Epidermal and hair follicle transglutaminases and crosslinking in skin.
Epidermal and hair follicle transglutaminases crosslink structural proteins in the skin by epsilon-(gamma-glutamyl)-lysine bonds. This crosslinking produces protein polymers that are extremely insoluble and, until recently, difficult to characterize. Epidermal transglutaminase is localized to the granular layer of the epidermis. It catalyzes the crosslinking of a soluble cytoplasmic precursor to form the cornified envelope that lines the inner membrane of the mature keratinocyte in the stratum corneum. Hair follicle transglutaminase is localized to the inner root sheath and medulla of the hair follicle. It crosslinks a poorly characterized citrulline-rich protein. The enzymes and their substrates have been shown to be important markers of normal differentiation. Regulation of these processes is currently under investigation.
D000217:Acyltransferases / Q000276:immunology / Q000378:metabolism*; D000818:Animals; D002103:Cadaverine / Q000378:metabolism; D002118:Calcium / Q000378:metabolism; D003432:Cross-Linking Reagents; D004817:Epidermis / Q000201:enzymology; D006197:Hair / Q000201:enzymology*; D007633:Keratins / Q000378:metabolism; D012867:Skin / Q000201:enzymology*; D011503:Transglutaminases
D003432:Cross-Linking Reagents; D007633:Keratins; D000217:Acyltransferases; D011503:Transglutaminases; D002103:Cadaverine; D002118:Calcium