ADVANCED PROTEIN GLYCOSYLATION IN DIABETES AND AGING

被引：1106

作者：

BROWNLEE, M

机构：

[1] YESHIVA UNIV ALBERT EINSTEIN COLL MED, DEPT MED, BRONX, NY 10461 USA

[2] YESHIVA UNIV ALBERT EINSTEIN COLL MED, DEPT PATHOL, BRONX, NY 10461 USA

来源：

ANNUAL REVIEW OF MEDICINE | 1995年 / 46卷

关键词：

ADVANCED GLYCATION END PRODUCTS; MATRIX; RECEPTORS; MITOGENS; DNA; AMINOGUANIDINE;

D O I：

10.1146/annurev.med.46.1.223

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

1001 ;

摘要：

Products of advanced protein glycosylation (advanced glycation end products, or AGEs) accumulate in tissues as a function of time and sugar concentration. AGEs induce permanent abnormalities in extracellular matrix component function, stimulate cytokine and reactive oxygen species production through AGE-specific receptors, and modify intracellular proteins, Pharmacologic inhibition of AGE formation in long-term diabetic animals prevents diabetic retinopathy, nephropathy, neuropathy, and arterial abnormalities in animal models. Clinical trials in humans are currently in progress.

引用

页码：223 / 234

页数：12

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