Proteomic tools for the investigation of human hair structural proteins and evidence of weakness sites on hair keratin coil segments.
Fiche publication
Date publication
février 2012
Auteurs
Membres identifiés du Cancéropôle Est :
Dr VAN DORSSELAER Alain
Tous les auteurs :
Barthelemy NR, Bednarczyk A, Schaeffer-Reiss C, Jullien D, Van Dorsselaer A, Cavusoglu N
Lien Pubmed
Résumé
Human hair is principally composed of hair keratins and keratin-associated proteins (KAPs) that form a complex network giving the hair its rigidity and mechanical properties. However, during their growth, hairs are subject to various treatments that can induce irreversible damage. For a better understanding of the human hair protein structures, proteomic mass spectrometry (MS)-based strategies could assist in characterizing numerous isoforms and posttranslational modifications of human hair fiber proteins. However, due to their physicochemical properties, characterization of human hair proteins using classical proteomic approaches is still a challenge. To address this issue, we have used two complementary approaches to analyze proteins from the human hair cortex. The multidimensional protein identification technology (MudPit) approach allowed identifying all keratins and the major KAPs present in the hair as well as posttranslational modifications in keratins such as cysteine trioxidation, lysine, and histidine methylation. Then two-dimensional gel electrophoresis coupled with MS (2-DE gel MS) allowed us to obtain the most complete 2-DE gel pattern of human hair proteins, revealing an unexpected heterogeneity of keratin structures. Analyses of these structures by differential peptide mapping have brought evidence of cleaved species in hair keratins and suggest a preferential breaking zone in alpha-helical segments.
Référence
Anal Biochem. 2012 Feb 1;421(1):43-55