Isolation and characterization of a collagen-binding glycoprotein from chondrocyte membranes.
AUTOR(ES)
Mollenhauer, J
RESUMO
A collagen-binding glycoprotein was isolated from purified chick chondrocyte surface membranes by affinity chromatography on type II collagen-Sepharose. The purified glycoprotein has an apparent mol. wt. of 31,000 and binds to native chick collagen types I, II, III, V and M. Although it contains 30% carbohydrates, the majority of which is fucose, it is hydrophobic and soluble only in detergents. The integral membrane protein character of the 31-K protein became apparent from its ability to insert into lecithin vesicles. Liposome-inserted 31-K protein binds 125I-labelled type II collagen in the presence of 0.5 M NaCl, while detergent-solubilized 31-K protein is dissociated from type II collagen by 0.05-0.1 M NaCl. Electron microscopic studies employing the rotary shadowing technique indicate that 31-K protein particles bind to the ends of collagen molecules. We propose that this glycoprotein serves as anchorage site for extracellular collagen to the chondrocyte membrane and thus may be involved in cell-matrix interactions in cartilage.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=555084Documentos Relacionados
- Collagen-binding growth factors: Production and characterization of functional fusion proteins having a collagen-binding domain
- Identification and isolation of a collagen-binding fragment of the adhesive glycoprotein fibronectin.
- Characterization of the Collagen-Binding S-Layer Protein CbsA of Lactobacillus crispatus
- Structural analysis of fibronectin and its collagen-binding fragment from several cell lines.
- Isolation of a glycoprotein from Mycoplasma pneumoniae membranes.