The molecule can be a homotrimer where the α chains are all similar, or a heterotrimer, where one (usually) or all the α chains are different from each other. The most abundant human collagen is type I collagen, a heterotrimer where the triple helix is formed with two similar and ...
type I collagen. However, the basic information about the formation of heterotrimeric type I collagen molecule is still needed. In particular, the order of the three chains required to form the triple helix in a heterotrimer is not known. The sequence of the α2(I) chain is similar to ...
The removal of the N- and C-propeptides of types I and II collagens occurs by similar mechanisms. Cleavage of the N-propeptides involves the procollagen N-proteinase ADAMTS2, and cleavage of the C-propeptides involved the procollagen C-endopeptidase BMP-1 and.the procollagen C-endopeptidase...
This study shows that mechanical stimulation of cell-sponge constructs produces similar increases in the expression of 2 structural genes, as well as linear stiffness and linear modulus.doi:10.1089/ten.2006.0339Natalia Juncosa-Melvin, Karl S. Matlin, Robert W. Holdcraft, Victor...
Population doubling time, morphology and saturation densities were similar to W8 cells with small alterations towards an epithelial morphology. These results demonstrated that α2(I) within heterotrimer is important for cell adhesion and anchorage independent growth. 展开 ...
Furthermore, while mutation or deletion of a particular binding site may alter the functional activity of a construct transfected into cultured cells, there is no guarantee that a similar change will have the same effect in vivo, where the entire gene locus is present in its native chromosomal ...
Similar to DDR2 inhibitors, knock-down of DDR2 inhibited collagen-induced migration of amnion mesenchymal cells significantly (Figure S2D). Collectively these data suggest that type 1 collagen not only provides a scaffold for migration but stimulates migration of human amnion mesenchymal cells through ...
Although it is well established that the extracellular matrix affects tumour progression, not much is known about the various components and their effect on head and neck squamous cell carcinoma (HNSCC) progression. Levels of collagen type XI α1 (colXI
Neither type XIIB from skin nor type XIIA from WISH cells are chondroitinase-sensitive. By similar analysis, a portion of the type XIV collagen chains in cartilage was also sensitive to chondroitinase digestion. Chondroitin sulfate is apparently not located on its NC3 domain. As in skin, ...
Special domainsRestin (also known as XV-endostatin), which is similar to XVIII-endostatin[6] Special neoepitopesC-terminal (NC1-XV) proteolytic production of restin (homologous to endostatin)[12,13] Protein structure and functionProteoglycan. Multiplexin is assembled into homotrimers with multiple ...