Type XII collagen
نویسندگان
چکیده
منابع مشابه
Identification and partial characterization of two type XII-like collagen molecules
We have identified two distinct collagenous macromolecules in extracts of fetal bovine skin. Each of the molecules appears to contain three identical alpha-chains with short triple-helical domains of approximately 25 kD, and nontriple-helical domains of approximately 190 kD. Consistent with these observations, extracted molecules contain a relatively short triple-helical domain (75 nm) and a la...
متن کاملMechanical strain increases expression of type XII collagen in murine osteoblastic MC3T3-E1 cells.
In adult mouse, the mRNA corresponding to the alpha1 chain of type XII collagen (alpha 1(XII)) is predominantly detected in the bone. Additionally, murine osteoblastic cells, MC3T3-E1, increased the mRNA level of alpha 1(XII) response to the mechanical strain in the stretch culture system. Cyclic stretch stress resulted in a threefold increase in mRNA level of alpha 1(XII) as compared to the co...
متن کاملType XII collagen: distinct extracellular matrix component discovered by cDNA cloning.
We have screened a cDNA library constructed from tendon fibroblast mRNA for the presence of collagenous coding sequences. Nucleotide sequence analysis of one isolated clone, pMG377, reveals that the clone encodes a polypeptide that is homologous to, yet distinctly different from, type IX short-chain collagen polypeptides. The structure of the conceptual translation product of the cDNA is also d...
متن کاملImmunolocalization of type XII collagen at the corneoscleral angle of the embryonic avian eye.
A monoclonal antibody specific for the chicken alpha 1 (XII) collagen chain was used to immunolocalize type XII collagen in the corneoscleral of 17-19-day-old chicken embryos. These immunofluorescence studies localized type XII collagen around the scleral cartilages and ossicles. There was also a striking positive staining in the scleral spur and stroma of the corneolimbus beneath the external ...
متن کاملType XII collagen regulates osteoblast polarity and communication during bone formation
Differentiated osteoblasts are polarized in regions of bone deposition, demonstrate extensive cell interaction and communication, and are responsible for bone formation and quality. Type XII collagen is a fibril-associated collagen with interrupted triple helices and has been implicated in the osteoblast response to mechanical forces. Type XII collagen is expressed by osteoblasts and localizes ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)47179-2