Transglutaminase-mediated cross-linking in mammalian epidermis.
The epsilon-(gamma-glutamyl)lysine isopeptide bond has been identified in certain structural proteins of the hair fibre and the epidermis. The major cross-linked proteins are not keratins and generally have little or no cysteine, but have a high glutamic acid/glutamine residue content. In the hair fibre the cross-link appears in the citrulline-containing proteins of the medulla and the inner root sheath of the follicle. In the epidermis the cross-linked proteins are involved in the formation of the cornified envelope of the stratum corneum cells. In both cases, the cross-linked proteins contribute the characteristic property of chemical resistance to their biological structures.
D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D002103:Cadaverine / Q000378:metabolism; D003432:Cross-Linking Reagents; D004817:Epidermis / Q000201:enzymology*; D006197:Hair / Q000201:enzymology; D007633:Keratins / Q000378:metabolism; D011506:Proteins / Q000378:metabolism; D013379:Substrate Specificity; D011503:Transglutaminases
D003432:Cross-Linking Reagents; D011506:Proteins; D007633:Keratins; D000217:Acyltransferases; D011503:Transglutaminases; D002103:Cadaverine