Collagen and Proteoglycan Forms of Type IX Collagen in Chick Embryo Cartilage
نویسندگان
چکیده
منابع مشابه
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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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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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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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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We have prepared a high buoyant density proteoglycan fraction from the vitreous humor of 13-day-old chick embryos. Using immunoblot analysis coupled with chondroitinase digestion, we demonstrate that the purified preparation is composed predominantly of type IX collagen-like chondroitin sulfate proteoglycan with an alpha 1(IX) chain Mr approximately 23,000 shorter than the known alpha 1 in cart...
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ژورنال
عنوان ژورنال: Trends in Glycoscience and Glycotechnology
سال: 1992
ISSN: 0915-7352,1883-2113
DOI: 10.4052/tigg.4.469