11 results on '"Juichi Sato"'
Search Results
2. Pyogenic spondylitis with acute course caused by Corynebacterium simulans
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T. Niwa, R. Oshima, Y. Ando, Takeshi Kondo, F. Sugiura, Juichi Sato, S. Kohri, Takaharu Matsuhisa, M. Ogasawara, and M. Sato
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0301 basic medicine ,Microbiology (medical) ,medicine.medical_specialty ,030106 microbiology ,Corynebacterium ,Lumbar vertebrae ,03 medical and health sciences ,0302 clinical medicine ,Diabetes mellitus ,medicine ,Back pain ,Pharmacology (medical) ,Blood culture ,030212 general & internal medicine ,Corynebacterium simulans ,Spondylitis ,biology ,medicine.diagnostic_test ,business.industry ,biology.organism_classification ,medicine.disease ,Dermatology ,Infectious Diseases ,medicine.anatomical_structure ,Vancomycin ,medicine.symptom ,business ,medicine.drug - Abstract
Corynebacterium simulans was first reported in 2000. Although it is a member of the normal skin flora, some cases of C. simulans infection have been reported. Other Corynebacterium spp. rarely cause chronic pyogenic spondylitis, and pyogenic spondylitis caused by C. simulans has not been reported at all. Here we report a case of acute pyogenic spondylitis due to C. simulans. A 78-year-old man with diabetes mellitus visited our hospital with a 3-day history of lower back pain and fever. Blood culture revealed C. simulans and magnetic resonance images of lumbar vertebrae showed pyogenic spondylitis. He recovered after treatment by vancomycin for 9 weeks and was discharged home. No recurrence has been observed for half a year. This is likely the first reported case of pyogenic spondylitis by C. simulans. In general, Corynebacterium spp. cause chronic pyogenic spondylitis, but this case showed an acute course.
- Published
- 2020
3. Diabetes as First Manifestation of Autoimmune Pancreatitis
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Nobutaro Ban, Takehiro Miyazaki, Juichi Sato, Eiji Hiraoka, and Toru Yamada
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medicine.medical_specialty ,030209 endocrinology & metabolism ,Gastroenterology ,Autoimmune Diseases ,Diabetes Complications ,03 medical and health sciences ,0302 clinical medicine ,Adrenal Cortex Hormones ,Diabetes mellitus ,Internal medicine ,Diabetes Mellitus ,medicine ,Humans ,Pancreatitis complications ,Aged ,Dyslipidemias ,Autoimmune pancreatitis ,Autoimmune disease ,Pioglitazone ,business.industry ,Sitagliptin Phosphate ,General Medicine ,Diabetes mellitus therapy ,medicine.disease ,Liver ,Pancreatitis ,Immunoglobulin G ,Hypertension ,Female ,Thiazolidinediones ,030211 gastroenterology & hepatology ,IgG4-related disease ,business ,medicine.drug - Published
- 2017
4. Fundamental studies on the inhibitory action of Acanthopanax senticosus Harms on glucose absorption
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Kazuhiro Watanabe, Keiko Kamata, Tunehisa Takahashi, and Juichi Sato
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Blood Glucose ,Male ,medicine.medical_specialty ,animal structures ,Phloretin ,medicine.medical_treatment ,Glucose uptake ,Cell Culture Techniques ,Administration, Oral ,Blood sugar ,Eleutherococcus ,Mice, Inbred Strains ,Diabetes Mellitus, Experimental ,Mice ,chemistry.chemical_compound ,Intestinal mucosa ,Internal medicine ,Drug Discovery ,Animals ,Humans ,Hypoglycemic Agents ,Insulin ,Medicine ,Acarbose ,Pharmacology ,Plant Extracts ,business.industry ,Glucose transporter ,alpha-Glucosidases ,Glucose Tolerance Test ,Glucose ,Endocrinology ,Postprandial ,Diabetes Mellitus, Type 2 ,chemistry ,Plant Bark ,Adsorption ,Caco-2 Cells ,alpha-Amylases ,business ,medicine.drug - Abstract
Aim of the study Acanthopanax senticosus Harms extract (ASE) is used as an ingredient of over-the-counter drugs and functional foods, such as health supplements, in Japan. ASE exhibits a hypoglycemic effect; however, the mechanism of the hypoglycemic effect is not clear. In the present study, we investigated whether ASE has a glucose absorption inhibitory action. Materials and methods We examined the effects of ASE on α-amylase and α-glucosidase activities, and on glucose uptake in Caco-2 cells. We also examined the effects of ASE oral administration on glucose tolerance in type 2 diabetes mellitus model db/db mice. Results The addition of ASE inhibited α-glucosidase activity but not α-amylase activity. The α-glucosidase inhibitory activity of ASE was approximately 1/13 of that of acarbose. The addition of ASE inhibited 2′-deoxy- d -glucose (DG) uptake in human intestinal Caco-2 cells, and the inhibitory activity of ASE was approximately 1/40 of that of phloretin. Kinetic analysis of glucose uptake indicated that ASE has no effects on DG uptake through passive diffusion, but that ASE inhibits intracellular DG uptake chiefly by inhibiting transport via a glucose transporter. In the glucose tolerance study, db/db mice orally administered ASE for 3 days showed significantly lower plasma glucose level than the control group 30 min after sucrose loading, without affecting plasma insulin levels. In addition, ASE oral administration significantly inhibited α-glucosidase activity in the small intestine mucosa extirpated from the mice. Conclusion These findings indicate that ASE may be useful as an ingredient of functional foods to improve postprandial hyperglycemia and prevent type II diabetes mellitus.
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- 2010
5. Branched-Chain Amino Acid Catabolism in Exercise and Liver Disease
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Kazunori Mawatari, Taro Murakami, Juichi Sato, Hisamine Kobayashi, Mariko Obayashi, Yoshiharu Shimomura, Makoto Shiraki, Takashi Honda, and Robert A. Harris
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Nutrition and Dietetics ,Catabolism ,Kinase ,Liver Diseases ,Branched-chain amino acid ,Medicine (miscellaneous) ,Biology ,3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) ,Rats ,Enzyme Activation ,Dephosphorylation ,chemistry.chemical_compound ,Enzyme activator ,Liver ,chemistry ,Biochemistry ,Mitochondrial matrix ,Animals ,Humans ,Phosphorylation ,Leucine ,Exercise ,Amino Acids, Branched-Chain - Abstract
Branched-chain alpha-keto acid dehydrogenase (BCKDH) complex, the enzyme catalyst for the second step of the BCAA catabolic pathway, plays a central role in the regulation of BCAA catabolism. The activity of the complex is regulated by a covalent modification cycle in which phosphorylation by BCKDH kinase inactivates and dephosphorylation by BCKDH phosphatase activates the complex. Many studies suggest that control of the activity of the kinase is a primary determinant of the activity of the complex. The kinase exists at all times in the mitochondrial matrix space in two forms, with a large amount being free and a smaller amount bound rather tightly to the BCKDH complex. Only the bound form of the kinase appears to be catalytically active and, therefore, responsible for phosphorylation and inactivation of the complex. alpha-Ketoisocaproate, the transamination product of leucine and the most important known physiological inhibitor of BCKDH kinase, promotes release of the kinase from the complex. alpha-Chloroisocaproate, the analogue of leucine and the most potent known inhibitor of the kinase, is more effective than alpha-ketoisocaproate in promoting release of BCKDH kinase from the complex. Exercise and chronic liver disease (liver cirrhosis) likewise decrease the amount of the kinase bound to the complex in rat liver. The resulting activation of the BCKDH complex appears responsible for the increase in BCAA catabolism caused by exercise and liver cirrhosis. Our findings support the use of BCAA supplements for patients with liver cirrhosis.
- Published
- 2006
6. Diagnostic accuracy of glycohemoglobin A1c (HbA1c) for postprandial hyperglycemia was equivalent to that of fasting blood glucose
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Kiyoshi Shibata, Shinichi Goto, Isao Ohsawa, Juichi Sato, Shinkan Tokudome, Isao Iritani, and Sadao Suzuki
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Adult ,Blood Glucose ,Male ,medicine.medical_specialty ,Epidemiology ,Diagnostic accuracy ,Sensitivity and Specificity ,Gastroenterology ,Internal medicine ,Diabetes mellitus ,medicine ,Humans ,Cutoff ,False Positive Reactions ,Aged ,Glycated Hemoglobin ,Glucose tolerance test ,Anthropometry ,medicine.diagnostic_test ,business.industry ,Fasting ,Odds ratio ,Glucose Tolerance Test ,Middle Aged ,Postprandial Period ,medicine.disease ,Exact test ,Postprandial ,Endocrinology ,Diabetes Mellitus, Type 2 ,Hyperglycemia ,Female ,business ,Biomarkers - Abstract
To compare the sensitivity, specificity, and total accuracy of an HbA1c ofor =6.5% in the detection of hyperglycemia (PPHG) relative to those of a fasting blood glucose (FBG) ofor =7.0 mmol/L.A total of 6,010 subjects (2,987 men and 3,023 women) living or working in Kasugai, Japan, underwent a medical checkup at Kasugai City Medical Care Center between April 2001 and March 2002. For the 91 subjects who had either a FBG ofor =7.0 mmol/L or an HbA1c ofor =6.5%, a 75-g oral glucose tolerance test was performed to confirm or exclude PPHG. We calculated the true- and false-positive odds ratios to evaluate the sensitivity and specificity of HbA1c relative to FBG, and compared the overall accuracy by calculating the conditional relative odds ratio (CROR).Among the 91 subjects, the true- and false-positive odds ratios were 0.43 (95% CI 0.26-0.69) and 0.40 (0.13-1.27) (Fisher's exact test, P.090), respectively; the CROR was 1.07 (95% CI 0.30-3.75).Although the HbA1c test was marginally more specific but less sensitive than the FBG test, at the given cutoff points the accuracies of two tests were equivalent.
- Published
- 2005
7. Effects of sex, age and BMI on screening tests for impaired glucose tolerance
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Shoji Kawazu, Kishio Nanjo, Arimasa Hososako, Ken-ichi Suzuki, Mari Hirata, Shigeaki Sato, Kazuhiko Kotani, Kazuyo Tsushita, Isao Kamae, Juichi Sato, Takeshi Usui, Mioko Gomyo, Yutaka Seino, Makoto Tominaga, Yutaka Kiyohara, Hideshi Kuzuya, Hideyo Yoshinaga, Toshihide Yoshida, Yuzo Sato, Naoki Sakane, and Satoru Tsujii
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Adult ,Blood Glucose ,Male ,Aging ,medicine.medical_specialty ,Optimal cutoff ,endocrine system diseases ,Screening test ,Endocrinology, Diabetes and Metabolism ,Gastroenterology ,Body Mass Index ,Diabetes Complications ,Impaired glucose tolerance ,Endocrinology ,Diabetes mellitus ,Internal medicine ,Glucose Intolerance ,Diabetes Mellitus ,Internal Medicine ,medicine ,Humans ,Mass Screening ,Mass screening ,Glycated Hemoglobin ,Sex Characteristics ,Receiver operating characteristic ,business.industry ,nutritional and metabolic diseases ,Fasting ,General Medicine ,Middle Aged ,medicine.disease ,ROC Curve ,Female ,business ,Body mass index ,hormones, hormone substitutes, and hormone antagonists ,Sex characteristics - Abstract
The discriminating abilities of fasting plasma glucose (FPG) and HbA1c were compared on screening tests for impaired glucose tolerance (IGT) and IGT plus diabetes mellitus by the receiver operating characteristic (ROC) curve analysis. Furthermore, effects of sex, age and BMI were examined on sensitivity and specificity of the optimal cutoff points. This study included 997 subjects who were recruited for 75 g OGTT after the first screening of the Japan Diabetes Prevention Program. According to the 1997 criteria of the American Diabetes Association (ADA), 140 subjects were classified as diabetic and 256 as IGT. The areas under the ROC curves of FPG were significantly larger than those of HbA1c. The optimal cutoff points of FPG were 102 mg/dl for IGT and 105 mg/dl for IGT plus diabetes mellitus. Those of HbA1c were both 5.3%. In screening with FPG, females had significantly lower sensitivity and higher specificity than males, and the specificity for IGT plus diabetes mellitus was the lowest in the obese group. In screening with HbA1c, the specificity was low in the older and the obese groups. We concluded that FPG was superior to HbA1c for screening of IGT and IGT plus diabetes mellitus and the optimal cutoff point of FPG would be 102 mg/dl or greater.
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- 2004
8. Effect of insulin on cephalexin uptake and transepithelial transport in the human intestinal cell line Caco-2
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Kazuhiro Watanabe, Toshiya Jinriki, Juichi Sato, and Kazuaya Terada
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Cephalexin ,medicine.medical_specialty ,Dose-Response Relationship, Drug ,Insulin ,medicine.medical_treatment ,Pharmaceutical Science ,Biological Transport ,Membrane transport ,Biology ,Apical membrane ,Intestinal absorption ,Endocrinology ,Intestinal Absorption ,Intestinal mucosa ,Caco-2 ,Internal medicine ,medicine ,Humans ,Caco-2 Cells ,Intestinal Mucosa ,Intracellular ,Antibacterial agent - Abstract
We investigated whether cephalexin transport in Caco-2 cells is regulated by insulin. After the insulin pretreatment, cephalexin uptake, and transport as well as PEPT1 mRNA and protein expression in the cells were measured. Cephalexin uptake was significantly increased by the insulin pretreatment. Insulin significantly increased cephalexin saturable uptake, but had no significant effect on the non-saturable one. PEPT1 protein expression on the apical membrane, but not PEPT1 mRNA expression, was increased by the insulin pretreatment. The enhancement of cephalexin uptake by the insulin pretreatment was inhibited by genistein, a tyrosine kinase inhibitor, and colchicine, an agent that disrupts protein translocation. Apical-to-basolateral transport of cephalexin has increased by the insulin pretreatment at the apical side and long-term insulin pretreatment at the basolateral side. It is considered that insulin mainly binds to its receptor on the apical and basolateral membranes, thereby promoting PEPT1 translocation from the intracellular pool to the apical membrane surface; consequently, PEPT1 protein expression on the apical membrane is increased.
- Published
- 2004
9. Starvation Increases the Amount of Pyruvate Dehydrogenase Kinase in Several Mammalian Tissues
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Juichi Sato, Kirill M. Popov, Jerzy Jaskiewicz, Paul V. Blair, Robert A. Harris, and Pengfei Wu
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Male ,Pyruvate dehydrogenase kinase ,Biophysics ,PDK4 ,Adipose tissue ,Mitochondria, Liver ,White adipose tissue ,Protein Serine-Threonine Kinases ,Pyruvate dehydrogenase phosphatase ,Biology ,Kidney ,Biochemistry ,Gene Expression Regulation, Enzymologic ,Mammary Glands, Animal ,Pregnancy ,Brown adipose tissue ,medicine ,Animals ,Tissue Distribution ,RNA, Messenger ,Rats, Wistar ,Molecular Biology ,Starvation ,Brain ,Pyruvate Dehydrogenase Acetyl-Transferring Kinase ,Pyruvate dehydrogenase complex ,Rats ,Isoenzymes ,Glucose ,medicine.anatomical_structure ,Female ,medicine.symptom ,Protein Kinases - Abstract
Covalent modification of the pyruvate dehydrogenase complex provides an important regulatory mechanism for controlling the disposal of glucose and other compounds metabolized to pyruvate. Regulation of the complex by this mechanism is achieved in part by tissue-specific expression of the genes encoding isoenzymes of pyruvate dehydrogenase kinase (PDK). Starvation is known from our previous work to increase PDK activity of heart and skeletal muscle by increasing the amount of PDK isoenzyme 4 (PDK4) present in these tissues. This study demonstrates that increased expression of both PDK4 and PDK2 occurs in rat liver, kidney, and lactating mammary gland in response to starvation. PDK4 and PDK2 message levels were also increased by starvation in the two tissues examined (liver and kidney), suggesting enhancement of gene transcription. Changes in PDK2 message and protein were of similar magnitude, but changes in PDK4 message were greater than those in PDK4 protein, suggesting regulation at the level of translation. In contrast to these tissues, starvation had little or no effect on PDK2 and PDK4 protein in brain, white adipose tissue, and brown adipose tissue. Nevertheless, PDK4 message levels were significantly increased in brain and white adipose tissue by starvation. The findings of this study indicate that increased expression of PDK isoenzymes is an important mechanism for bringing about inactivation of the pyruvate dehydrogenase complex during starvation in many but not all tissues of the body. The absence of this mechanism preserves the capacity of neuronal tissue to utilize glucose for energy during starvation.
- Published
- 2000
10. Studies on the regulation of the mitochondrial α-ketoacid dehydrogenase complexes and their kinases
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Juichi Sato, Yu Zhao, Kirill M. Popov, Jerzy Jaskiewicz, Robert A. Harris, Yoshiharu Shimomura, Thomas D. Hurley, and John W. Hawes
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Models, Molecular ,Pyruvate decarboxylation ,Cancer Research ,Pyruvate dehydrogenase kinase ,Protein Conformation ,Molecular Sequence Data ,Mitochondria, Liver ,Pyruvate Dehydrogenase Complex ,Protein Serine-Threonine Kinases ,Biology ,Pyruvate dehydrogenase phosphatase ,3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) ,Multienzyme Complexes ,Genetics ,Animals ,Amino Acid Sequence ,Phosphorylation ,Dihydrolipoyl transacetylase ,Molecular Biology ,Binding Sites ,Pyruvate Dehydrogenase Acetyl-Transferring Kinase ,Ketone Oxidoreductases ,Pyruvate dehydrogenase complex ,Recombinant Proteins ,Diet ,Rats ,Citric acid cycle ,Biochemistry ,Mutation ,Molecular Medicine ,Thiamine Pyrophosphate ,Branched-chain alpha-keto acid dehydrogenase complex ,Oxoglutarate dehydrogenase complex ,Protein Kinases - Abstract
Five mitochondrial protein kinases, all members of a new family of protein kinases, have now been identified, cloned, expressed as recombinant proteins, and partially characterized with respect to catalytic and regulatory properties. Four members of this unique family of eukaryotic protein kinases correspond to pyruvate dehydrogenase kinase isozymes which regulate the activity of the pyruvate dehydrogenase complex, an important regulatory enzyme at the interface between glycolysis and the citric acid cycle. The fifth member of this family corresponds to the branched-chain alpha-ketoacid dehydrogenase kinase, an enzyme responsible for phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the most important regulatory enzyme in the pathway for the disposal of branched-chain amino acids. At least three long-term control mechanisms have evolved to conserve branched chain amino acids for protein synthesis during periods of dietary protein insufficiency. Increased expression of the branched-chain alpha-ketoacid dehydrogenase kinase is perhaps the most important because this leads to phosphorylation and nearly complete inactivation of the liver branched-chain alpha-ketoacid dehydrogenase complex. Decreased amounts of the liver branched-chain alpha-ketoacid dehydrogenase complex secondary to a decrease in liver mitochondria also decrease the liver's capacity for branched-chain keto acid oxidation. Finally, the number of E1 subunits of the branched-chain alpha-ketoacid dehydrogenase complex is reduced to less than a full complement of 12 heterotetramers per complex in the liver of protein-starved rats. Since the E1 component is rate-limiting for activity and also the component of the complex inhibited by phosphorylation, this decrease in number further limits overall enzyme activity and makes the complex more sensitive to regulation by phosphorylation in this nutritional state. The branched-chain alpha-ketoacid dehydrogenase kinase phosphorylates serine 293 of the E1 alpha subunit of the branched-chain alpha-ketoacid dehydrogenase complex. Site-directed mutagenesis of amino acid residues surrounding serine 293 reveals that arginine 288, histidine 292 and aspartate 296 are critical to dehydrogenase activity, that histidine 292 is critical to binding the coenzyme thiamine pyrophosphate, and that serine 293 exists at or in close proximity to the active site of the dehydrogenase. Alanine scanning mutagenesis of residues in the immediate vicinity of the phosphorylation site (serine 293) indicates that only arginine 288 is required for recognition of serine 293 as a phosphorylation site by the branched-chain alpha-ketoacid dehydrogenase kinase. Phosphorylation appears to inhibit dehydrogenase activity by introducing a negative charge directly into the active site pocket of the E1 dehydrogenase component of the branched-chain alpha-ketoacid dehydrogenase complex. A model based on the X-ray crystal structure of transketolase is being used to predict residues involved in thiamine pyrophosphate binding and to help visualize how phosphorylation within the channel leading to the reactive carbon of thiamine pyrophosphate inhibits catalytic activity. The isoenzymes of pyruvate dehydrogenase kinase differ greatly in terms of their specific activities, kinetic parameters and regulatory properties. Chemically-induced diabetes in the rat induces significant changes in the pyruvate dehydrogenase kinase isoenzyme 2 in liver. Preliminary findings suggest hormonal control of the activity state of the pyruvate dehydrogenase complex may involves tissue specific induced changes in expression of the pyruvate dehydrogenase kinase isoenzymes.
- Published
- 1997
11. Simple, rapid and sensitive reversed-phase high-performance liquid chromatographic method for the determination of mefenamic acid in plasma
- Author
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Yuichi Niida, Keiji Ito, Akio Wakamatsu, Juichi Sato, Masao Umetsu, and Eiji Owada
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Chromatography ,Mefenamic acid ,Chemistry ,Infant, Newborn ,General Chemistry ,Plasma ,Plasma levels ,Reversed-phase chromatography ,High-performance liquid chromatography ,Mefenamic Acid ,Phase (matter) ,Recien nacido ,Blood plasma ,medicine ,Humans ,Spectrophotometry, Ultraviolet ,Ductus Arteriosus, Patent ,Chromatography, High Pressure Liquid ,Infant, Premature ,medicine.drug - Abstract
Measurement of plasma levels mefenamic acid MA by a high-performance liquid chromatographic method adapted for monitoring plasma MA in infants between sub-therapeutic and overdose levels using a small amount of plasma
- Published
- 1989
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