Collagen, type XVII, alpha 1 to interact with Keratin 18, Actinin alpha 4, Dystonin, Actinin, alpha 1, CTNND1 and ITGB4. Collagen, type XVII, alpha 1 Collagen XVII, previously called BP180, is a transmembrane protein which plays a critical role in maintaining the linkage between the intracellular and the extracellular structural elements involved in epidermal adhesion. Collagen XVII is a homotrimer of three alpha1(XVII)-chains and a transmembrane protein in type II orientation. Each 180 kD a-chain contains a globular intracellular domain of approximately 70 kDa, which interacts with beta4-integrin, plectin, and BP230 and is necessary for the stable attachment of hemidesmosomes to keratin intermediate filaments. The
Keratin Cells in the epidermis contain a structural matrix of keratin, which makes this outermost layer of the skin almost waterproof, and along with collagen and elastin, gives skin its strength. Rubbing and pressure cause thickening of the outer, cornified layer of the epidermis and form protective calluses, which is useful for athletes and on the fingertips of musicians who play stringed instruments. Keratinized epidermal cells are constantly shed and replaced. These hard, integumentary structures are formed by intercellular cementing of fibers formed from the dead, cornified cells generated by specialized beds deep within the skin. Hair grows continuously and feathers