6 results on '"VanTol A"'
Search Results
2. Cloning and molecular characterization of the glucose transporter 1 in tilapia (Oreochromis niloticus)
- Author
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Carol M. Morrison, Brenna vanTol, Olga Hrytsenko, Bill Pohajdak, James R. Wright, and Bao-You Xu
- Subjects
Untranslated region ,Molecular Sequence Data ,Biology ,Nile tilapia ,Endocrinology ,Complementary DNA ,Gene expression ,Animals ,Amino Acid Sequence ,Cloning, Molecular ,Promoter Regions, Genetic ,Peptide sequence ,chemistry.chemical_classification ,Glucose Transporter Type 1 ,Base Sequence ,Reverse Transcriptase Polymerase Chain Reaction ,Gene Expression Profiling ,Glucose transporter ,Blotting, Northern ,biology.organism_classification ,Molecular biology ,Amino acid ,Blotting, Southern ,Oreochromis ,Gene Expression Regulation ,Biochemistry ,chemistry ,Animal Science and Zoology ,Sequence Alignment ,Tilapia - Abstract
Facilitative glucose transporters (GLUTs) are responsible for passively transporting monosaccharides across the plasma membrane. We sequenced and characterized the Nile tilapia (Oreochromis niloticus) GLUT-1 (tGLUT-1) cDNA and genomic DNA. Using rapid amplification of the cDNA ends (RACE), two tGLUT-1 transcripts were detected differing in the length of the 3' untranslated region, 2851 and 4577 bp. Translated tGLUT-1 is a 490 amino acid product, which shares 74% homology with that of humans. Computer analysis of the amino acid sequence predicted 12 transmembrane domains, which are conserved in the GLUT-1 of various species. The tGLUT-1 gene spans more than 11 kb, and similar to the mammalian GLUT-1 genes has a 10 exon, 9 intron organization. Potential promoter regulatory elements have some similarity to those recorded for human, mouse, and rat GLUT-1 genes. Tissue expression studies revealed both GLUT-1 transcripts in liver, Brockmann bodies (BB), heart, small intestine, adipose tissue, white and red muscle, gill, spleen, pituitary gland, and brain. The highest level of expression was detected in tilapia heart, followed by BB, brain, and muscle. Protein based food and glucose had minor or no effects on the level of tGLUT-1 expression in most tissues. The tGLUT-1 mRNA level was significantly induced by glucose and food only in white muscle. Current results suggest that tGLUT-1 is similar to the GLUT-1 of other teleost species and mammals at the genomic, mRNA, and amino acid levels, supporting the concept that tGLUT-1 functions as a ubiquitous basal level glucose transporter.
- Published
- 2010
3. Contribution of KCNQ1 to the regulatory volume decrease in the human mammary epithelial cell line MCF-7
- Author
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Paul Linsdell, Shasta Moser, Sergey Missan, William H. Baldridge, Julie Crack, Brenna vanTol, and Elizabeth A. Cowley
- Subjects
medicine.medical_specialty ,Physiology ,Mammary gland ,Breast Neoplasms ,Adenocarcinoma ,Biology ,Membrane Potentials ,Osmotic Pressure ,Cell Line, Tumor ,Internal medicine ,medicine ,Humans ,Osmotic pressure ,RNA, Messenger ,Mammary Glands, Human ,Cell Polarity ,Epithelial Cells ,Extracellular Fluid ,Cell Biology ,Water-Electrolyte Balance ,medicine.disease ,Potassium channel ,Epithelium ,Cell biology ,medicine.anatomical_structure ,Endocrinology ,Hypotonic Solutions ,MCF-7 ,Potassium Channels, Voltage-Gated ,Cell culture ,KCNQ1 Potassium Channel ,Mutagenesis, Site-Directed ,Potassium ,Isotonic Solutions - Abstract
Using the human mammary epithelial cell line MCF-7, we have investigated volume-activated changes in response to hyposmotic stress. Switching MCF-7 cells from an isosmotic to a hyposmotic solution resulted in an initial cell swelling response, followed by a regulatory volume decrease (RVD). This RVD response was inhibited by the nonselective K+ channel inhibitors Ba2+, quinine, and tetraethylammonium chloride, implicating K+ channel activity in this volume-regulatory mechanism. Additional studies using chromonol 293B and XE991 as inhibitors of the KCNQ1 K+ channel, and also a dominant-negative NH2-terminal truncated KCNQ1 isoform, showed complete abolition of the RVD response, suggesting that KCNQ1 plays an important role in regulation of cell volume in MCF-7 cells. We additionally confirmed that KCNQ1 mRNA and protein is expressed in MCF-7 cells, and that, when these cells are cultured as a polarized monolayer, KCNQ1 is located exclusively at the apical membrane. Whole cell patch-clamp recordings from MCF-7 cells revealed a small 293B-sensitive current under hyposmotic, but not isosmotic conditions, while recordings from mammalian cells heterologously expressing KCNQ1 alone or KCNQ1 with the accessory subunit KCNE3 reveal a volume-sensitive K+ current, inhibited by 293B. These data suggest that KCNQ1 may play important physiological roles in the mammary epithelium, regulating cell volume and potentially mediating transepithelial K+ secretion.
- Published
- 2007
4. Cholesteryl Ester Transfer Protein Gene Polymorphism Is a Determinant of HDL Cholesterol and of the Lipoprotein Response to a Lipid-Lowering Diet in Type 1 Diabetes
- Author
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A vanTol, BK Stulp, Klaas Hoogenberg, SC Riemens, Robin P. F. Dullaart, Jem Groener, and Willem Sluiter
- Subjects
Adult ,Male ,Apolipoprotein E ,Heterozygote ,medicine.medical_specialty ,Very low-density lipoprotein ,Apolipoprotein B ,Lipoproteins ,Endocrinology, Diabetes and Metabolism ,Cholesterol, Dietary ,Linoleic Acid ,chemistry.chemical_compound ,High-density lipoprotein ,Dietary Fats, Unsaturated ,Internal medicine ,Cholesterylester transfer protein ,Internal Medicine ,medicine ,Humans ,Alleles ,Triglycerides ,Glycoproteins ,Polymorphism, Genetic ,Apolipoprotein A-I ,biology ,Cholesterol ,Cholesterol, HDL ,Homozygote ,Smoking ,Middle Aged ,Cholesterol Ester Transfer Proteins ,Diabetes Mellitus, Type 1 ,Endocrinology ,chemistry ,biology.protein ,Female ,lipids (amino acids, peptides, and proteins) ,Gene polymorphism ,Carrier Proteins ,Lipoprotein - Abstract
The TaqlB cholesteryl ester transfer protein (CETP) gene polymorphism (B1B2) is a determinant of HDL cholesterol in nondiabetic populations. Remarkably, this gene effect appears to be modified by environmental factors. We evaluated the effect of this polymorphism on HDL cholesterol levels and on the lipoprotein response to a linoleic acid-enriched, low-cholesterol diet in patients with type 1 diabetes. In 44 consecutive type 1 diabetic patients (35 men), CETP polymorphism, apolipoprotein (apo) E genotype, serum lipoproteins, serum CETP activity (measured with an exogenous substrate assay, n = 30), clinical variables, and a diet history were documented. The 1-year response to diet was assessed in 14 type 1 diabetic patients, including 6 B1B1 and 6 B1B2 individuals. HDL cholesterol was higher in 10 B2B2 than in 14 B1B1 homozygotes (1.63 ± 0.38 vs. 1.24 ± 0.23 mmol/l, P < 0.01). HDL cholesterol, adjusted for triglycerides and smoking, was 0.19 mmol/l higher for each B2 allele present. CETP activity levels were not significantly different between CETP genotypes. Multiple regression analysis showed that VLDL + LDL cholesterol was associated with dietary polyunsaturated: saturated fatty acids ratio (P < 0.02) and total fat intake (P < 0.05) in the B1B1 homozygotes only and tended to be related to the presence of the apo E4 allele (P < 0.10). In response to diet, VLDL + LDL cholesterol fell (P < 0.05) and HDL cholesterol remained unchanged in 6 B1B1 homozygotes. In contrast, VLDL + LDL cholesterol was unaltered and HDL cholesterol decreased (P < 0.05) in 6 B1B2 heterozygotes (P < 0.05 for difference in change in VLDL + LDL/HDL cholesterol ratio). This difference in response was unrelated to the apo E genotype. Thus, the TaqlB CETP gene polymorphism is a strong determinant of HDL cholesterol in type 1 diabetes. This gene effect is unlikely to be explained by a major influence on the serum level of CETP activity, as an indirect measure of CETP mass. Our preliminary data suggest that this polymorphism may be a marker of the lipoprotein response to dietary intervention.
- Published
- 1997
5. Pharmacological separation of hEAG and hERG K+ channel function in the human mammary carcinoma cell line MCF-7
- Author
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Paul Linsdell, Jonathan Blay, Brenna vanTol, Jeremy Roy, and Elizabeth A. Cowley
- Subjects
congenital, hereditary, and neonatal diseases and abnormalities ,Cancer Research ,ERG1 Potassium Channel ,Imipramine ,Pyridines ,Cell ,hERG ,Breast Neoplasms ,Pharmacology ,Adenocarcinoma ,Piperidines ,Anti-Allergic Agents ,medicine ,Tumor Cells, Cultured ,Humans ,Channel blocker ,RNA, Messenger ,Ion channel ,Cell Proliferation ,Cell Size ,biology ,Cell growth ,business.industry ,Reverse Transcriptase Polymerase Chain Reaction ,General Medicine ,Cell cycle ,Astemizole ,Potassium channel ,Ether-A-Go-Go Potassium Channels ,Long QT Syndrome ,medicine.anatomical_structure ,Oncology ,biology.protein ,business ,Anti-Arrhythmia Agents ,medicine.drug - Abstract
Pharmacological inhibitors of the human ether-ago-go (hEAG) potassium channel, astemizole and imipramine, have been used to demonstrate that hEAG plays a role in cancer cell proliferation. Astemizole and imipramine are, however, relatively non-specific ion channel blockers, as astemizole can also block the related potassium channel, human ether-a-go-go-related (hERG). Therefore, we aimed to determine the molecular target of astemizole, in the human mammary carcinoma cell line MCF-7. We initially confirmed the expression of KCNH1 and KCNH2 mRNA and hEAG and hERG channel protein in MCF-7 cells. Using a [ 3 H]-thymidine incorporation assay we determined that astemizole inhibited MCF-7 cell proliferation, whereas the hERG-specific channel blocker E-4031 had no effect. We then determined that E-4031 inhibited the regulatory volume decrease (RVD) observed in these cells following exposure to hypotonic solutions, confirming that functional hERG channels are present and may be important for cell volume regulation in MCF-7 cells. Our results suggest, for the first time, that hERG is involved in cell volume regulation. In addition, the function of hEAG and hERG in MCF-7 cell proliferation can be separated pharmacologically by utilizing the channel inhibitors astemizole and E-4031. The hEAG channel function in MCF-7 cells appears to be involved in the regulation of cell proliferation, whereas hERG is involved in cell volume regulation.
- Published
- 2008
6. Factors influencing hepatic glutathione concentrations: a study in surgical patients
- Author
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E. C. P. Shi, John M. Ham, Margaret Rose, Rebecca Vantol, R. Fisher, and Maeve McEvoy
- Subjects
Adult ,Male ,Risk ,medicine.medical_specialty ,Pathology ,Adolescent ,Reference range ,Biology ,Gastroenterology ,Protein-Energy Malnutrition ,chemistry.chemical_compound ,Liver Function Tests ,Hepatic glutathione ,Internal medicine ,medicine ,Humans ,Aged ,medicine.diagnostic_test ,Potential risk ,Histology ,General Medicine ,Glutathione ,Middle Aged ,chemistry ,Liver ,Liver biopsy ,Surgical Procedures, Operative ,Female ,Liver function ,Surgical patients - Abstract
1. Hepatic total glutathione (reduced plus oxidized) and oxidized glutathione levels were measured in operative wedge liver biopsy specimens obtained from 70 patients. 2. The effects on hepatic reduced glutathione (GSH) level of four potential risk factors (abnormal liver histology, abnormal preoperative tests of liver function, drug ingestion and protein malnutrition) were examined. 3. Each of the four risk factors was associated with a significant reduction in hepatic GSH. Multivariate analysis indicated that only three of these risk factors (abnormal liver histology, drug ingestion and protein malnutrition) had independent effects in reducing hepatic GSH. 4. Twenty-five of the 70 patients studied did not have any of the four risk factors. The mean hepatic GSH level in these patients was 3.92 μmol/g of liver wet weight (sd 0.62), giving a 95% reference range of 2.71–5.14 μmol/g of liver wet weight.
- Published
- 1982
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