Collagen type VI shows a high affinity, specific interaction with biglycan and decorin by binding with high affinity to its core protein. The interaction is with the N-terminal globular domain of the collagen 6. as well as interactions with other matrix proteins e.g. hyaluronan, heparan sulphate and NG-2 proteoglycans. Type VI collagen also binds to the a1b1 integrin.
Binding of biglycan or somewhat less efficiently of decorin appears to have a central role in the organization of collagen 6 into a network. The effect depends on the core protein with its intact glycosaminoglycan chains. These interactions also retain the proteoglycans in the completed collagen 6 beaded filament. Indeed such filaments can be isolated from tissue by high shear procedures and then shown to contain biglycan/decorin bound at the N-terminus. The proteoglycan simultaneously bind either of the matrilins 1,2 or 3, which in turn binds to aggrecan, collagen cross-striated fibers and interestingly also procollagen 2. The complex of biglycan/decorin and a matrilin thus appears to function as a linker molecule between collagen 6 and other major constituents in the matrix.
Storage: Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.