Recognition of osteopontin and related peptides by an α(v)β3 integrin stimulates immediate cell signals in osteoclasts

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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363 Scopus citations


We have investigated the nature of immediate cell signals produced by occupancy of the chicken osteoclast α(v)β3 integrin. Synthetic osteopontin 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 a monoclonal antibody to the α(v)β3 integrin, LM609. 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 appeared to be due to activation of a plasma membrane Ca2+-ATPase by calmodulin. Thus, the data suggest that ligand binding to the osteoclast α(v)β3 integrin results in calmodulin-dependent reduction in cytosolic Ca2+ which participates in regulation of osteoclast function.

Original languageEnglish
Pages (from-to)20369-20374
Number of pages6
JournalJournal of Biological Chemistry
Issue number30
StatePublished - 1991


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