Characterization of the class III collagen receptor, a phosphorylated, transmembrane glycoprotein expressed in nucleated human cells.

摘要: We previously identified a 90-kDa cell surface glycoprotein, termed the class III collagen receptor (CRIII), that bound to in affinity chromatography experiments (Wayner, E. A., and Carter, W. G. (1987) J. Cell Biol. 105, 1873-1884). Here, we utilize monoclonal antibodies define three domains of CRIII, hydrophobic transmembrane, phosphorylated cytoplasmic, glycosylated extracellular. The domain designations are based on following characteristics. (i) Differential extraction, phase partitioning with Triton X-114, incorporation into liposomes all indicate CRIII is an intrinsic membrane domain. After binds collagen. (ii) Immunofluorescence microscopy reveals most nucleated cells express after extraction X-100, Triton-insoluble distributes fibrillar pattern at periphery closed loops partially co-distributed vimentin. contains phosphoserine residues which located cytoplasmic may interact cytoskeleton. (iii) 25% carbohydrate 8-10 asparagine-linked chains 2800 daltons each 65-kDa core peptide extracellular Peptide mapping trypsin defined 27-kDa fragment 35-kDa transmembrane fragment. These data suggest model for links cytoskeleton matrix.