Binding of osteopontin to the osteoclast integrin αvβ3

A. Miyauchi, J. Alvarez, E. M. Greenfield, A. Teti, M. Grano, S. Colucci, A. Zambonin-Zallone, F. P. Ross, S. L. Teitelbaum, D. Cheresh, K. A. Hruska

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Occupancy of the chicken osteoclast αvβ3 integrin stimulates immediate cell signals. Peptides from osteopontin containing Arg-Gly-Asp and peptides from the osteopontin and bone sialoprotein sequences containing Arg-Gly-Asp stimulated immediate reductions in osteoclast cytosolic Ca2+. The changes in cytosolic Ca2+ required the Arg-Gly-Asp sequence, and were blocked by LM609, a monoclonal antibody to the αvβ3 integrin. Osteoclast stimulation by the proteins through the integrin did not require immobilization since soluble peptides produced changes in cytosolic Ca2+ and inhibited osteoclast binding to bone particles and bone resorption. The decrease in cytosolic Ca2+ stimulated by osteopontin and related peptides was due to activation of a plasma membrane Ca2+-ATPase. Thus, the data suggest that ligand binding to the osteoclast αvβ3 integrin results in a reduction in cytosolic Ca2+ which participates in regulation of osteoclast function.

Original languageEnglish
Pages (from-to)132-135
Number of pages4
JournalOsteoporosis International
Issue number1 Supplement
StatePublished - Jan 1993


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