A distinct class of vertebrate collagen genes encodes chicken type IX collagen polypeptides.

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چکیده

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Monoclonal antibody against chicken type IX collagen: preparation, characterization, and recognition of the intact form of type IX collagen secreted by chondrocytes

A series of monoclonal antibodies was prepared against the pepsin-resistant fragment of type IX collagen designated HMW. One of these antibodies (called 2C2) was selected for further analysis. Antibody 2C2 showed no cross-reactivity with other collagen types by inhibition enzyme-linked immunosorbent assays. It recognized an epitope present in native HMW, but failed to recognize any of the three...

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Structural and functional comparison of type IX collagen-proteoglycan from chicken cartilage and vitreous humor.

Type IX collagen-proteoglycan is a major component of hyaline cartilages where it is located on the surface of the collagen fibrils so that a collagenous domain of the molecule (called COL3) and a non-collagenous domain (called NC4) project at periodic distances away from the surface of the fibril. Type IX collagen-proteoglycan is also present on the surface of the collagen fibrils of the adult...

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On the role of type IX collagen in the extracellular matrix of cartilage: type IX collagen is localized to intersections of collagen fibrils

The tissue distribution of type II and type IX collagen in 17-d-old chicken embryo was studied by immunofluorescence using polyclonal antibodies against type II collagen and a peptic fragment of type IX collagen (HMW), respectively. Both proteins were found only in cartilage where they were co-distributed. They occurred uniformly throughout the extracellular matrix, i.e., without distinction be...

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Collagen type IX: evidence for covalent linkages to type II collagen in cartilage.

A major site of pyridinoline cross-linking in bovine type IX collagen was traced to a tryptic peptide derived from one of the molecule's HMW chains. This peptide gave two amino acid sequences (in 2/1 ratio) consistent with it being a three-chained structure. The major sequence matched exactly that of the C-telopeptide of type II collagen from the same tissue. A second HMW chain that contained p...

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D-periodic distribution of collagen type IX along cartilage fibrils

It has recently become apparent that collagen fibrils may be composed of more than one kind of macromolecule. To explore this possibility, we developed a procedure to purify fibril fragments from 17-d embryonic chicken sternal cartilage. The fibril population obtained shows, after negative staining, a uniformity in the banding pattern and diameter similar to the fibrils in situ. Pepsin digestio...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 1985

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.82.12.4050