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Research Article Free access | 10.1172/JCI118197

A ryanodine receptor-like molecule expressed in the osteoclast plasma membrane functions in extracellular Ca2+ sensing.

M Zaidi, V S Shankar, R Tunwell, O A Adebanjo, J Mackrill, M Pazianas, D O'Connell, B J Simon, B R Rifkin, and A R Venkitaraman

St. George's Hospital Medical School, University of London, United Kingdom.

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St. George's Hospital Medical School, University of London, United Kingdom.

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St. George's Hospital Medical School, University of London, United Kingdom.

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St. George's Hospital Medical School, University of London, United Kingdom.

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St. George's Hospital Medical School, University of London, United Kingdom.

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St. George's Hospital Medical School, University of London, United Kingdom.

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St. George's Hospital Medical School, University of London, United Kingdom.

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St. George's Hospital Medical School, University of London, United Kingdom.

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Published September 1, 1995 - More info

Published in Volume 96, Issue 3 on September 1, 1995
J Clin Invest. 1995;96(3):1582–1590. https://doi.org/10.1172/JCI118197.
© 1995 The American Society for Clinical Investigation
Published September 1, 1995 - Version history
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Abstract

Ryanodine receptors (RyRs) reside in microsomal membranes where they gate Ca2+ release in response to changes in the cytosolic Ca2+ concentration. In the osteoclast, a divalent cation sensor, the Ca2+ receptor (CaR), located within the cell's plasma membrane, monitors changes in the extracellular Ca2+ concentration. Here we show that a RyR-like molecule is a functional component of this receptor. We have demonstrated that [3H] ryanodine specifically binds to freshly isolated rat osteoclasts. The binding was displaced by ryanodine itself, the CaR agonist Ni2+ and the RyR antagonist ruthenium red. The latter also inhibited cytosolic Ca2+ elevations induced by Ni2+. In contrast, the responses to Ni2+ were strongly potentiated by an antiserum Ab129 raised to an epitope located within the channel-forming domain of the type II RyR. The antiserum also stained the surface of intact, unfixed, trypan blue-negative osteoclasts. Serial confocal sections and immunogold scanning electron microscopy confirmed a plasma membrane localization of this staining. Antiserum Ab34 directed to a putatively intracellular RyR epitope expectedly did not stain live osteoclasts nor did it potentiate CaR activation. It did, however, stain fixed, permeabilized cells in a distinctive cytoplasmic pattern. We conclude that an RyR-like molecule resides within the osteoclast plasma membrane and plays in important role in extracellular Ca2+ sensing.

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