Appearance and persistence of fibronectin in cartilage. Specific interaction of fibronectin with collagen type II.
Binding of fibronectins (FN) to collagen types I-IV were studied using polyclonal antibodies against human and chicken FNs, proteoglycan monomers, collagen type II and monoclonal antibodies reacting with both soluble and insoluble forms of human FN. Plasma fibronectin and type II collagen were shown to interact specifically in a homologous system. Type II collagen, however, proved to be less effective in inhibition assays compared to other types of collagen. In high density cultures of chicken limb bud cells, fibronectin was first localized within the fibroblast-like cells of 4 hr cultures and an extensive extracellular filamentous network developed by the end of day 1. Fibronectin was present in the newly formed cartilage nodules although it seemed to disappear by day 6, when the proteoglycan accumulation became more intensive. Enzyme treatments (testicular hyaluronidase, chondroitinase ABC) helped to localize FN at this stage of development of chicken cartilage, in microdroplet high density cultures of human fetal chondrocytes and in articular cartilage. Fibronectin was localized only in the pericellular ring of intact human articular cartilage using monoclonal antibodies with the biotin-avidin system.
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D002356:Cartilage / Q000032:analysis*; D002417:Cattle; D002642:Chick Embryo; D003094:Collagen / Q000378:metabolism*; D004285:Dogs; D005353:Fibronectins / Q000032:analysis* / Q000276:immunology / Q000378:metabolism; D006801:Humans; D051379:Mice; D008807:Mice, Inbred BALB C
D000911:Antibodies, Monoclonal; D005353:Fibronectins; D003094:Collagen