Angiogenic Effects of Advanced Glycation End Products of the Maillard Reaction on Cultured Human Umbilical Cord Vein Endothelial Cells

Tezuka, Mariko; Koyama, Noriyuki; Morisaki, Naho; Saito, Yoichi; Yoshida, Shizuo; Araki, Nobuhito; Horiuchi, Seikoh

doi:10.1006/bbrc.1993.1677

Cited by 37 publications

(35 citation statements)

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“…One explanation for these discrepant results may be the nature of the tests used in the two studies to assess direct toxicity of AGE-BSA in pericytes [25]. The finding that AGE-BSA is also toxic to aortic endothelial cells but only at the high concentration of 62.5 m g/ml is in agreement with Tezuka et al [26] showing that AGE-BSA at 50 m g/ml inhibits the proliferation of cultured human umbilical cord vein endothelial cells (HUVEC). Despite the low level of AGE-mediated toxicity in BAEC, it is possible that exposure to AGE-BSA may have resulted in changes to the cytoskeleton and cell permeability as reported by Esposito et al [10].…”

Section: Discussionsupporting

confidence: 80%

“…Previous studies have reported that AGE-modified proteins have a number of biological effects [28], endothelial cell migration and tube formation [26], alteration in cell shape/ cytoskeleton along with perturbation of barrier and coagulant function [10]. Most of these effects are suggested to be mediated by the interaction of AGE with AGE-specific receptors which are localized on various cell types, including smooth muscle cells, monocytes, macrophages and mesangial cells [29].…”

Section: Discussionmentioning

confidence: 99%

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Toxic action of advanced glycation end products on cultured retinal capillary pericytes and endothelial cells: relevance to diabetic retinopathy

et al. 1997

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Summary The toxic effects of advanced glycation end products (AGEs) on bovine retinal capillary pericytes (BRP) and endothelial cells (BREC) were studied. AGE-modified bovine serum albumin (AGE-BSA) was toxic to BRP. At a concentration of 500 m g/ml it reduced the BRP number to 48 ± 3 % (p < 0.05) of untreated controls, as determined by cell counting with haemocytometer. AGE-BSA was also toxic to bovine aortic endothelial cells (BAEC) reducing cell number to 84 ± 3.1 % of untreated controls. Under similar conditions, low concentrations (62.5 m g/ml) of AGE-BSA were mitogenic to BREC increasing the cell proliferation to 156 ± 11 % (p < 0.05) above that of untreated controls. At a higher dose of 500 m g/ml AGE-BSA decreased the proliferation of BREC to 85 ± 6 % of untreated controls. Immunoblot analysis demonstrated that BRP and BREC express the p60 AGE-receptor. Retinal capillary bed from the human also stained positively for the p60 AGE-receptor. Addition of 0.25 m g/ml of p60 AGE-receptor antibody was able to block the effects of AGE-BSA on BRP and BREC. The level of binding of [ 125 I]-labelled AGE-BSA to the cell surface was small but significant among the three cell types. There was also an increase in the internalized pool of radioligand in BRP and BREC but this was very much lower than in BAEC. In all the cell types the internalized pool of [ 125 I]-labelled AGE-BSA was much larger than the amount associated with the cell surface. Degradation products were not detected in the media over the 24-h incubation of the cells with [ 125 I]AGE-BSA. The binding of [ 125 I]-labelled AGE-BSA to the cell surface was prevented by the addition of p60 AGE-receptor. These results suggest that the interaction of AGE-modified proteins with the membrane-bound AGE-receptor may play an important role in the pathogenesis of diabetic retinopathy. [Diabetologia (1997) 40: 156-164]

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Section: Discussionsupporting

confidence: 80%

Section: Discussionmentioning

confidence: 99%

Toxic action of advanced glycation end products on cultured retinal capillary pericytes and endothelial cells: relevance to diabetic retinopathy

et al. 1997

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“…Although the AGE-induced changes appeared to be modest, chronic exposure to AGE accumulated during prolonged hyperglycemic states may give rise to local deterioration in the growth or function of the endothelium. Tezuka et al reported that similar concentrations of AGE stimulated the migration and tube formation of human umbilical vein endothelial cells but did not affect their proliferation [11]. Although no explanation as to why the endothelial cell growth under AGE differed between the two studies is available, the differences in the type of growth supplements employed or in the AGE preparations may be responsible.…”

Section: Discussionmentioning

confidence: 99%

Advanced glycosylation end products stimulate the growth but inhibit the prostacyclin‐producing ability of endothelial cells through interactions with their receptors

et al. 1996

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The influence of advanced glycosylation end products (AGE) on endothelial cells was investigated. When human umbilical endothelial cells were cultured with AGE-bovine serum albumin, viable cell number as well as DNA synthesis was significantly stimulated, whereas prostacyclin production by the endothelial cells was decreased. Antisense oligodeoxyribonucleotides against mRNA coding for AGE receptor were found to reverse both the AGE-induced growth stimulation and the inhibition of prostacyclin production in endothelial cells. These results thus suggest that AGE ligand-receptor interactions in endothelial cells can promote angiogenesis and thrombogenesis, leading to the development of diabetic vascular complications.

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“…After long term incubation, these early products are converted to advanced glycation end products (AGE), 1 which are characterized physicochemically by fluorescence, brown color, and intra-or inter-molecular crosslinking (1, 2), and biologically by specific recognition by AGE receptors. The presence of AGE in several human tissues suggests that they may be involved in the aging process, diabetic complications, and atherosclerosis (3-11).The physiological significance of AGE has been analyzed primarily using AGE structure(s) expressed in vivo and AGEbinding proteins or AGE receptors, through which AGE are believed to elicit several biological phenomena in monocytes/ macrophages (12-17), endothelial cells (18,19), and mesangial cells (20,21). Several AGE receptors have been characterized (22-25), one of which is a novel 35-kDa protein (called RAGE) from bovine lung endothelium that belongs to the immunoglobulin superfamily (23).…”

mentioning

confidence: 99%

“…The physiological significance of AGE has been analyzed primarily using AGE structure(s) expressed in vivo and AGEbinding proteins or AGE receptors, through which AGE are believed to elicit several biological phenomena in monocytes/ macrophages (12)(13)(14)(15)(16)(17), endothelial cells (18,19), and mesangial cells (20,21). Several AGE receptors have been characterized (22)(23)(24)(25), one of which is a novel 35-kDa protein (called RAGE) from bovine lung endothelium that belongs to the immunoglobulin superfamily (23).…”

mentioning

confidence: 99%

Scavenger Receptor Class B Type I-mediated Reverse Cholesterol Transport Is Inhibited by Advanced Glycation End Products

Ohgami

Nagai

Miyazaki

et al. 2001

Journal of Biological Chemistry

157

105

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Cellular interactions of advanced glycation end products (AGE) are mediated by AGE receptors. We demonstrated previously that class A scavenger receptor types I and II (SR-A) and CD36, a member of class B scavenger receptor family, serve as the AGE receptors. In this study, we investigated whether scavenger receptor class B type I (SR-BI), another receptor belonging to class B scavenger receptor family, was also an AGE receptor. We used Chinese hamster ovary (CHO) cells overexpressed hamster SR-BI (CHO-SR-BI cells).125 I-AGE-bovine serum albumin (AGE-BSA) was endocytosed in a dose-dependent fashion and underwent lysosomal degradation by CHO-SR-BI cells.125 I-AGE-BSA exhibited saturable binding to CHO-SR-BI cells (K d ‫؍‬ 8.3 g/ml). Endocytic uptake of 125 I-AGE-BSA by CHO-SR-BI cells was completely inhibited by oxidized low density lipoprotein (LDL) and acetylated LDL, whereas LDL exerted only a weak inhibitory effect (<20%). Cross-competition experiments showed that AGE-BSA had no effect on HDL binding to these cells and vice versa. Interestingly, however, SR-BI-mediated selective uptake of HDL-CE was completely inhibited by AGE-BSA in a dose-dependent manner (IC 50 <10 g/ml). Furthermore, AGE-BSA partially inhibited (by <30%) the selective uptake of HDL-CE in human hepatocarcinoma HepG2 cells (IC 50 <30 g/ml). In addition, [ 3 H]cholesterol efflux from CHO-SR-BI cells to HDL was significantly inhibited by AGE-BSA in a dose-dependent manner (IC 50 <30 g/ml). Our results indicate that AGE proteins, as ligands for SR-BI, effectively inhibit both SR-BI-mediated selective uptake of HDL-CE and cholesterol efflux from peripheral cells to HDL, suggesting that AGE proteins might modulate SR-BI-mediated cholesterol metabolism in vivo.In the Maillard reaction, proteins react with glucose to form Schiff base and Amadori products. After long term incubation, these early products are converted to advanced glycation end products (AGE), 1 which are characterized physicochemically by fluorescence, brown color, and intra-or inter-molecular crosslinking (1, 2), and biologically by specific recognition by AGE receptors. The presence of AGE in several human tissues suggests that they may be involved in the aging process, diabetic complications, and atherosclerosis (3-11).The physiological significance of AGE has been analyzed primarily using AGE structure(s) expressed in vivo and AGEbinding proteins or AGE receptors, through which AGE are believed to elicit several biological phenomena in monocytes/ macrophages (12-17), endothelial cells (18,19), and mesangial cells (20,21). Several AGE receptors have been characterized (22-25), one of which is a novel 35-kDa protein (called RAGE) from bovine lung endothelium that belongs to the immunoglobulin superfamily (23). Two AGE-binding proteins of 60-and 90-kDa (called p60 and p90) were also identified from the rat liver (24).Recently, galectin-3, a lectin-like protein with a high binding affinity for galactose-containing glycoproteins, was identified as a component of p90 (25). We have re...

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Angiogenic Effects of Advanced Glycation End Products of the Maillard Reaction on Cultured Human Umbilical Cord Vein Endothelial Cells

Cited by 37 publications

References 0 publications

Toxic action of advanced glycation end products on cultured retinal capillary pericytes and endothelial cells: relevance to diabetic retinopathy

Toxic action of advanced glycation end products on cultured retinal capillary pericytes and endothelial cells: relevance to diabetic retinopathy

Advanced glycosylation end products stimulate the growth but inhibit the prostacyclin‐producing ability of endothelial cells through interactions with their receptors

Scavenger Receptor Class B Type I-mediated Reverse Cholesterol Transport Is Inhibited by Advanced Glycation End Products

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