Keratin 6C Keratin 6C Keratin 6C (protein name K6C; gene name "KRT6C"), is a type II cytokeratin, one of a number of isoforms of keratin 6 encoded by separate genes located within the type II keratin gene cluster on human chromosome 12q. This gene was uncovered recently by the Human Genome Project and its expression patterns in humans remains unknown. Keratins are the intermediate filament proteins that form a dense meshwork of filaments throughout the cytoplasm of epithelial cells. Keratins form heteropolymers consisting of a type I and a type II keratin. Keratins are generally expressed in particular pairs of type I
Collagen receptor N-terminal domain rich in cystein, F2 fibronectin type II domain and several C-lectin domains. From this mannose family, collagen is specifically bound by mannose receptor, M-phospholipase A2 receptor and Endo180 receptor. Binding of collagen or denatured collagen (gelatin) is provided by F2 domain and partly by C-terminal domain (aa 1000-1453), which binds type I collagen triple helix. Inability to internalize collagen and reduced ability of adhesion and related increased migration in collagen matrix was observed in fibroblast population with nonfunctional Endo180 receptor. The exact principal of collagen binding to mannose receptor is not known so far. Endo180 receptor is expressed