[Partial purification and characterization of bone-resorbing factor from bovine bone matrix].
The mechanism of bone remodeling has been investigated by many researchers. However, little is known about the role of the local factors which exist in the bone matrix. In this study, the author attempted to purify the bone-resorbing factor from the bovine bone matrix and to find its role in bone remodeling. The demineralized bovine bone matrix was extracted with 4M Gdn-HCl and the bone-resorbing factor was purified by means of heparin affinity and gel filtration chromatography. The analysis of bone resorption was carried out by the measurement of the released 45Ca from the pre-labeled mouse calvariae. The results of this study were that the bone-resorbing factor in the bone matrix was suggested to be a heat-stable glycoprotein having a molecular size higher than 150,000, which stimulated osteoclastic bone resorption via a prostaglandin-mediated mechanism.
Mori
M
M
Second Department of Oral Surgery, Faculty of Dentistry, Tokyo Medical and Dental University.
D000818:Animals; D001857:Bone Matrix / Q000737:chemistry*; D001862:Bone Resorption; D002417:Cattle; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D016207:Cytokines / Q000032:analysis / Q000302:isolation & purification* / Q000502:physiology; D005260:Female; D006023:Glycoproteins / Q000302:isolation & purification; D051379:Mice; D008970:Molecular Weight; D011247:Pregnancy; D011453:Prostaglandins / Q000096:biosynthesis
D016207:Cytokines; D006023:Glycoproteins; D011453:Prostaglandins; C025940:bone resorption factor