Abstract
Chondroadherin, which is reported to be synthesized by chondrocytes and to promote their attachment, was purified from bovine bone. It was a minor component of bone organic matrix, and was present in the 4 M guanidine extract of demineralized bone. Chondroadherin promoted attachment of osteoblastic cells to solid-state substrates, and bound to collagen. Binding of chondroadherin to collagen was significantly higher than that of osteonectin or decorin. These findings imply that chondroadherin may play a role in maintaining bone cells on the collagen matrices of bone.
MeSH terms
-
Amino Acid Sequence
-
Amino Acids / analysis
-
Animals
-
Blotting, Western
-
Bone and Bones / chemistry*
-
Bone and Bones / cytology
-
Bone and Bones / metabolism
-
Cattle
-
Cell Adhesion
-
Collagen / metabolism*
-
Decorin
-
Electrophoresis, Polyacrylamide Gel
-
Enzyme-Linked Immunosorbent Assay
-
Extracellular Matrix Proteins / chemistry
-
Extracellular Matrix Proteins / isolation & purification
-
Extracellular Matrix Proteins / physiology*
-
Molecular Sequence Data
-
Molecular Weight
-
Osteoblasts / cytology
-
Osteoblasts / metabolism*
-
Osteonectin / metabolism
-
Protein Binding
-
Proteoglycans / metabolism
-
Serum Albumin, Bovine / metabolism
Substances
-
Amino Acids
-
Decorin
-
Extracellular Matrix Proteins
-
Osteonectin
-
Proteoglycans
-
chondroadherin
-
Serum Albumin, Bovine
-
Collagen