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Biochim Biophys Acta. 2013 Dec;1830(12):5480-5. doi: 10.1016/j.bbagen.2013.04.024. Epub 2013 Apr 23.

Clinical, pathophysiological and structure/function consequences of modification of albumin by Amadori-glucose adducts.

Author information

1
Glycadia, Inc., 1880 JFK Boulevard, Suite 200, Philadelphia, PA 19103, United States. Electronic address: drmpcohen@aol.com.

Abstract

BACKGROUND:

The nonenzymatic condensation of glucose with albumin results in the formation of albumin modified by Amadori glucose adducts, the principal form in which glycated albumin exists in vivo.

SCOPE OF REVIEW:

This review focuses on (a) the utility of measurement of Amadori-modified glycated albumin (AGA) as a biomarker in diabetes, where elevated levels attend the hyperglycemic state; (b) the role of AGA as a causal factor in the pathogenesis of complications of diabetes; (c) effects on transport properties; and (d) structural and functional consequences of the modification of albumin by Amadori glucose adducts. It does not discuss counterparts with respect to Advanced Glycation Endproducts (AGE), which may be found in other publications.

MAJOR CONCLUSIONS:

Nonenzymatic glycation of albumin, which is increased in diabetes, has clinical relevance and pathophysiologic importance, with ramifications for the management of this disease, the development of its complications, and the transport of endogenous and exogenous ligands.

GENERAL SIGNIFICANCE:

Appreciation of the manifold consequences of AGA has afforded new avenues for assessing clinical management of diabetes, awareness of the impact of nonenzymatic glycation on albumin biology, insights into the pathogenesis of vascular complications of diabetes, and avenues of investigation of and intervention strategies for these complications. This article is part of a Special Issue on albumin. This article is part of a Special Issue entitled Serum Albumin.

KEYWORDS:

Albumin

PMID:
23624335
DOI:
10.1016/j.bbagen.2013.04.024
[Indexed for MEDLINE]

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