Effects of advanced glycation end product modification on proximal tubule
epithelial cell processing of albumin.
Authors Ozdemir AM, Hopfer U, Rosca MV, Fan XJ, Monnier VM, Weiss MF
Submitted By Submitted Externally on 10/1/2015
Status Published
Journal American journal of nephrology
Year 2008
Date Published
Volume : Pages 28 : 14 - 24
PubMed Reference 17890854
Abstract The goal of this work is to understand the cellular effects of advanced
glycation end product (AGE)-modified protein on renal proximal tubule cells., 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., 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., 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., 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.

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