Effect of advanced glycation end products on lens epithelial cells in vitro.

Abstract:

:The extended exposure of proteins to reducing sugars leads to nonenzymatic glycation with the accumulation of advanced glycation end products (AGEs). Long-lived proteins, such as collagen and crystallins, are subjected to this modification, and are implicated as causal factors in several diseases including diabetic complications, cataracts, and arteriosclerosis. One means through which AGEs modulate cellular interactions is via binding to specific receptors. In the current study, the existence of AGEs in human anterior polar lens capsules of cataracts was confirmed using a combination of dot-immunoblot and fluorescent detection. Human lens epithelial cells (LECs) attached to anterior lens capsules expressed mRNA for the receptor for AGEs (RAGE). The interaction of LECs with AGEs using bovine lens epithelial explants demonstrated that AGEs induced mRNAs and proteins of fibronectin, collagen type I, aberrant extracellular matrix proteins, and alpha-SMA, a specific marker for myofibroblastic cells. These findings suggest that AGEs may alter cellular functions which induce mRNAs and proteins associated with fibrosis in LECs.

authors

Hong SB,Lee KW,Handa JT,Joo CK

doi

10.1006/bbrc.2000.3245

subject

Has Abstract

pub_date

2000-08-18 00:00:00

pages

53-9

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(00)93245-5

journal_volume

275

pub_type

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