Ultracytochemical evidence for a proton-pump adenosine triphosphatase in chick osteoclasts |
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Authors: | Toskitaka Akisaka Dr Carol V Gay |
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Institution: | (1) Molecular and Cell Biology Program, The Pennsylvania State University, University Park, Pennsylvania, USA;(2) 508 Mueller Laboratory, The Pennsylvania State University, 16802 University Park, PA, USA;(3) Present address: Department of Anatomy, School of Dentistry, Hiroshima University, Kasumi 1-2-3, 734 Hiroshima, Japan |
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Abstract: | Summary The distribution of Mg+ +-ATPase in osteoclasts along the endosteal surface of the chick tibia was investigated by neutral and alkaline pH cytochemical methods at the electron-microscopic level. Reaction product was observed in mitochondria, cytoplasmic vesicles, and ruffled-border membrane. Levamisole, ouabain, and vanadate did not affect the enzymatic activity. Para-chloromercuribenzoic acid (PCMB) prevented staining of mitochondria, ruffled border, and most cytoplasmic vesicles. Tri-n-butyltin decreased the amount of reaction product in cytoplasmic vesicles and ruffled-border membrane, but did not inhibit reaction product formation within mitochondria. Duramycin, which is a potent inhibitor for proton-pump ATPase, blocked reaction-product formation along the ruffled-border membrane, in mitochondria, and in cytoplasmic vesicles at alkaline pH, but not at neutral pH. It is concluded that the alkaline pH method for Mg+ +-ATPase appears to demonstrate sites of proton-pump ATPase activity. |
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Keywords: | Osteoclasts H+-ATPase Ultracytochemistry Chicken |
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