Domains of type X collagen: alteration of cartilage matrix by fibril association and proteoglycan accumulation.
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چکیده
منابع مشابه
Domains of type X collagen: alteration of cartilage matrix by fibril association and proteoglycan accumulation
During endochondral bone formation, hypertrophic cartilage is replaced by bone or by a marrow cavity. The matrix of hypertrophic cartilage contains at least one tissue-specific component, type X collagen. Structurally type X collagen contains both a collagenous domain and a COOH-terminal non-collagenous one. However, the function(s) of this molecule have remained largely speculative. To examine...
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A recent immunoelectron microscopic study of type X collagen in developing cartilage gave results that could be explained by movement of the molecule from one region of the cartilage matrix to another, there becoming associated with preexisting collagen fibrils. In the present study, to test the feasibility of this model we incubated pieces of nonhypertrophic, embryonic chicken sternal cartilag...
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The in vitro phenotype of bovine articular chondrocytes is described. Chondrocytes plated at high density in roller-bottle and dish cultures were maintained in vitro. The major matrix macromolecules, collagen and proteoglycan, synthesized by these cells were characterized during the course of the culture period. The chondrocytes synthesized mainly Type II collagen, which was found predominantly...
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چکیده ندارد.
Type III collagen, a fibril network modifier in articular cartilage.
The collagen framework of hyaline cartilages, including articular cartilage, consists largely of type II collagen that matures from a cross-linked heteropolymeric fibril template of types II, IX, and XI collagens. In the articular cartilages of adult joints, type III collagen makes an appearance in varying amounts superimposed on the original collagen fibril network. In a study to understand be...
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ژورنال
عنوان ژورنال: The Journal of Cell Biology
سال: 1992
ISSN: 0021-9525,1540-8140
DOI: 10.1083/jcb.117.3.687