Collagen receptor on fibroblasts, endotelial cells and macrophages. Vogel, W.F., 2001. Collagen-receptor signaling in health and disease. European Journal of Dermatology 11, 506-514. White, D.J., Puranen, S., Johnson, M.S., Heino, J., 2004. The collagen receptor subfamily of the integrins. International Journal of Biochemistry & Cell Biology 36, 1405-1410. Collagen receptor Collagen receptors are membrane proteins that bind the extracellular matrix protein collagen, the most abundant protein in mammals. They control mainly cell proliferation, migration and adhesion, coagulation cascade activation and they affect ECM structure by regulation of MMP (matrix metalloproteinases). There are at least eight human collagen receptors belonging to four different
Collagen helix – this should not be confused with the right-handed alpha helix. These three left-handed helices are twisted together into a right-handed triple helix or "super helix", a cooperative quaternary structure stabilized by many hydrogen bonds. With type I collagen and possibly all fibrillar collagens, if not all collagens, each triple-helix associates into a right-handed super-super-coil referred to as the collagen microfibril. Each microfibril is interdigitated with its neighboring microfibrils to a degree that might suggest they are individually unstable, although within collagen fibrils, they are so well ordered as to be crystalline. A distinctive feature of collagen is the