Section Review: Oncologic, Endocrine & Metabolic: The vacuolar H⁺-ATPase: A potential target for drug development in bone diseases

References

• SUDA T, TAKAHASHI N, MARTIN TJ: Modulation of osteo-clast differentiation. Endocrine Reviews (1992) 13:66–80.
   PubMed Web of Science ®Google Scholar
• TETI A, MARCHISIO PC, ZAMBONIN ZALLONE A: Clearzone in osteoclast function: role of podosomes in regu-lation of bone-resorbing activity. Am. J. Physiol. (1991) 261:C1–C7.
   PubMed Web of Science ®Google Scholar
• KANEHISA J, YAMANAKA T, DOI S, TURKSEN K, HEERSCHEJNM, AUBIN JE, TAKEUCHI H: A band of F-actin contain-ing podosomes is involved in bone resorption by osteo-clasts. Bone (1990) 11:287–293.
   PubMed Web of Science ®Google Scholar
• MIYAUCHI A, ALVAREZ J, GREENFIELD E, TETI A, ZAM-BONIN ZALLONE A, ROSS FP, TEITELBAUM SL, CHERESH D, HRUSICA K: Matrix protein binding to the osteoclast adhesion integrin (ay) mediates a reduction in [Ca2+1i. J. Bone Miner. Res. (1991) 6:596.
   Google Scholar
• AUBIN JE: Osteoclast adhesion and resorption: The role of podosomes. J. Bone Miner. Res. (1992) 7(4):365.
   PubMed Web of Science ®Google Scholar
• BARON R, NEFF L, BROWN W, COURTOY PJ, LOUVARD D, FARQUHAR MG: Polarized secretion of lysosomal en-zymes: Co-distribution of cation-independent man-nose-6-phosphate receptors and lysosomal enzymes along the osteoclast exocytic pathway. J. Cell Biol. (1988) 106:1863–1872.
   PubMed Web of Science ®Google Scholar
• BARON R, NEFF L, LIPPINCOTT-SCHWARTZ J, LOUVARD D, MELLMAN I, HELENIUS A, MARSH M: Distribution of lysosomal membrane proteins in the osteodast and their relationship to acidic compartments. J. Cell Biol. (1985) 101:53a.
   PubMed Web of Science ®Google Scholar
• ANDERSSON G, EK-RYLANDER B, HAMMARSTROM LE,LINDSKOG S, TOVERUD SU: Immunocytochemical local-ization of a tartrate-resistant and vanadate-sensitive acid nucleotide tri-and diphosphatase. j IhStochem. Cy-tochem. (1986) 34:293–298.
   PubMed Web of Science ®Google Scholar
• BARON R, NEFF L, LOUVARD D, COURTOY PJ: Cell-medi-ated extracellular acidification and bone resorption: Evidence for a low pH in resorbing lacunae and local-ization of a 100 kDa lysosomal membrane protein at the osteoclast ruffled border. J. Cell Biol. (1985) 101:2210–2222.
   PubMed Web of Science ®Google Scholar
• SILVER A, MURRILLS Rj. ETHERINGTON DJ: Microelec-trode studies on the add microenvironrnent beneath adherent macrophages and osteoclasts. Exp. Cell Res. (1988) 175:266–276.
   PubMed Web of Science ®Google Scholar
• TETI A, BLAIR HC, SCHLESINGER P, GRANO M, ZAMBONIN ZALLONE A, KAHN AJ TEITELBAUM SL, HRUSKA KA: Extracellnlar protons acidify osteoclasts, reduce cytoso- lieand promote expression of cell-matrixattachment structures. J. Clin. Invest. (1989) 84:773–780.
   PubMedGoogle Scholar
• BARON R: Molecular mechanisms of bone resorption by the osteodast. Anat. Rec. (1989) 224:317–324.
   PubMedGoogle Scholar
• BLAIR HC, TEITELBAUM SL, GHISELLI R, GLUCK S: Osteo-elastic bone resorption by a polarized vacuolar proton pump. Science (1989) 245:855–857.
   PubMed Web of Science ®Google Scholar
• BEKKER PJ, GAY CV: Biochemical characterization of an electrogenic vacuolar proton pump in purified chicken osteoclast plasma membrane vesicles. J. Bone Miner. Res. (1990) 5:569–579.
   PubMed Web of Science ®Google Scholar
• VAANANEN HK, KARHUKORPI EK, SUNDQUIST K, WALL-MARK B, ROININEN I, HENTUNEN T, TUUKKANEN J, LAKICAKORPI P: Evidence for the presence of a proton pump of the vacuolar HtATPase type in the ruffled border of osteoclasts. J. Cell Biol. (1990) 111:1305–1311.
   PubMed Web of Science ®Google Scholar
• CHAI1hRJEE D, CHAKRABORTY M, LEIT M, NEFF L, JAMSA-KELLOKUMPU S, FUCHS R, BARON R: Sensitivity to vanailate and isofortns of subunits A and B distinguish the osteoclast proton pump from other vacuolar IltAT-Pases . Proc. Natl. Acad. Sci. USA (1992) 89:6257–6261.
   PubMed Web of Science ®Google Scholar
• LAITALA T, VAANANEN HK: Inhibition of bone resorp-tion in vitro by antisense RNA and DNA molecules targeted against carbonic anhydrase II or two subunits of vacuolar 11.-ATPase. J. Clin. Invest. (1994) 93:2311–2318.
   PubMed Web of Science ®Google Scholar
• GAY CV, MUELLER WJ: Carbonic anhydrase and osteo-clasts: loc.liTation by labelled inhibitor autoradiogra-phy. Science (1974) 183:432–434.
   Google Scholar
• MINKIN C, JENNINGS JM: Carbonic anhydrase and bone remodeling: sulfonamide inhibition of bone resorption in organ culture. Science (1972) 176:1031–1033.
   PubMed Web of Science ®Google Scholar
• WAITE LC, VOLKERT WA, KENNY AD: Inhibition of bone resorption by acetazolamide in the rat. Endocrinology (1970) 87:1129–1139.
   PubMedGoogle Scholar
• HUNTER SJ, SCHRAER H, GAY CV: Characterization of Isolated and cultured chick osteoclasts: the effects of acetazolsmirli-, calcitonin and parathyroid hormone on add production. J. Bone Miner. Res. (1988) 3:297–303.
   PubMed Web of Science ®Google Scholar
• RAVESLOOT J-H, EISEN T, BARON R, BORON WF: Role of Na../11* exchangers and vacuolar Htpumps in intracel-lular pH regulation in neonatal rat osteoclasts. J. Gen. Physiol. (1995) 105:177–208.
   Google Scholar
• HALL TJ, CHAMBERS TJ: Na+/Iftantiporter is the primary proton transport system used by osteoclasts during bone resorption. J. Cell. Physiol. (1990) 142:420–424.
   PubMed Web of Science ®Google Scholar
• HALL TJ, CHAMBERS TJ: Optimal bone resorption by Isolated rat osteoclasts requires chloride/bicarbonate exchange. Calcif. Tissue Int. (1989) 45 :378–380.
   PubMed Web of Science ®Google Scholar
• NORDSTOM T, ROTSTEIN OD, ROMANEK R, ASOTRA S, HEERSCHE JNM, MANOLSON MF, BRISSEAU GF, GRIN-STEIN S: Regulation of cytoplasmic pH in osteoclast - contribution of proton pumps and proton selective conductance. J. Biol. Chem. (1995) 270:2203–2212.
   PubMed Web of Science ®Google Scholar
• LEII A, BLAIR HC, TEITELBAUM SL, KAHN AJ, KOZIOL C, KONSEK J, ZAMBONIN-ZALLONE A, SCHLESINGER PH: Cytoplasmic pH regulation and chloride bicarbonate exchange in avian osteoclasts. J. Clin. Invest. (1989) 83:227–233.
   Google Scholar
• BARON R, NEFF L, BROWN W, LOUVARD D, COURTOY PJ:Selective internalization of the apical plasma mem-brane and rapid redistribution of lysosomal enzymes and mannose 6-phosphate receptors during osteoclast Inactivation by caldtonin. J. Cell Sci. (1990) 97:439–447.
   PubMed Web of Science ®Google Scholar
• BARON R, NEFF L, ROY C, BOISVERT A, CAPLAN M: Evidence for a high and specific concentration of (Na',10)-ATPase in the plasma membrane of the osteo-dast. Cell (1986) 46:311–320.
   PubMed Web of Science ®Google Scholar
• BEKKER PJ, GAY CV: Characterization of a caldum ATPase In osteodast plasma membrane. J. Bone Miner. Res. (1990) 5:557–567.
   PubMed Web of Science ®Google Scholar
• RAVESLOOT JH, YPEY DL, VRIJHEID-LAMMERS T, NI-JWEIDE PJ: Voltage-activated IC conductances in freshly isolated embryonic chicken osteoclasts. Proc. Natl. Acad, Sci. USA (1989) 86:6821–6825.
   PubMed Web of Science ®Google Scholar
• RAVESLOOT JH, YPEY DL, NIJWEIDE PJ, BUISMAN HP, VRIJHEID-LAMMERS T: Three voltage-activated IC con-ductances and an ATP-activated conductance in freshly Isolated embryonic chick osteoclasts. Pflugers Arch. (1989) 414:S166–S167.
   PubMedGoogle Scholar
• SIMS SM, KELLY MEM, DIXON SJ: le" and Cr currents infreshly isolated rat osteoclasts. Pflugers Arch. (1991) 419:358–370.
   PubMed Web of Science ®Google Scholar
• SIMS SM, DIXON SJ: Inwardly rectifying IC current inosteoclasts. Am. J. Physiol. (1989) 256:C1277–C1282.
   PubMed Web of Science ®Google Scholar
• SIMS SM, KELLY MEM, ARKETT SA, DIXON SJ: Electro-physiology of osteodasts. In: Biology and Physiology of the Osteoclast. Rifkin BR, Gay CV (Eds.). CRC Press, Boca Raton, Fla, (1991).
   Google Scholar
• SCHOPPA NE, SU Y, BARON R, BOULPAEP EL: Identifica-tion of single ion channels in neonatal rat osteodasts. J. Bone Miner. Res. (1990) 5:S204.
   Web of Science ®Google Scholar
• BLAIR HC, TEITELBAUM SL, TAN HL, KOZIOL CM SCHLESINGER PH: Passive chloride permeability charge coupled to 11+-ATPase of avian osteodast ruffled mem-brane. Am .J. Physiol. (1991) 260:C1315–C1324.
   PubMedGoogle Scholar
• BARON R, BARTKIEWICZ M, DAVID P, HERNANDO-SO-BRINO N: Acidification and bone resorption: the role and characteristics of V-ATPases in the osteodast. Organellar Proton-A7Pases. Nelson N (Ed.). RG Landes, Austin, TX (1995).
   Google Scholar
• BARON R, NEFF L, VUKASIN A: Basolateral targeting ofInfluenza virus and endolysosmal nature of the apical ruffled-border membrane distinguish osteoclasts from polarized epithelial cells.]. Bone Miner. Res. (1993) 8:S377.
   Google Scholar
• FORGAC M: Structure and function of vacuolar class ofATP-driven proton pumps. Physiol. Rev. (1989) 69:765–796.
   PubMed Web of Science ®Google Scholar
• NELSON N: Organellar proton-ATPases. Current Opinion in Cell Biology (1992)4:654–660.
   PubMedGoogle Scholar
• NELSON N: Molecular and cellular biology of F-and V-ATPases. In: Organellar Proton-A7Pases. Nelson N (Ed.). RG Landes, Austin, TX (1995).
   Google Scholar
• SUDHOF TC, FRIED VA, STONE DK, JOHNSTON PA, X1EX-S: Human endomembrane le-pump strongly resem-bles the ATP-synthetase of Archaebacteria. Proc. Natl. Acad. Sci. USA (1989) 86:6067–6071.
   PubMed Web of Science ®Google Scholar
• SHULL GE, LINGREL JB: Molecular Cloning of the RatStomach Ir/K+)-ATPase. J. Biol. Chem. (1986) 261:16788–16791.
   PubMed Web of Science ®Google Scholar
• GLUCK 5, KELLY S, AL-AWQATI Q: The proton transloca-tionATPase responsible for urinary acidification. J. Biol. Chem. (1982) 257:9230–9233.
   PubMed Web of Science ®Google Scholar
• GLUCK S, AL-AWQATI Q,: An electrogenic proton-translocation adenosine triphosphatase from bovine kidney medulla.]. Clin. Invest. (1984) 73: 1704-1710.
   Google Scholar
• BROWN D, GLUCK S, HARTWIG J: Structure of the novelmembrane-coating material in proton-secreting epi-thelial cells and identification as an HtATPase. J. Cell Biol. (1987) 105:1637–1648.
   PubMed Web of Science ®Google Scholar
• BOWMAN BJ, DSCHIDA WJ, HARRIS T, BOWMAN EJ: Thevacuolar ATPase of Neurospora crassa contains an Fl-like structure.]. Biol. Chem. (1989) 264:15606–15612.
   PubMed Web of Science ®Google Scholar
• MORIYAMA Y, NELSON N: Cold inactivation of vacuolar proton-ATPases. J. Biol. Chem (1989) 264:3577–3582.
   PubMed Web of Science ®Google Scholar
• NELSON N: Evolution of organellar proton-ATPases. Biocbim. Biophys. Acta (1992) 1100:109–124.
   PubMed Web of Science ®Google Scholar
• BELTRAN C, KOPECKY J, PAN Y-CE, NELSON H, NELSON N: Cloning and mutational analysis of the gene encod-ing subunit C of yeast vacuolar 11*-ATPase. J. Biol. Chem. (1992) 267:774–779.
   PubMed Web of Science ®Google Scholar
• HIRSCH S, STRAUSS A, MASOOD K, LEE S, SUKHATME V,GLUCK S: Isolation and sequence of a cDNA clone encoding the 31-kDa subunit of bovine vacuolar 11*-AT-Pase. .Proc. Natl. Acad. Sci. USA (1988) 85:3004–3008.
   PubMed Web of Science ®Google Scholar
• NELSON H, MANDIYAN S, NELSON N: The Sacchoromyusceranisiae VMA7 gene encodes a 14-kDa subunit of the vacuolar 11*-ATPases catalytic sector. J. Biol. Chem. (1994) 26924150–24155.
   Google Scholar
• SUSPEK F, SUPEKOVA L, MANDIYAN S, PAN YE, NELSONH, NELSON N: A novel accessory subunit for vacuolar 11+-ATPase from chromaffin granules. J. Biol. Chem. (1994) 269:24102–24106.
   PubMed Web of Science ®Google Scholar
• STONE DK, CRIDER BP, XIE XS: Structural properties ofvacuolar proton pumps. Kidney International (1990) 38:649–653.
   PubMed Web of Science ®Google Scholar
• FORGAC M: Structure, function and regulation of thecoated vesicle V-ATPase. J. Exp. Biol. (1992) 172:155–170.
   PubMed Web of Science ®Google Scholar
• GLUCK SL, NELSON RD, LEE BSM, HOLLIDAY LS, IYORI M:Properties of kidney plasma membrane vacuolar 11*-ATPases: proton pumps responsible for bicarbonate transport, urinary acidification, and acid-base homeo-stasis. In: Organellar Proton-ATPases. Nelson N (Ed.). RG Landes, Austin, TX (1995).
   Google Scholar
• PUOPOLO K, KUMAMOTOC, ADACHI I, MAGNER R, FOR-GAC M: Differential expression of the IV subunit of the vacuolar fe-ATPase in bovine tissues. J. Biol. Chem. (1992) 267:3696–3706.
   PubMed Web of Science ®Google Scholar
• NELSON RD, GUO X-L, MASOOD K, BROWN D, KALKBREN-NER M, GLUCK S: Selectively amplified expression of an isoform of the vacuolar 11*-ATPase 56-kilodalton subunit in renal intercalated celL Proc. Natl. Acad. Sci. USA (1992) 89:3541–3545.
   PubMed Web of Science ®Google Scholar
• VAN HILLE B, RICHENER H, SCHMID P, PUETTNER I, GREEN JR, BILBE G: Heterogeneity of vacuolar 11*-AllPase : differential expression of two human subunit B 'so-forms. Biochem. J. (1994) 303:191–198.
   PubMed Web of Science ®Google Scholar
• PENG S, CRIDER B, >LEE X, STONE D: Alternative mRNAsplicing generates tissue-specific isoforms of 116-kDa polypeptide of vacuolar pump. J. Biol. Chem. (1994) 269:17262–17266.
   PubMed Web of Science ®Google Scholar
• VAN HILLE B, RICHENER H, EVANS DB, GREEN JR, BILBEG: Identification of two subunit A isoforms of the vacuolar le-ATPase in human osteodastotna. J. Biol. Chem. (1993) 268:7075–7080.
   PubMed Web of Science ®Google Scholar
• HERNANDO-SOBRINO N, BARTKIEWICZ M, FABRICANT C,DAVID P, COLLIN-OSDOBY P, OSDOBY P, BARON R: The osteoclast H-ATPases isolation of the genes encoding the catalytic subunits and studies of their expression in chicken tissues. J. Bone Miner. Res. (1993) 8\(Suppl. 1):S128.
   Google Scholar
• HERNANDO-SOBRINO N, BARTKIEWICZ M, COLLIN-OS-DOBY P, OSDOBY P, BARON R: Alternative splicing generates a new isoform of the catalytic A subunit of the vacuolar It-ATPase. Proc. Natl. Acad. Sci. USA (1995) 92:6087–6091.
   PubMed Web of Science ®Google Scholar
• GLUCK SL, NELSON RD, LEE BS, WANG Z-Q, GUO X-L, FU J-Y, ZHANG K: Biochemistry of the renal V-ATPase. J. Exp. Biol. (1992) 172:219–230.
   PubMed Web of Science ®Google Scholar
• CHATTERJEE D, NEFF L, CHAKRABORTY M, FABRICANT C, BARON R: Sensitivity to nitrate and other oxyanions further distinguishes the vanadate-sensitive osteociast proton pump from other vacuolar It-ATPases. Bio-chemistry (1993) 32:2808–2812.
   Google Scholar
• DAVID P, BARON R: The catalytic cycle of the vacuolar It-ATPase. Comparison of proton transport in kidney-and osteoclast-derived vesicles. J. Biol. Chem. (1994) 269:30158–30163.
   Google Scholar
• MATTISSON JP, SCHLESINGER PH, KEELING DJ, TEML-BAUM SL, STONE DK, XIE XS: Isolation and reconstitu-tion of a vacuolar-type proton pump of osteodast membranes. J. Biol. Chem. (1994) 269:24979–24982.
   PubMedGoogle Scholar
• BARON R, BARTKIEWICZ M, CHA1IERJEE D, CHAK-RABORTY M, DAVID P, FABRICANT C, HERNANDO N: Characterization of the osteodast vacuolar It-ATPase: biochemistry, subunit composition and cloning of cata-lytic subunits. Im Molecular and cellular mechanisms of I-T-transport. Hirst BH (Ed.). Springer-Verlag, Berlin (1994).
   Google Scholar
• BARTKIEWICZ M, HERNANDO N, REDDY SV, ROODMANGD, BARON R: Characterization of the osteoclast vacuo-lar it-ATPase B subunit. Gene (1995). In press.
   Google Scholar
• VAN HILLF B, VANEK M, RICHENER H, GREEN JR, BILBEG: Cloning and tissue distribution of subunits C, D, and E of the human vacuolar It-ATPase. Biochem. Biophys. Res. Commun. (1993) 197:15–21.
   PubMed Web of Science ®Google Scholar
• BRUBMEYER C, CROSS R, PENEFSKY H: Mechanism ofATP hydrolysis by beef heart mitochondria' ATPase. J. Biol. Chem. (1982) 257:12092–12100.
   PubMedGoogle Scholar
• UCHIDA E, OHSUMI Y, ANRAKU Y: Characterization andfunction of catalytic subunit alpha of It-translocating adenosine triphosphatase from vacuolar membranes of Saccbaromyces cerevistae. A study with 7-chloro-4-nitrobenzo-2-oxa,-1,3-diazole. J. Biol. Chem. (1988) 263:45–51.
   Google Scholar
• HUTTON RE, BOYER PD: Subunit interaction during catalysis: alternating site cooperativity of mitochon-dria' adenosine triphosphatase. J. Biol. Chem. (1979) 254:9990–9993.
   PubMed Web of Science ®Google Scholar
• O'NEAL CC, BOYER PD: Assessment of the rate of boundsubstrate interconversion and of ATP acceleration of product release during catalysis by mitochondria' adenosine triphosphatase. J. Biol. Chem. (1984) 259:5761–5767.
   PubMed Web of Science ®Google Scholar
• KASHO VN, BOYER PD: Vacuolar ATPases, like Ft/Fo-AT-Pases, show a strong dependence of the reaction veloc-ity on the binding of more than one ATP per enzyme. Proc. Natl. Acad. Sci. USA (1989) 86:8708–8711.
   PubMed Web of Science ®Google Scholar
• ANRAKU Y, UMENOTO N, HIRATA R, WADY Y: Structureand function of the yeast vacuolar membrane proton ATPase. J. Bioener. Biomernbr. (1989) 21:589.
   PubMed Web of Science ®Google Scholar
• PENEFSKY HS, CROSS EL: Structure and mechanism ofFO,F1-Type ATP synthases and ATPases. In: Advances in Enzymology and Related Areas of Molecular Biology. Meister A (Ed.). John Wiley & Sons, Inc., New York (1991).
   Google Scholar
• WAKER JE, FEARNLEY IM, GAY NJ, GIBSON BW, NORTHROP FD, POWELL SJ, RUNSWICK MJ, SARASTE M, TYBULEWICZ VL: Primary structure and subunit sto-chiometry of Fl-ATPase from bovine mitochondria. J. Mol. Biol.(1985) 184:677–701.
   PubMed Web of Science ®Google Scholar
• MANOLSON MF, REA PA, POOLE RJ: Identification of BzATP and DCCD-binding subunits of a higher plant 11-translocation ATPase. J. Biol. Chem. (1983) 260:12273–12279.
   Google Scholar
• ARAI K, SHIMAYA A, HIRATANI N, OHKUMA S: Purifica-tion and characterization of lysosomal lt-ATPase. J. Biol. Chem. (1993) 268:5649–5660.
   PubMed Web of Science ®Google Scholar
• DAVID P, BARON R: Comparison of the catalytic cycle in osteoclast and kidney vacuolar HtATPases and their transition state inhibition by vanadate. J. Bone Miner. Res. (1994) 9\(Suppl. 1):177S.
   Google Scholar
• ZHANG J, MYERS M, FORGAC M: Characterization of the Vo domain of the coated vesicle (1t)-ATPase. J. Biol. Chem. (1992) 267:9773–9778.
   PubMed Web of Science ®Google Scholar
• XIE X, STONE D: Partial resolution and reconstitution ofthe subunits of the clathrin-coated vesicle proton AT-Pase responsible for Ca2*-activated ATP hydrolysis. J. Biol. Chem. (1988) 263:9859–9867.
   PubMed Web of Science ®Google Scholar
• BELTRAN C, NELSON N: The membrane sector of vacuo-lar It-ATPases by itself is impermeable to protons. Ada Physfol. Scand. (1992) 146:41–47.
   PubMed Web of Science ®Google Scholar
• CRIDER BP, XIE XS, STONE DK: Bafilomydn inhibits proton flow through the It-channel of vacuolar proton pumps. J. Biol. Chem. (1994) 269:17379–17381.
   PubMed Web of Science ®Google Scholar
• ZHANG J, FORGAC M: Proton conduction and bafilomy-cin binding by the V. Domain of the coated vesicle V-ATPase. J. Biol. Chem. (1994) 269:23518–23523.
   PubMed Web of Science ®Google Scholar
• BOWMAN EJ, SIEBERS A, ALTENDORF K: Bafilomycins: A class of inhibitors of membrane ATPases from micro-organisms, animal cells, and plant cells. Proc. Natl, Acad. Sci. USA (1988) 85:7972–7976.
   PubMed Web of Science ®Google Scholar
• MATTSSON JP, VAANANEN HK, WALLMARK B, LOREN-TZON P: Omeprazole and bafliomycin, two proton pump inhibitors: differentiation of their effects on gastric, kidney and bone It-translocating ATPases. Bio-chim. Biophys. Acta (1991) 1065:261–268.
   PubMed Web of Science ®Google Scholar
• SUNDQUIST K, LAKKAKORPI P, WALLMARK B, VAANANEN K: Inhibition of osteociast proton transport by bafilomydn-A1 abolishes bone resorption. Biochem. Biophys. Res. Commun. (1990) 168:309–313.
   PubMed Web of Science ®Google Scholar
• SASAKI T, HONG MH, UDAGAWA N, MORIYAMA Y: Ex-pression of vacuolar It-ATPase in osteoclasts and its role in resorption_ Cell & Tissue Research (1994) 278:265–271.
   Google Scholar
• ARAI H, BERNE M, TERRES G, TRRES H, PUOPOLO K, FORGAC M: Subunit composition and ATP site labeling of the coated vesicle proton-translocation adenosine triphosphatase. Biochemistry (1987) 26:6632–6638.
   PubMed Web of Science ®Google Scholar
• FORGAC M, CANTLEY L: Characterization of the ATP-de- pendent proton pump of clathrin-coated vesicles. J. Biol. Chem. (1984) 259:8101–8105.
   Google Scholar
• FENG Y, FORGAC M: Cysteine 254 of the 73-kDa A subunit is responsible for inhibition of the coated vesicle litATPase upon modification by sulfhydryl reagents. J. Biol. Chem. (1992) 267:5817–5822.
   PubMed Web of Science ®Google Scholar
• TAIZ L, NELSON H, MAGGERT K, MORGAN L, YATABE B, TA1Z SL, RUBINSTEIN B, NELSON N: Functional analysis of conserved cysteine residues in the catalytic subunit of the yeast vacuolar IrtATPase. Biochim. Biophys. Acta (1994) 1194:329–334.
   PubMed Web of Science ®Google Scholar
• PUOPOLO K, KUMAMOTO C, ADACHI I, FORGAC M: A single gene encodes the catalytic 'A' subunit of the bovine vacuolar ii-ATPase. J. Biol. Chem. (1991) 266:24564–24572.
   PubMed Web of Science ®Google Scholar
• HIRATA R, OHSUMI Y, NAKANO A, KAWASAKI H, ANRAKU Y: Molecular Structure of a gene, VMA1, encoding the catalytic subunit of IV translocation adenosine triphos-phatase from vacuolar membranes of Saccbaromyces cerevisiae. J. Biol. Chem. (1990) 265:6726–6733.
   PubMed Web of Science ®Google Scholar
• FENG Y, FORGAC M: Inhibition of vacuolar fitATPase by disulfide bond formation between cysteine 254 and cysteine 532 in subunit A. J. Biol. Chem. (1994) 269:13224–13230.
   PubMed Web of Science ®Google Scholar
• FENG Y, FORGAC M: A novel mechanism for regulationof vacuolar acidification. J. Biol. Chem. (1992) 267:19769–19772.
   PubMed Web of Science ®Google Scholar
• BOWMAN EJ: Comparison of the vacuolar membraneATPase of Neurospora crassa with the mitochondrial and plasma membrane ATPases. J. Biol. Chem. (1983) 258:15238–15244.
   PubMedGoogle Scholar
• MANDALA S, TA1Z L: Proton transport in isolated vacu-oles from corn coleoptiks. Plant Physiol. (1985) 78:104–109.
   PubMed Web of Science ®Google Scholar
• ARAI H, PINK S, FORGAC M: Interaction of anions and ATP with the coated vesicle proton pump. Biochemistry (1989) 28:3075–3082.
   PubMed Web of Science ®Google Scholar
• KANE PM, YAMASHIRO CT, STEVENS TH: Biochemical characterization of the yeast vacuolar IltAITase. J. Biol. Chem. (1989) 264:19236–19244.
   PubMed Web of Science ®Google Scholar
• DSCHIDA wjA, BOWMAN BJ: The vacuolar ATPase: sulfite stabilization and the mechanism of nitrate inactivation. J. Biol. Chem. (1995) 270:1557–1563.
   PubMed Web of Science ®Google Scholar
• SACHS G, MUNSON K, BALAJ1 V, ACRES-FISCHER D, HERSEY S, HALL K: Functional domains of the gastric HVICtATPase. J. Bioener. Biomembr. (1989) 21:573.
   PubMedGoogle Scholar
• CLYNN IM, KARLISH SJ: Occluded cations in active trans-port. Annual Review of Biochemist?), (1990) 59:171–205.
   PubMed Web of Science ®Google Scholar
• AL-AWQAT1 Q: Proton-translocating ATPases. Cell Biol. (1986) 2:179–199.
   Web of Science ®Google Scholar
• CHATLEY L, JR, CANTLEY L, JOSEPHSON L: A charac-terization of vanadate interactions with the (Na,K) -ATPase. J. Biol. Chem. (1978) 253:7361–7368
   PubMedGoogle Scholar
• MORIYAMA Y, NELSON N: The purified ATPase from chromaffin granule membranes is an anion-dependent proton pump. J. Biol. Chem. (1987) 262:9175–9180.
   PubMed Web of Science ®Google Scholar
• LINDBERG P, BRANDSTORM A, WLLMARK B, MATTSSON H, RIKNER L, HOFFMANN KJ: Omeprazole: the first pro-ton pump inhibitor. Medicinal Research Reviews (1990) 10:1–54.
   PubMed Web of Science ®Google Scholar
• LORENTZON P, JACKSON R, WLLMARK B, SACHS G: Inhi-bition of (Ir/KtATPase by omeprazole in isolated gas-tric vesicles requires proton transport. Biochim Biophys. Acta (1987) 897:41–51.
   PubMed Web of Science ®Google Scholar
• TUUKKANEN J, VAANANEN HK: Omeprazole, a specific inhibitor of 11*-KtATPase, inhibits bone resorption in vitro. Calcif. Tissue Int. (1986) 38:123–125.
   PubMed Web of Science ®Google Scholar
• MIZUNASHI K, FURUKAWA Y, KATANO K, ABE K: Effect of omeprazole, an inhibitor of H7V-ATPase, on bone resorption in humans. Calcif. Tissue Int. (1993) 53:21–25.
   PubMed Web of Science ®Google Scholar
• KHARODE Y, BUDMAN L, CALTABIANO S, CORBIN A, MARZOLF J, MCCORMACK N, PEGG M, TAMASI J, BEX F: Anti-resorptive properties of WY-47,766, a novel bone-sparing compound. J. Bone Miner. Res. (1992) 7\(Suppl. 1):S139.
   Google Scholar
• FABRICANT C, DAVID P, CHATTERJEE D, BARON R: The omeprazole analog MY-47766] is a selective inhibitor of vacuolar-type IV-ATPases. J. Bone Miner. Res. (1993) 8\(Suppl. 1):S392.
   Google Scholar
• CORBETT JW, KERR JS, HOLIDAY LS, LEE BS, BOS WELL GA, HARLOW PP, WONG PC, GLUCK SL: Novel in vitro anti-resorptive agents, inhibitors of the osteoclast iltAT-Pase. J. Bone Miner. Res. (1994) 9\(Suppl. 1):200S.
   Google Scholar
• FLEISCH H: Bisphosphonates - history and experimen-tal basis. Bone (1987) 8:S23–S28.
   PubMed Web of Science ®Google Scholar
• FLEISCH H: Bisphosphonates in Bone Disease . Stampfli, Berne (1993).
   Google Scholar
• FLEISCH H: Bisphosphonates pharmacology and use in the treatment of tumor-induced hypercalcaemic and metastatic bone disease. Drugs (1991) 42:19–944.
   PubMedGoogle Scholar
• SATO M, GRASSER W, ENDO N, AKINS R, SIMMONS H, THOMPSON DD, GOLUB E, RODAN GA: Bisphosphonate action: akndronate localization in rat bone and effects on osteoclast uhrastructure. J. Clin.Invest.(1991) 88: 2095–2105.
   PubMed Web of Science ®Google Scholar
• MURAKAMI H, TAKAHASHI N, UDAGAWA N, TANAKA S, NAKAMLTRA I, ZHANG A, SUDA T: Tiludronate selectively affects polarized osteodasts with the ringed structure of podosomes. J. Bone Miner. Res. (1994) 9\(Suppl. 1):320S.
   Google Scholar
• CARANO A, TEITELBAUM SL, KONSEK JD, SCHLESINGER PH,BLAIR HC: Bisphosphonates directly inhibit the bone resorption activity of isolated avian osteodasts in vitro. Clin. Invest. (1991) 85:456–461.
   Google Scholar
• ZIMOLO Z, WESOLOWSKI G, RODAN G: Aminobisphos-phonate alendronate inhibits Natindependent acid ex-trusion (H-pumping) in osteoclast attached to bone. J. Bone Miner. Res. (1994) 9\(Suppl. 1):201S.
   Google Scholar
• ZIMOLO Z, WESOLOWSKI G, RODAN G: Osteoclasts at-tached to bone, but not glass exhibit Na-independent extrusion (H.-pumping). J. Bone Miner. Res. (1994) 9\(Suppl. 1):248S.
   Google Scholar
• DAVID P, NGUYEN H, BARBIER A, BARON R: Tiludronate Is a potent and specific inhibitor of the osteoclast vacuolar litATPase. Bone (1995) 16\(Suppl. 1):166S.
   Google Scholar