Oct 1, 1989

The osteoclast functional antigen, implicated in the regulation of bone resorption, is biochemically related to the vitronectin receptor

The Journal of Cell Biology
J DaviesM Horton


We have defined the structure of the Osteoclast Functional Antigen (OFA) by immunological and biochemical means. OFA is an abundant surface antigen in human and animal osteoclasts and has been characterized previously by monoclonal antibodies 13C2 and 23C6, one of which mimicks the inhibitory activity of calcitonin on osteoclastic bone resorption. By the following criteria we show that OFA is a member of the integrin family of extracellular matrix receptors and is identical, or at least highly related, to the vitronectin receptor (VNR) previously isolated from placenta and melanoma cells. Immunoprecipitation analysis demonstrates that OFA from osteoclasts and a monkey kidney cell line Vero is a heterodimeric molecule of 140 kD (alpha chain) and 85 kD (beta chain) under nonreducing conditions; on reduction at least one low molecular mass (alpha') species (of approximately 30-kD size) is released, resulting in a 120/100-kD dimer. Immunoblots of OFA isolated from osteoclasts and Vero cells and VNR purified from placenta and probed with heterosera to OFA and monoclonal antibodies to platelet gp111a (VNR beta chain) show immunological cross-reactivity between the alpha chains of OFA and VNR and the use of gp111a as a beta chain by b...Continue Reading

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Mentioned in this Paper

CALCA gene
Monoclonal Antibodies
Monoclonal antibodies, antineoplastic
Immunofluorescence Assay
Calcitonin preparation
Protein Sequence Determination
Bone Resorption
Epithelial Cell of Renal Tubule
Placenta Specimen
Platelet Glycoproteins

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