title: Characterization of proton transport in bone-derived membrane vesicles.
abstract: ATP-dependent proton transport was characterized in membrane vesicles, prepared by differential centrifugation from medullary bone of egg laying hens, a source rich in osteoclasts. The H(+)-ATPase present in this preparation showed the characteristics of a vacuolar H(+)-ATPase in its sensitivity to inhibitors, including bafilomycin A1, its sensitivity to cold treatment and its electrogenic mechanism. There was no evidence for a direct activation of the H(+)-ATPase by anions, including Cl-. These results are consistent with the view that the osteoclast, the cell responsible for bone resorption, secrets acid by means of a vacuolar H(+)-ATPase.
authors.affiliation: Department of Cell Biology, Astra Hässle AB, Mölndal, Sweden.
authors.forename: J P
authors.initials: JP
authors.lastname: Mattsson
authors.forename: B
authors.initials: B
authors.lastname: Wallmark
authors.forename: P
authors.initials: P
authors.lastname: Lorentzon
authors.forename: D J
authors.initials: DJ
authors.lastname: Keeling
mesh_terms: D000255:Adenosine Triphosphate; D000818:Animals; D001842:Bone and Bones / Q000378:metabolism*; D002645:Chickens; D003080:Cold Temperature; D005260:Female; D008565:Membrane Proteins / Q000378:metabolism; D008566:Membranes / Q000378:metabolism; D010010:Osteoclasts / Q000201:enzymology; D017494:Proton Pumps / Q000502:physiology*; D006180:Proton-Translocating ATPases / Q000378:metabolism
chemical_list: D008565:Membrane Proteins; D017494:Proton Pumps; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases