title: Human hemolysate glycated proteome.
abstract: 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.
authors.affiliation: Department of Human Protein Sciences, University Medical Centre, University of Geneva, Geneva, Switzerland.
authors.forename: Feliciano
authors.initials: F
authors.lastname: Priego-Capote
authors.forename: Maria
authors.initials: M
authors.lastname: Ramirez-Boo
authors.forename: Christine
authors.initials: C
authors.lastname: Hoogland
authors.forename: Alexander
authors.initials: A
authors.lastname: Scherl
authors.forename: Markus
authors.initials: M
authors.lastname: Mueller
authors.forename: Frédérique
authors.initials: F
authors.lastname: Lisacek
authors.forename: Jean-Charles
authors.initials: JC
authors.lastname: Sanchez
mesh_terms: D005947:Glucose / Q000378:metabolism*; D006442:Glycated Hemoglobin / Q000378:metabolism; D006031:Glycosylation; D006461:Hemolysis; D006801:Humans; D020543:Proteome / Q000378:metabolism*
chemical_list: D005947:Glucose; D006442:Glycated Hemoglobin; D020543:Proteome; C517652:hemoglobin A1c protein, human