Human hemolysate glycated proteome.

Détails

ID Serval
serval:BIB_68F402393899
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Human hemolysate glycated proteome.
Périodique
Analytical chemistry
Auteur⸱e⸱s
Priego-Capote F., Ramirez-Boo M., Hoogland C., Scherl A., Mueller M., Lisacek F., Sanchez J.C.
ISSN
1520-6882 (Electronic)
ISSN-L
0003-2700
Statut éditorial
Publié
Date de publication
15/07/2011
Peer-reviewed
Oui
Volume
83
Numéro
14
Pages
5673-5680
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
Despite continuous advances in hyperglycemia treatments, a precise control through monitoring of glucose and glycated hemoglobin remains in most diabetic patients as the diagnosis/prognosis tool. An alternative perspective could be the discovery and quantitation of new blood glycated proteins formed by nonenzymatic reaction with circulatory glucose. As a result, the human hemolysate is an incomparable source of glycated proteins to further monitor glycemia and interpret changes at the level of this post-translational modification. The human hemolysate is here studied based on the differential labeling of proteins with isotopically labeled-glucose ([(13)C(6)] glucose), named glycation isotopic labeling. Due to the chemoselectivity of glycation, only preferential targets are labeled by this protocol. The approach provides qualitative data through the detection of preferential protein glycation sites as well as quantitative information to evaluate the abundance of this modification. This strategy was applied to human hemolysate samples corresponding to different glycemic states estimated by laboratory-certified concentrations of glycated hemoglobin. The glycation level of each protein can then be employed to interpret the effect of glucose exposition as a consequence of glycemic unbalance. This information should provide new molecular insights into protein glycation mechanisms that might generate a new hypothesis to clinicians to improve the understanding of underlying pathologies associated to prolonged hyperglycemia.
Mots-clé
Glucose/metabolism, Glycated Hemoglobin A/metabolism, Glycosylation, Hemolysis, Humans, Proteome/metabolism
Pubmed
Web of science
Création de la notice
08/12/2019 17:52
Dernière modification de la notice
09/12/2019 7:26
Données d'usage