Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 419, Issue 1, Pages 25-30Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2003.08.012
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Funding
- NEI NIH HHS [EY11825] Funding Source: Medline
- NIDDK NIH HHS [DK54608, DK54143] Funding Source: Medline
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Modification of proteins by nonenzymatic glycation is one of the underlying factors contributory to the development of complications of diabetes. In general, the nature of this structural modification falls into two broad categories: nonenzymatic glycation per se. which refers to the attachment of free carbohydrate to proteins in the Amadori construct, and Advanced Glycation End-products (AGE), which refers to a heterogeneous group of carbohydrate-modified products generated from the Amadori adduct by oxidation, polymerization, and other spontaneous reactions. This review will focus on the role of nonenzymatically glycated proteins, and in particular glycated serum albumin, in the pathogenesis of diabetic complications, and on pharmacologic approaches to mitigate their deleterious effects. Potential intervention strategies to lessen the influence of AGE-modified proteins, as well as of other contributory abnormalities, are discussed elsewhere in this volume. (C) 2003 Elsevier Inc. All rights reserved.
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