Evidence for a high and specific concentration of (Na+,K+)ATPase in the plasma membrane of the osteoclast.
During bone resorption, the osteoclast actively acidifies a limited extracellular compartment. We hypothesized that, like other cells engaged in ion transport and proton translocation, the osteoclast's membrane might be highly enriched in sodium pumps. Using monoclonal antibodies to both the alpha and the beta subunits, immunoblot analysis, and [3H]ouabain binding, we have demonstrated that the osteoclast plasma membrane is both highly and specifically enriched in (Na+,K+)ATPase, compared with other bone cells, monocytes, macrophages, and other blood and bone marrow cells. The density of binding sites on the osteoclast is equivalent to that of kidney tubule cells. This observation is consistent with the hypothesis that the (Na+,K+)ATPase plays a role in the mechanism of bone resorption, possibly coupled with secondary active calcium and/or proton transport. Monoclonal antibodies against the (Na+,K+)ATPase can therefore be used as specific markers for the osteoclast in bone and bone marrow preparations.
D000818:Animals; D001862:Bone Resorption; D002454:Cell Differentiation; D002462:Cell Membrane / Q000201:enzymology*; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D007473:Ion Channels / Q000201:enzymology / Q000502:physiology; D010010:Osteoclasts / Q000166:cytology / Q000201:enzymology*; D010042:Ouabain / Q000378:metabolism; D011955:Receptors, Drug / Q000032:analysis; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*
D007473:Ion Channels; D011955:Receptors, Drug; C028996:cardiac glycoside receptors; D010042:Ouabain; D000254:Sodium-Potassium-Exchanging ATPase