Structural changes of human epidermal alpha-keratin in disorders of keratinization.
The chemistry and structure of the epidermal alpha-keratin extracted from the skin of patients with a variety of disorders of keratinization have been investigated using biochemical, biophysical, and electron microscopic techniques developed for the characterization of normal mammalian epidermal keratin. Generally, the alpha-keratin polypeptides of the diseased epidermis differed from those of uninvolved epidermis or of normal volunteers in having varying numbers of polypeptide components of lower molecular weights, numerous free amino acids, higher contents of alpha-helix, and only limited facility for polymerization in vitro into native-type epidermal keratin filaments. As the alpha-helix-enriched fragments, which represent up to two-thirds of the polypeptide chains, isolated after limited tryptic digestion of the keratin filaments of normal, uninvolved, and involved epidermis, were physicochemically identical, it seems that the end-terminal non-alpha-helical regions of the polypeptides of diseased epidermis are abnormal. These differences may be a result of degradation or of altered protein synthesis.
D000595:Amino Acid Sequence; D002145:Callosities / Q000378:metabolism; D003599:Cytoskeleton / Q000648:ultrastructure*; D004817:Epidermis / Q000648:ultrastructure*; D006801:Humans; D007633:Keratins / Q000032:analysis / Q000378:metabolism*; D008854:Microscopy, Electron; D008970:Molecular Weight; D011487:Protein Conformation; D011565:Psoriasis / Q000473:pathology; D012871:Skin Diseases / Q000473:pathology*
D007633:Keratins