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

Sung Baek Hong; Kwang Won Lee; James T. Handa; Choun Ki Joo

doi:10.1006/bbrc.2000.3245

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

Sung Baek Hong, Kwang Won Lee, James T. Handa, Choun Ki Joo

Research output: Contribution to journal › Article › peer-review

36 Citations (Scopus)

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 α-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. (C) 2000 Academic Press.

Original language	English
Pages (from-to)	53-59
Number of pages	7
Journal	Biochemical and biophysical research communications
Volume	275
Issue number	1
DOIs	https://doi.org/10.1006/bbrc.2000.3245
Publication status	Published - 2000 Aug 18
Externally published	Yes

Bibliographical note

Funding Information:
The authors thank Dr. B. Ortwerth, University of Missouri, Department Ophthalmology, Columbia, Missouri for valuable comments and critical review of the manuscript, and H.-K. Park, S. J. Lee, and J.-H. Kim for their technical assistance. This research was funded by National Resech Laboratory grant from Ministry of Science and Technology of Korea.

Keywords

AGEs
Bovine lens explants
Cataracts
Extracellular matrix
Fibrosis
Glycation
RAGE
Transdifferentiation

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1006/bbrc.2000.3245

Cite this

@article{b74f605d96564db38b05df4f674a31c1,

title = "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 α-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. (C) 2000 Academic Press.",

keywords = "AGEs, Bovine lens explants, Cataracts, Extracellular matrix, Fibrosis, Glycation, RAGE, Transdifferentiation",

author = "Hong, {Sung Baek} and Lee, {Kwang Won} and Handa, {James T.} and Joo, {Choun Ki}",

note = "Funding Information: The authors thank Dr. B. Ortwerth, University of Missouri, Department Ophthalmology, Columbia, Missouri for valuable comments and critical review of the manuscript, and H.-K. Park, S. J. Lee, and J.-H. Kim for their technical assistance. This research was funded by National Resech Laboratory grant from Ministry of Science and Technology of Korea.",

year = "2000",

month = aug,

day = "18",

doi = "10.1006/bbrc.2000.3245",

language = "English",

volume = "275",

pages = "53--59",

journal = "Biochemical and biophysical research communications",

issn = "0006-291X",

publisher = "Elsevier B.V.",

number = "1",

}

TY - JOUR

T1 - Effect of advanced glycation end products on lens epithelial cells in vitro

AU - Hong, Sung Baek

AU - Lee, Kwang Won

AU - Handa, James T.

AU - Joo, Choun Ki

N1 - Funding Information: The authors thank Dr. B. Ortwerth, University of Missouri, Department Ophthalmology, Columbia, Missouri for valuable comments and critical review of the manuscript, and H.-K. Park, S. J. Lee, and J.-H. Kim for their technical assistance. This research was funded by National Resech Laboratory grant from Ministry of Science and Technology of Korea.

PY - 2000/8/18

Y1 - 2000/8/18

N2 - 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 α-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. (C) 2000 Academic Press.

AB - 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 α-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. (C) 2000 Academic Press.

KW - AGEs

KW - Bovine lens explants

KW - Cataracts

KW - Extracellular matrix

KW - Fibrosis

KW - Glycation

KW - RAGE

KW - Transdifferentiation

UR - http://www.scopus.com/inward/record.url?scp=0034683040&partnerID=8YFLogxK

U2 - 10.1006/bbrc.2000.3245

DO - 10.1006/bbrc.2000.3245

M3 - Article

C2 - 10944440

AN - SCOPUS:0034683040

SN - 0006-291X

VL - 275

SP - 53

EP - 59

JO - Biochemical and biophysical research communications

JF - Biochemical and biophysical research communications

IS - 1

ER -

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this