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Title: Advanced glycation end products impair function of late endothelial progenitor cells through effects on protein kinase Akt and cyclooxygenase-2

Abstract

Endothelial progenitor cells (EPCs) exhibit impaired function in the context of diabetes, and advanced glycation end products (AGEs), which accumulate in diabetes, may contribute to this. In the present study, we investigated the mechanism by which AGEs impair late EPC function. EPCs from human umbilical cord blood were isolated, and incubated with AGE-modified albumin (AGE-albumin) at different concentrations found physiologically in plasma. Apoptosis, migration, and tube formation assays were used to evaluate EPC function including capacity for vasculogenesis, and expression of the receptor for AGEs (RAGE), Akt, endothelial nitric oxide synthase (eNOS), and cycloxygenase-2 (COX-2) were determined. Anti-RAGE antibody was used to block RAGE function. AGE-albumin concentration-dependently enhanced apoptosis and depressed migration and tube formation, but did not affect proliferation, of late EPCs. High AGE-albumin increased RAGE mRNA and protein expression, and decreased Akt and COX-2 protein expression, whilst having no effect on eNOS mRNA or protein in these cells. These effects were inhibited by co-incubation with anti-RAGE antibody. These results suggest that RAGE mediates the AGE-induced impairment of late EPC function, through down-regulation of Akt and COX-2 in these cells.

Authors:
; ; ;  [1]
  1. Department of Cardiology, Drum Tower Hospital, Nanjing University Medical School, 321 Zhongshan Road, Nanjing 210008 (China)
Publication Date:
OSTI Identifier:
21255955
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 381; Journal Issue: 2; Other Information: DOI: 10.1016/j.bbrc.2009.02.040; PII: S0006-291X(09)00271-X; Copyright (c) 2009 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ALBUMINS; ANTIBODIES; APOPTOSIS; BLOOD PLASMA; CELL PROLIFERATION; GENE REGULATION; HUMAN POPULATIONS; NITRIC OXIDE; RECEPTORS

Citation Formats

Qin, Chen, Li, Dong, Lian, Wang, Lina, Kang, and Xu Biao. Advanced glycation end products impair function of late endothelial progenitor cells through effects on protein kinase Akt and cyclooxygenase-2. United States: N. p., 2009. Web. doi:10.1016/j.bbrc.2009.02.040.
Qin, Chen, Li, Dong, Lian, Wang, Lina, Kang, & Xu Biao. Advanced glycation end products impair function of late endothelial progenitor cells through effects on protein kinase Akt and cyclooxygenase-2. United States. https://doi.org/10.1016/j.bbrc.2009.02.040
Qin, Chen, Li, Dong, Lian, Wang, Lina, Kang, and Xu Biao. 2009. "Advanced glycation end products impair function of late endothelial progenitor cells through effects on protein kinase Akt and cyclooxygenase-2". United States. https://doi.org/10.1016/j.bbrc.2009.02.040.
@article{osti_21255955,
title = {Advanced glycation end products impair function of late endothelial progenitor cells through effects on protein kinase Akt and cyclooxygenase-2},
author = {Qin, Chen and Li, Dong and Lian, Wang and Lina, Kang and Xu Biao},
abstractNote = {Endothelial progenitor cells (EPCs) exhibit impaired function in the context of diabetes, and advanced glycation end products (AGEs), which accumulate in diabetes, may contribute to this. In the present study, we investigated the mechanism by which AGEs impair late EPC function. EPCs from human umbilical cord blood were isolated, and incubated with AGE-modified albumin (AGE-albumin) at different concentrations found physiologically in plasma. Apoptosis, migration, and tube formation assays were used to evaluate EPC function including capacity for vasculogenesis, and expression of the receptor for AGEs (RAGE), Akt, endothelial nitric oxide synthase (eNOS), and cycloxygenase-2 (COX-2) were determined. Anti-RAGE antibody was used to block RAGE function. AGE-albumin concentration-dependently enhanced apoptosis and depressed migration and tube formation, but did not affect proliferation, of late EPCs. High AGE-albumin increased RAGE mRNA and protein expression, and decreased Akt and COX-2 protein expression, whilst having no effect on eNOS mRNA or protein in these cells. These effects were inhibited by co-incubation with anti-RAGE antibody. These results suggest that RAGE mediates the AGE-induced impairment of late EPC function, through down-regulation of Akt and COX-2 in these cells.},
doi = {10.1016/j.bbrc.2009.02.040},
url = {https://www.osti.gov/biblio/21255955}, journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 2,
volume = 381,
place = {United States},
year = {Fri Apr 03 00:00:00 EDT 2009},
month = {Fri Apr 03 00:00:00 EDT 2009}
}