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dc.contributor.advisorMichael W. Martin
dc.creatorSchafer, Grant D.
dc.date.accessioned2019-08-22T19:57:59Z
dc.date.available2019-08-22T19:57:59Z
dc.date.issued2002-06-01T00:00:00-07:00
dc.date.submitted2014-03-31T08:48:16-07:00
dc.identifier.urihttps://hdl.handle.net/20.500.12503/27425
dc.description.abstractSchafer, Grant D., Osmoregulatory Alterations in Taurine Uptake by Cultured Human and Bovine Lens Epithelial Cells. Master of Science (Biomedical Sciences), July, 2002, 47 pp., 3 tables, 12 figures, bibliography, 43 titles. Purpose. Using cultured human lens epithelial cells (HLECs) and bovine lens epithelial cells (BLECs) and the nature of the relationship between taurine-concentrating capability and intracellular polyol accumulation or extracellular hypertonicity. Methods. The kinetic characteristics of taurine accumulation based upon the measurement in vitro [3H]-taurine uptake were compared in cultured HLECs and BLECs pre-exposed to either galactose-supplemented medium or extracellular hypertonicity. Results: The capacity to accumulate [3H]-taurine was significantly lowered after chronic (20 hour) incubation of cultured BLECs in 40 mmol/l galactose in contrast to HLECs. Inhibition of the intracellular taurine transport site appeared to be noncompetitive as there was a marked reduction in the Vmax without significant alteration in the Km. Galactitol content in BLECs exceeded five times that found in HLECs. The coadministration of the aldose reductase inhibitor, sorbinil with 40 mmol/l galactose completely prevented the inhibitory effect of galactose on [3H]-taurine uptake. Acute expression (3 hours) of HLECs and BLECs to a range of 10 to 40 mmol/l galactitol or 10 to 40 mmol/l galactose plus sorbinil-supplemented medium suggested by Dixon plot analysis that neither galactitol nor galactose interacted with the extracellular taurine transport site. In contrast, [3H]-taurine accumulation was markedly elevated in both HLECs and BLECs after chronic exposure to galactose-free medium made hyperosmotic by supplementation with sodium chloride. The enhanced taurine uptake capacity involved an increase in Vmax without significant change in the Km value. Conclusions: These results demonstrate lens epithelial cells express a taurine transporter protein capable of active uptake but predisposed to inhibition by intracellular galactitol when the sugar alcohol is present in high enough concentration to interfere with cell metabolism. Furthermore, lens epithelial cells respond to hypertonic stress by raising taurine transport activity.
dc.format.mimetypeapplication/pdf
dc.language.isoen
dc.subjectCell Anatomy
dc.subjectCell and Developmental Biology
dc.subjectCell Biology
dc.subjectCells
dc.subjectCellular and Molecular Physiology
dc.subjectChemicals and Drugs
dc.subjectDevelopmental Biology
dc.subjectEye Diseases
dc.subjectLife Sciences
dc.subjectMedical Cell Biology
dc.subjectMedical Sciences
dc.subjectMedicine and Health Sciences
dc.subjectOphthalmology
dc.subjectOptometry
dc.subjectOther Cell and Developmental Biology
dc.subjectSense Organs
dc.subjectVision Science
dc.subjectOsmoregulatory alterations
dc.subjecttaurine uptake
dc.subjectcultured human lens epithelial cells
dc.subjectbovine lens epithelial cells
dc.subjectbiomedical sciences
dc.subjectHLECs
dc.subjectBLECs
dc.subjectin vitro taurine uptake
dc.subjectgalactose-supplemented medium
dc.subjectextracellular hypertonicity
dc.subjectgalactitol content
dc.subjectaldose reductase inhibitor
dc.subjectsorbinil
dc.subjectDixon plot analysis
dc.subjectchronic exposure
dc.subjectcell metabolism
dc.subjectsugar alcohol
dc.subjecthypertonic stress
dc.subjecttaurine transport activity
dc.titleOsmoregulatory Alterations in Taurine Uptake by Cultured Human and Bovine Lens Epithelial Cells
dc.typeThesis
thesis.degree.departmentGraduate School of Biomedical Sciences
thesis.degree.disciplineBiomedical Sciences
thesis.degree.grantorUniversity of North Texas Health Science Center at Fort Worth
thesis.degree.nameMaster of Science
dc.contributor.committeeMemberNeeraj Agarwal
dc.type.materialtext
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