the HMG-CoA reductase activity in either normal or Type III fibroblasts. VLDL, IDL, and LDL fractionated by zonal ultracentrifugation from Type III plasma gave half-maximum inhibition at 0.2-0.5 mug of protein/ml, indistinguishable from the suppression caused by normal LDL. Type III VLDL did not suppress HMG-CoA reductase in mutant LDL receptor-negative fibroblasts. Zonally isolated VLDL obtained from one Type IV and one Type V patient gave half-maximal suppression at 5 and 0.5 mug of protein/ml, respectively. Molecular diameters and apoprotein compositions of the zonally isolated normal and Type III VLDL were similar; the major difference in composition was that Type III VLDL contained more cholesteryl esters and less triglyceride than did normal VLDL. The compositions and diameters of the Type IV and Type V VLDL were similar to normal VLDL. These findings show that the basic defect in Type III hyperlipoproteinemia is qualitatively different from the cellular defect found in familial hypercholesterolemia, since the regulation of HMG-CoA reductase activity is normal in Type III fibroblasts. The metabolic defect in hypertriglyceridemia is related to the triglyceriderich lipoproteins which, free of other lipoproteins, have an enhanced ability to interact with cultured fibroblasts to regulate HMG-CoA reductase activity. These studies suggest that, in hypertriglyceridemia, there is a mechanism for direct cellular catabolism of VLDL which is not functional for normal VLDL. more...
- Published
- 1978
192. Inverse relationship between blood levels of high density lipoprotein subfraction 2 and magnitude of postprandial lipemia
- Author
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Lynne W. Scott, Louis C. Smith, Joan B. Karlin, Antonio M. Gotto, and Josef R. Patsch
- Subjects
Adult ,Male ,medicine.medical_specialty ,Apolipoprotein B ,Metabolic Clearance Rate ,Apolipoprotein A-II ,chemistry.chemical_compound ,High-density lipoprotein ,Internal medicine ,medicine ,Humans ,Triglycerides ,Meal ,Multidisciplinary ,biology ,Triglyceride ,Cholesterol ,Radioimmunoassay ,Lipoproteins, HDL3 ,Dietary Fats ,Lipids ,Lipoproteins, HDL2 ,Postprandial ,Endocrinology ,Apolipoproteins ,chemistry ,biology.protein ,lipids (amino acids, peptides, and proteins) ,Female ,Lipoproteins, HDL ,Research Article - Abstract
Triglyceridemic response to a standard oral fat meal was determined in 28 healthy subjects and related to the levels of several lipids, lipoproteins, and apolipoproteins in the post-absorptive plasma. A fatty test meal was administered orally, and postprandial plasma triglyceride levels were determined. In the fasting blood samples, concentrations of apolipoproteins (apo) A-I, A-II, and B were determined by radioimmunoassay, and those of high density lipoprotein (HDL) subfractions HDL2 and HDL3, by zonal ultracentrifugation. The magnitude of triglyceridemic response showed a negative correlation with the plasma levels of HDL2 (r = -0.860, P less than 0.001), HDL-associated cholesterol (r = -0.605, P less than 0.001), and apoA-I (r = -0.459, P less than 0.02). No correlation was found between the triglyceridemic response and the levels of total cholesterol, HDL3, and apoA-II. Triglyceridemic response was correlated positively with fasting triglyceride concentrations (r = 0.450, P less than 0.02) and apoB levels (r = 0.396, P less than 0.03). In two subjects followed for 3 yr, when HDL2 levels rose or fell, the triglyceridemic response decreased or increased, respectively (r = -0.944; r = -0.863). Our data indicate that normolipidemic individuals with high HDL2 levels in the plasma are able to clear alimentary fat at a faster rate than normolipidemic subjects with low HDL2 levels. The pronounced difference in severity and duration of postprandial lipemia among subjects with varying HDL2 levels may help to explain the negative correlation between the risk of atherosclerosis and HDL cholesterol levels. more...
- Published
- 1983
193. Effects of Dietary Polyunsaturated and Saturated Fat on the Properties of High Density Lipoproteins and the Metabolism of Apolipoprotein A-I
- Author
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Josef R. Patsch, James Shepherd, O. David Taunton, Christopher J. Packard, and Antonio M. Gotto
- Subjects
Adult ,Male ,medicine.medical_specialty ,Very low-density lipoprotein ,Saturated fat ,chemistry.chemical_compound ,Polyunsaturated fat ,High-density lipoprotein ,Internal medicine ,medicine ,Humans ,Phospholipids ,Triglycerides ,Triglyceride ,Cholesterol ,General Medicine ,Articles ,Dietary Fats ,Centrifugation, Zonal ,Fats, Unsaturated ,Endocrinology ,Apolipoproteins ,Biochemistry ,chemistry ,Low-density lipoprotein ,lipids (amino acids, peptides, and proteins) ,Lipoproteins, HDL ,Lipoprotein - Abstract
In this study we have investigated, in four normal males the effects of dietary saturated and polyunsaturated fat on the chemical composition and thermotropic properties of human high density lipoproteins (HDL) and have measured the influence of the diets on the metabolism of that fraction of HDL apolipoprotein A-I (apoA-I) that undergoes exchange in vitro and accounts for approximately two-thirds of the lipoprotein's apoA-I complement. When compared with the saturated fat diet, the polyunsaturated diet reduced plasma cholesterol (24%, P0.01) by affecting the cholesterol content in the very low density lipoprotein ( downward arrow25%, P0.02), low density lipoprotein ( downward arrow20%, P0.01), and high density lipoprotein fractions ( downward arrow33%, P0.01). Plasma triglyceride was also lowered (by 13%, P0.01). Furthermore, polyunsaturated fat ingestion caused a significant fall in the palmitate and stearate content of HDL triglyceride (41 and 37%, respectively), cholesteryl esters (29 and 35%), and phospholipids (17 and 9%) with a concomitant increase in the linoleate content of these moieties (157, 28, and 29%, respectively). The polyunsaturated diet also produced reciprocal changes in the percentage protein ( downward arrow9%, P0.02) and phospholipid ( downward arrow11.5%, P0.01) in HDl. These compositional changes were associated with an increase in the microscopic fluidity of the polyunsaturated HDL, although both diets had little effect on the fluidity parameters of HDL at body temperature. Rate zonal ultracentrifugation indicated that the HDL(2)/HDL(3) ratio fell by 28% (P0.05) on the polyunsaturated fat diet. In addition to the above, this diet reduced plasma apoA-I by 21% (P0.01). No change was seen in the fractional catabolic rate or the distribution of the apoprotein between intravascular and extravascular compartments on the two diets. However, when compared with the saturated diet, the synthetic rate of apoA-I was reduced by 26% during polyunsaturated fat feeding. The results show that polyunsaturated fat alters the chemical composition, thermotropic properties, and subfraction distribution of HDL without changing the fractional rate of catabolism of their major protein, apoA-I.These findings deserve careful consideration in determining the applicability and efficacy of polyunsaturated fat diet therapy in the prevention of atherosclerosis in man. more...
- Published
- 1978
194. Diagnosis of Type III Hyperlipoproteinemia by Means of Rate Zonal Ultracentrifugation
- Author
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S. Sailer, Josef R. Patsch, and W. Patsch
- Subjects
Very low-density lipoprotein ,Chromatography ,Chemistry ,lipids (amino acids, peptides, and proteins) ,Fraction (chemistry) ,Ultracentrifuge ,Lipoprotein - Abstract
The partial conflicting reports regarding the definition and diagnosis of type III hyperlipoproteinemia gave rise to our investigation of the main lipoprotein density classes in the plasma of type III patients. Since not only the VLDL fraction is altered in these patients, we separated the lipoprotein fractions d more...
- Published
- 1977
- Full Text
- View/download PDF
195. Effects of HDL subclasses on 3-hydroxy-3-methylglutaryl coenzyme A reductase in human fibroblasts
- Author
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Josef R. Patsch, L. C. Smith, W.H. Daerr, Sandra H. Gianturco, and Antonio M. Gotto
- Subjects
7-Dehydrocholesterol reductase ,Medicine (miscellaneous) ,Reductase ,Biology ,Tissue culture ,Humans ,Enzyme inducer ,Cells, Cultured ,Nutrition and Dietetics ,Cell growth ,3 hydroxy 3 methylglutaryl coenzyme a reductase ,Cell Cycle ,Lipoproteins, HDL3 ,Cell cycle ,Fibroblasts ,Hydroxymethylglutaryl-CoA reductase ,Molecular biology ,Lipoproteins, HDL2 ,Cholesterol ,Biochemistry ,Hydroxymethylglutaryl-CoA-Reductases, NADP-dependent ,Enzyme Induction ,biology.protein ,lipids (amino acids, peptides, and proteins) ,Hydroxymethylglutaryl CoA Reductases ,Lipoproteins, HDL - Abstract
Monolayer cultures of normal human fibroblasts were used to study the effects of the main subclasses of high-density lipoproteins, HDLa and HDL3, on 3-hydroxy-3-methylglutaryl CoA reductase (EC 1.1.1.34) activity. In this system, HDL3 (d= 1.125–1.210 g/cm3) specifically induced HMG-CoA reductase activity. Evaluation of culture dynamics revealed that enzyme induction was restricted to the stationary phase of growth. When the cells were incubated with HDL2 (d = 1.063–1.125 g/cm3), suppression of reductase activity was observed. Mixtures of HDL2 and HDL3 suppressed reductase activity when HDL2 was greater than 35% of the total HDL. The suppressive effects of HDL2 were abolished by treatment with cyclohexanedione and restored by regeneration of the arginyl residues, suggesting an apoprotein-mediated suppressive mechanism. These observations show that the cellular effects of HDL depend upon the stage of cell growth and the ratio of HDL subclasses in HDL as usually isolated. more...
- Published
- 1980
196. Chapter 7 Metabolism of high density lipoproteins
- Author
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Josef R. Patsch and Antonio M. Gotto
- Subjects
chemistry.chemical_classification ,Signal peptidase ,Apolipoprotein B ,Cholesterol ,Endoplasmic reticulum ,Reverse cholesterol transport ,nutritional and metabolic diseases ,Metabolism ,Biology ,Amino acid ,chemistry.chemical_compound ,Biochemistry ,chemistry ,biology.protein ,lipids (amino acids, peptides, and proteins) ,Chylomicron - Abstract
Publisher Summary This chapter highlights high-density lipoproteins (HDL) metabolism in humans. HDL concentration in plasma is expressed as HDL cholesterol that remains in the supernatant after precipitation of the apolipoprotein (apo)B-containing lipoproteins and represents a minor fraction of cholesterol in plasma. HDL particles have a spherical shape and possess a core of neutral lipids comprising mostly of cholesteryl esters. Variable amounts of triglycerides are present in the core, depending on the plasma triglyceride levels. The hydrophobic core is surrounded by a surface monolayer consisting of phospholipids, cholesterol, and apolipoproteins. HDL particles are heterogeneous with respect to size, composition, and density. The two major apolipoproteins in HDL are apoA-I and apoA-II. The primary translation product of human apoA-I mRNA possesses an additional peptide that contains 18 amino acids that is cleaved intracellularly by a signal peptidase of the endoplasmic reticulum leaving pro-apoA. The apoA-I gene contains six homologous tandemly repeated 66 bp regions indicating internal gene duplication. more...
- Published
- 1987
- Full Text
- View/download PDF
197. Stimulation of Human Early and Late Erythropoietic Progenitor Cells by Insulin: Evidence for Different Mechanisms
- Author
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Christian J. Wiedermann, Dietmar Geissler, AL Petzer, Christoph Breier, Günther Konwalinka, Kurt Grünewald, and Josef R. Patsch
- Subjects
chemistry.chemical_classification ,medicine.medical_specialty ,food.ingredient ,biology ,Insulin ,medicine.medical_treatment ,Monocyte ,Stimulation ,medicine.anatomical_structure ,Endocrinology ,food ,chemistry ,Transferrin ,hemic and lymphatic diseases ,Internal medicine ,medicine ,biology.protein ,Erythropoiesis ,Agar ,Bone marrow ,Bovine serum albumin - Abstract
In order to investigate cellular mechanisms involved in insulin stimulation of erythropoiesis, we have studied the response of early (BFU-e) and late (CFU-e) erythroid progenitor cells in a serum-free agar culture system. In this assay system, CFU-e proliferation occurred in media containing low-density lipoproteins, bovine serum albumin, transferrin and recombinant erythropoietin (rEPO). Insulin in physiological concentrations as low as 10-12M, added directly to cultures, augmented CFU-e colony formation. This stimulatory effect was also seen when monocyte- and T lymphocyte-depleted cells from normal donors were cultured. In contrast, BFU-e was not stimulated by media devoid of insulin. Occurrence of BFU-e colonies required the presence of insulin in concentrations higher than 10-8M This insulin effect was not dependent on the presence of monocytes and T lymphocytes. Delayed addition studies of rEPO to insulin containing cultures revealed a slight but significant survival rate of CFU-e. A similar survival rate was found for BFU-e. From this, we conclude that insulin stimulates CFU-e by an EPO-like activity. For BFU-e, however, the decline in the number of bursts caused by EPO deprivation implies that insulin does not act directly as a burst-promoting activity but that it probably induces the release of this activity from non-adherent and T lymphocyte-depleted bone marrow cells. more...
- Published
- 1988
- Full Text
- View/download PDF
198. Measurement of glycated protein by a rapid and specific method for absolute quantification of lysine-bound glucose
- Author
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H Klocker, Josef R. Patsch, Braunsteiner H, Ch. Breier, and Heinz Drexel
- Subjects
Quality Control ,Glycosylation ,Resolution (mass spectrometry) ,Lipoproteins ,Clinical Biochemistry ,Lysine ,Serum albumin ,Hydrolysate ,chemistry.chemical_compound ,Column chromatography ,Chemical Precipitation ,Humans ,Chromatography, High Pressure Liquid ,Glycoproteins ,Ethanol ,Chromatography ,biology ,Chemistry ,Biochemistry (medical) ,Liter ,Blood Proteins ,Blood proteins ,Glucose ,Immunoglobulin G ,biology.protein ,Tyrosine - Abstract
We modified the liquid-chromatographic assay of Schleicher and Wieland (J Clin Chem Clin Biochem 1981; 19:81-7) for measuring lysine-bound glucose in serum proteins, increasing its performance and practicality. After precipitating serum proteins from 10- to 50-microL samples with ethanol (700 mL/L) and hydrolyzing these in 6 mol/L HCl, we inject 20 microL of the diluted hydrolysate directly into the chromatograph, which consists of an acid-resistant C18 precolumn combined with a high-resolution C18 main column. The eluent is 3.5 mmol/L H3PO4 solution containing 30 mL of acetonitrile per liter. These modifications increase sensitivity, provide excellent resolution and longevity of stationary phases, shorten assay times to 15 to 20 min, and are suited for automation. The assay is highly sensitive and highly specific, quantifying nanomoles of lysine-bound glucose per milligram of protein. A precision (CV) of 5.1% is achievable at physiological and supra-physiological glucose concentrations, and analytical recovery is 99%. This inexpensive method has been applied to serum albumin, bulk serum proteins, and preparations of low-density lipoproteins and immunoglobulins. more...
- Published
- 1987
199. Effects of Nicotinic Acid Therapy on Plasma High Density Lipoprotein Subfraction Distribution and Composition and on Apolipoprotein A Metabolism
- Author
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O. David Taunton, Josef R. Patsch, James Shepherd, Antonio M. Gotto, and Christopher J. Packard
- Subjects
Adult ,Male ,medicine.medical_specialty ,Very low-density lipoprotein ,Apolipoprotein B ,Phospholipid ,Lipoproteins, VLDL ,chemistry.chemical_compound ,High-density lipoprotein ,Internal medicine ,medicine ,polycyclic compounds ,Humans ,Triglycerides ,biology ,Triglyceride ,Cholesterol ,Nicotinic Acids ,nutritional and metabolic diseases ,General Medicine ,Articles ,Lipoproteins, LDL ,Nicotinic agonist ,Endocrinology ,Apolipoproteins ,chemistry ,biology.protein ,lipids (amino acids, peptides, and proteins) ,Female ,Lipoproteins, HDL - Abstract
This report describes the effects of pharmacologic doses (3 g/d) of nicotinic acid on the plasma distribution and chemical composition of the high density lipoprotein (HDL) subfractions HDL2 and HDL3 and examines the influence of the drug on the metabolism of the major HDL apoproteins, apolipoproteins A-I (ApoA-I) and A-II (Apo-II). The drug lowered plasma cholesterol (15%, P < 0.05) and triglyceride (27%, P < 0.01); the former effect a result of a fall in the amount of cholesterol associated with very low density lipoproteins (31%, P < 0.02) and low density lipoproteins (36%, P < 0.02). Conversely, it raised plasma HDL cholesterol (23%, P < 0.05) and increased (by 345%) the plasma HDL2:HDL3 ratio. The latter derived from an absolute increment (646%) in circulating HDL2, coupled with a fall (47%) in HDL3. This change was not associated with major alterations in the overall cholesterol (free and esterified), triglyceride, phospholipid, or protein content of the subfractions; however, it was accompanied by substantial changes in their protein composition. In particular, the molar ratio of ApoA-I:ApoA-II in HDL3 declined from 2.7:1 to 2.1:1 during nicotinic acid treatment. Significant perturbations of ApoA-I and ApoA-II metabolism accompanied the drug-induced HDL subfraction redistribution. Specifically, the plasma concentration of ApoA-I rose by 7% (P < 0.05) because of a decrease in its fractional catabolic rate. Moreover, whereas before treatment 6 and 94% of the plasma ApoA-I circulated with HDL2 and HDL3, after commencement of nicotinic acid therapy this distribution became 49 and 51% in HDL2 and HDL3, respectively. ApoA-II was found mainly in HDL3, both before and during nicotinic acid treatment. Administration of the drug caused a 14% reduction in its plasma concentration (P < 0.05), which derived principally from a fall (22%, P < 0.01) in its synthetic rate. These data suggest that the effects of nicotinic acid on the HDL subfraction distribution may be mediated via (a) net transfer of ApoA-I from HDL3 to HDL2 and (b) a reduction in ApoA-II synthesis. Our present understanding of the association between HDL and atherosclerosis indicates that such changes may have prophylactic value in the prevention of coronary artery disease. more...
- Published
- 1979
200. Polypeptide distribution of the main lipoprotein density classes separated from human plasma by rate zonal ultracentrifugation
- Author
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Herbert Braunsteiner, Josef R. Patsch, Gerhard M. Kostner, Anton Holasek, and S. Sailer
- Subjects
Adult ,Male ,Immunodiffusion ,Apolipoprotein B ,Adolescent ,Lipoproteins ,Lipoproteins, VLDL ,Biochemistry ,Distribution (pharmacology) ,Humans ,Polyacrylamide gel electrophoresis ,Chromatography ,biology ,Chemistry ,Immune Sera ,Middle Aged ,Centrifugation, Zonal ,Lipoproteins, LDL ,Human plasma ,biology.protein ,lipids (amino acids, peptides, and proteins) ,Electrophoresis, Polyacrylamide Gel ,Female ,Ultracentrifuge ,Apoproteins ,Lipoproteins, HDL ,Peptides ,Lipoprotein ,Densitometry - Abstract
The polypeptide distribution of lipoprotein density fractions isolated from normal human serum by rate zonal ultracentrifugation was investigated by polyacrylamide gel electrophoresis and qualitative and quantitative immunochemical methods. In very-low-density lipoproteins all known apoA and apoC peptides were present in amounts similar to these preparations from fixed-angle rotors. Low-density apolipoproteins consisted primarily of apoB (98%) but some small amounts of apoAIII and apoCIII were also present. No region of 100% apoB, uncontaminated by A and C peptides could be isolated by subfractionation of the low-density peak. There were marked differences in the protein part of the high-density lipoprotein subtractions 2 and 3, as compared to these subfractions separated in the angle-head rotor. The weight ratio apoAI: apoAII was found to be approximately three times as high for subfraction 2 as for subfraction 3. In addition, apoAIII was detectable only in subfraction 3. Of the known apoC peptides, apoCII was present in both fractions only in trace amounts, while the concentration of apoCI was in the order of 1% and that of apoCIII1 and of apoCIII2 in the order of 1.5%. Apolipoprotein B was not detectable in subfraction 2. Two density regions were found with small amounts of lipoproteins consisting only of apoAI polypeptides. A peak corresponding to subfraction 1 of the high-density lipoprotein from fixed-angle rotor preparations could not be detected in the eluate of zonal rotors after 24-h runs; the low-density lipoprotein peak was symmetrical in all experiments. Lipoproteins present in the bottom fraction amounted to about 2.5–4% of the total lipoprotein content. The only apolipoprotein found in this fraction was apoAI. more...
- Published
- 1974
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