albumin - publications

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1. Diabetes Metab. 2012 Feb 18. [Epub ahead of print]

Structural modifications of human albumin in diabetes.

Guerin-Dubourg A, Catan A, Bourdon E, Rondeau P.

Laboratoire de biochimie et génétique moléculaire (LBGM), groupe d'étude sur
l'inflammation chronique et l'obésité (GEICO), université de La Réunion, 15,
avenue René-Cassin, BP 7151, 97715 Saint-Denis Messag cedex 09, Réunion; Unité
fonctionnelle de recherche biochimie, centre hospitalier Félix-Guyon, 97405
Saint-Denis, Réunion.

AIM: Albumin, a major protein in the blood circulation, can undergo increased
glycation in diabetes. From recent studies, it has become evident that glycation
has important implications for albumin actions and impact on cell functioning.
This study compares the structural and functional properties of albumin glycated
by glucose and methylglyoxal (MGO) with those of albumin purified from diabetic
patients. METHODS: Human serum albumin (HSA) was purified from diabetic patients
and control subjects using affinity chromatography, and oxidation parameters in
various albumin preparations were determined. Tryptophan and
1-anilino-8-naphthalene sulphonic acid (ANSA) probe fluorescence, redox state,
antioxidant and copper-binding capacities of the different preparations of
albumin were also determined and compared. RESULTS: Occurrence of oxidative
modifications was enhanced in albumin whether purified from diabetic patients, or
glycated by glucose or MGO, after determination of their fructosamine and free
thiol and amino group contents, carbonyl content and antioxidant activities.
Whereas more quantitative changes in oxidative and structural parameters were
observed in the glucose- and MGO-modified albumins, significant impairment of
albumin function (free-radical-scavenging and copper-binding capacities) were
demonstrated in the HSA purified from diabetics. These findings reveal different
structural and functional features of diabetic HSA compared with in vitro models.
CONCLUSION: This study provides new information supporting albumin as an
important biomarker for monitoring diabetic pathophysiology. In addition, it
reconfirms the influence of experimental conditions in which advanced glycation
end-products (AGEs) are generated in tests designed to mimic the pathological
conditions of diabetes.

Copyright © 2011 Elsevier Masson SAS. All rights reserved.

PMID: 22349032 [PubMed - as supplied by publisher]