Premium
The partial degradation of osteonectin by a bone‐derived metalloprotease enhances binding to type I collagen
Author(s) -
Tyree Bernadette
Publication year - 1989
Publication title -
journal of bone and mineral research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.882
H-Index - 241
eISSN - 1523-4681
pISSN - 0884-0431
DOI - 10.1002/jbmr.5650040612
Subject(s) - osteonectin , type i collagen , metalloproteinase , degradation (telecommunications) , chemistry , matrix metalloproteinase , microbiology and biotechnology , biochemistry , medicine , biology , enzyme , alkaline phosphatase , computer science , osteocalcin , telecommunications
Cultured neonatal rat calvaria produce latent metalloproteases capable of degrading collagen, gelatin, and osteonectin. The osteonectin‐degrading activity was further characterized and found to be optimally active between pH 6 and 8 and inhibited with EDTA and 1,10‐phenanthroline but not phenylmethylsulfonyl fluoride. Analysis of the degradation products of osteonectin by SDS‐PAGE in the presence of dithiothreitol showed the generation of a somewhat stable 32,000 mw cleavage product. Comparison of the binding properties of this cleavage product with intact osteonectin indicated that the fragment retained its ability to bind hydroxyapatite in the presence of high salt (2 M NaCl). Importantly, the binding of osteonectin to type I collagen fibrils was enhanced by limited proteolysis.