The isolation and partial characterization of chondronectin, an attachment factor for chondrocytes

We have previously demonstrated that the adhesion of embryonic chick sternal chondrocytes to a type II-collagen substrate is not mediated by fibronectin but rather by a distinct attachment factor which we have named chondronectin. Here we describe the isolation, properties, and biological activity o...

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Bibliographic Details
Published in:The Journal of biological chemistry 1982-03, Vol.257 (5), p.2330-2334
Main Authors: Hewitt, A T, Varner, H H, Silver, M H, Dessau, W, Wilkes, C M, Martin, G R
Format: Article
Language:English
Subjects:
Animals
Antigens
Cartilage - physiology
Cell Adhesion
Chick Embryo
chickens
chondronectin
Chromatography, Affinity
Fibronectins - pharmacology
Fluorescent Antibody Technique
Glycoproteins - pharmacology
Immune Sera
Laminin
Proteins - isolation & purification
purification
serum
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Summary:We have previously demonstrated that the adhesion of embryonic chick sternal chondrocytes to a type II-collagen substrate is not mediated by fibronectin but rather by a distinct attachment factor which we have named chondronectin. Here we describe the isolation, properties, and biological activity of chondronectin prepared from chicken serum. Chondronectin is shown to be a glycoprotein with an estimated Mr = 180,000. After reduction, it migrates as subunits of Mr = 70,000. Antibodies directed against chondronectin inhibited the attachment of chondrocytes to type II collagen. Chondronectin is immunologically distinct from either fibronectin or laminin. Immunofluorescence studies on frozen sections of embryonic chick sternal cartilage and of cultured sternal chondrocytes showed that chondronectin is cell-associated rather than a major matrix component.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)34926-3