دورية أكاديمية
Effects of advanced glycation end product modification on proximal tubule epithelial cell processing of albumin.
| العنوان: | Effects of advanced glycation end product modification on proximal tubule epithelial cell processing of albumin. |
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| المؤلفون: | Ozdemir AM; Department of Pathology, Case Western Reserve University, Cleveland, Ohio, USA., Hopfer U, Rosca MV, Fan XJ, Monnier VM, Weiss MF |
| المصدر: | American journal of nephrology [Am J Nephrol] 2008; Vol. 28 (1), pp. 14-24. Date of Electronic Publication: 2007 Sep 20. |
| نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Karger Country of Publication: Switzerland NLM ID: 8109361 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1421-9670 (Electronic) Linking ISSN: 02508095 NLM ISO Abbreviation: Am J Nephrol Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Basel ; New York : Karger, [1981- |
| مواضيع طبية MeSH: | Diabetic Nephropathies/*metabolism , Glycation End Products, Advanced/*metabolism , Kidney Tubules, Proximal/*metabolism , Pyruvaldehyde/*pharmacokinetics , Serum Albumin, Bovine/*pharmacokinetics, Cell Line, Transformed ; Diabetic Nephropathies/pathology ; Epithelial Cells/cytology ; Epithelial Cells/metabolism ; Fluorescein-5-isothiocyanate ; Fluorescent Dyes ; Humans ; Kidney Tubules, Proximal/cytology ; Microscopy, Confocal |
| مستخلص: | Aim: The goal of this work is to understand the cellular effects of advanced glycation end product (AGE)-modified protein on renal proximal tubule cells. Background: A major function of the proximal tubule is to reabsorb and process filtered proteins. Diabetes is characterized by increased quantities of tissue and circulating proteins modified by AGEs. Therefore in diabetes, plasma proteins filtered at the glomerulus and presented to the renal proximal tubule are likely to be highly modified by AGEs. Methods: The model system was electrically resistant polarized renal proximal tubular epithelial cells in monolayer culture. The model proteins comprise a well-characterized AGE, methylglyoxal-modified bovine serum albumin (MGO-BSA), and unmodified BSA. Results: Renal proximal tubular cells handle MGO-BSA and native BSA in markedly disparate ways, including differences in: (1) kinetics of binding, uptake, and intracellular accumulation, (2) processing and fragmentation, and (3) patterns of electrical conductance paralleling temporal changes in binding, uptake and processing. Conclusion: These differences support the idea that abnormal protein processing by the renal tubule can be caused by abnormal proteins, thereby forging a conceptual link between the pathogenic role of AGEs and early changes in tubular function that can lead to hypertrophy and nephropathy in diabetes. ((c) 2007 S. Karger AG, Basel.) |
| معلومات مُعتمدة: | DK45619 United States DK NIDDK NIH HHS; DK57733 United States DK NIDDK NIH HHS; ES11461 United States ES NIEHS NIH HHS; P30 CA43703-12 United States CA NCI NIH HHS |
| المشرفين على المادة: | 0 (Fluorescent Dyes) 0 (Glycation End Products, Advanced) 27432CM55Q (Serum Albumin, Bovine) 722KLD7415 (Pyruvaldehyde) I223NX31W9 (Fluorescein-5-isothiocyanate) |
| تواريخ الأحداث: | Date Created: 20070925 Date Completed: 20071213 Latest Revision: 20171116 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1159/000108757 |
| PMID: | 17890854 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1421-9670 |
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| DOI: | 10.1159/000108757 |