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PMID: 1385872 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Sensitivity to vanadate and isoforms of subunits A and B distinguish the osteoclast proton pump from other vacuolar H+ ATPases.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 89 ·No. 14 ·1992-07-15 ·Pages 6257-61

Chatterjee D, Chakraborty M, Leit M, Neff L, Jamsa-Kellokumpu S, Fuchs R, Baron R

Abstract

Analysis of proton (H+) transport by inside-out vesicles derived from highly purified chicken osteoclast (OC) membranes has revealed the presence of a newly discovered type of vacuolar H+ ATPase (V-ATPase). Unlike vesicles derived from any other cell type or organelle, H+ transport in OC-derived vesicles is sensitive to V-ATPase inhibitors (N-ethylmaleimide and Bafilomycin A1) and vanadate (IC50, 100 microM), an inhibitor previously found to affect only P-type ATPases. The OC H+ ATPase contains several V-like subunits (115, 39, and 16 kDa) but subunits A and B of the catalytic domain of the enzyme differ from that of other V-ATPases. In OCs, subunit A has a mass of 63 kDa instead of the 67-70 kDa expressed in monocytes, macrophages, and kidney microsomes, which contain a vanadate-insensitive H+ ATPase. Moreover, two types of 57- to 60-kDa B subunits are also found: one is expressed predominantly in OCs and the other is expressed in kidney microsomes. The OC H+ pump may therefore constitute a class of H+ ATPase with a unique pharmacology and specific isoforms of two subunits in the catalytic portion of the enzyme. This H+ ATPase is involved in resorption of bone and may be expressed in a cell-specific manner, thereby opening possibilities for therapeutic intervention.

MeSH Terms
Animals Biological Transport, Active Chickens Chromaffin Granules/enzymology Ethylmaleimide/pharmacology Female Isoenzymes/antagonists & inhibitors,chemistry Molecular Weight Osteoclasts/enzymology Proton-Translocating ATPases/antagonists & inhibitors,chemistry Vacuoles/enzymology Vanadates/pharmacology
Chemicals
Isoenzymes Vanadates Proton-Translocating ATPases Ethylmaleimide
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Chatterjee D
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.
Chakraborty M
Leit M
Neff L
Jamsa-Kellokumpu S
Fuchs R
Baron R
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.89.14.6257
Published
1992-07-15
Pages
6257-61
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC49479
Subset
IM
Grants
NIAMS NIH HHS · AR-41339 · United States
NIDCR NIH HHS · DE-04724 · United States
External Links
PubMed source DOI: 10.1073/pnas.89.14.6257 PMC Full Text View journal details
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