Collagen evolution of collagens was a fundamental step in the early evolution of life, supporting the coalescence of multicellular life forms. Collagen D-banding is viable as periodic formation of ridging on all fibrils forming collagen. D-bands are created due to the semi-crystalline formation of the collagen within the fibrils. The pattern exhibited by D-banding is consistently independent of fibril diameter. When undergoing deformation, collagen fibrils may lose their D-banding, making the disappearance of the d-bands an indicator of the type of damage undergone by then tendon fibrils. Collagen Collagen is the main structural protein in the extracellular space in the various
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