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Volumn 292, Issue 1, 2007, Pages

New insights into the regulation of V-ATPase-dependent proton secretion

Author keywords

Cytoskeleton; Epididymis; Kidney; Plasma membrane; Proton pumping ATPase; Vesicle trafficking

Indexed keywords

ACTIN; ADENYLATE CYCLASE; CADMIUM; HOLOENZYME; PROTON; PROTON PUMP; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 33846268425     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.00340.2006     Document Type: Review
Times cited : (107)

References (140)
  • 2
    • 0035009245 scopus 로고    scopus 로고
    • Endocytic traffic in polarized epithelial cells: Role of the actin and microtubule cytoskeleton
    • Apodaca G. Endocytic traffic in polarized epithelial cells: role of the actin and microtubule cytoskeleton. Traffic 2: 149-159, 2001.
    • (2001) Traffic , vol.2 , pp. 149-159
    • Apodaca, G.1
  • 3
    • 0037125922 scopus 로고    scopus 로고
    • Localization of subunits D, E, and G in the yeast V-ATPase complex using cysteine-mediated cross-linking to subunit B
    • Arata Y, Baleja J, Forgac M. Localization of subunits D, E, and G in the yeast V-ATPase complex using cysteine-mediated cross-linking to subunit B. Biochemistry 41: 11301-11307, 2002.
    • (2002) Biochemistry , vol.41 , pp. 11301-11307
    • Arata, Y.1    Baleja, J.2    Forgac, M.3
  • 5
    • 0019225817 scopus 로고
    • Luminal acidification by the perfused rat cauda epididymidis
    • Au C, Wong P. Luminal acidification by the perfused rat cauda epididymidis. J Physiol 309: 419-427, 1980.
    • (1980) J Physiol , vol.309 , pp. 419-427
    • Au, C.1    Wong, P.2
  • 6
    • 0034992010 scopus 로고    scopus 로고
    • Remodeling the cellular profile of collecting ducts by chronic carbonic anhydrase inhibition
    • Bagnis C, Marshansky V, Breton S, Brown D. Remodeling the cellular profile of collecting ducts by chronic carbonic anhydrase inhibition. Am J Physiol Renal Physiol 280: F437-F448, 2001.
    • (2001) Am J Physiol Renal Physiol , vol.280
    • Bagnis, C.1    Marshansky, V.2    Breton, S.3    Brown, D.4
  • 8
    • 0028269161 scopus 로고
    • Adaptation of inner medullary collecting duct vacuolar H-adenosine triphosphatase to chronic acid or alkali loads in the rat
    • Bastani B, McEnaney S, Yang L, Gluck S. Adaptation of inner medullary collecting duct vacuolar H-adenosine triphosphatase to chronic acid or alkali loads in the rat. Exp Nephrol 2: 171-175, 1994.
    • (1994) Exp Nephrol , vol.2 , pp. 171-175
    • Bastani, B.1    McEnaney, S.2    Yang, L.3    Gluck, S.4
  • 9
    • 0025738533 scopus 로고
    • Expression and distribution of renal vacuolar proton-translocating adenosine triphosphatase in response to chronic acid and alkali loads in the rat
    • Bastani B, Purcell H, Hemken P, Trigg D, Gluck S. Expression and distribution of renal vacuolar proton-translocating adenosine triphosphatase in response to chronic acid and alkali loads in the rat. J Clin Invest 88: 126-136, 1991.
    • (1991) J Clin Invest , vol.88 , pp. 126-136
    • Bastani, B.1    Purcell, H.2    Hemken, P.3    Trigg, D.4    Gluck, S.5
  • 11
    • 33644935227 scopus 로고    scopus 로고
    • + ATPase: Molecular structure and function, physiological roles and regulation
    • + ATPase: molecular structure and function, physiological roles and regulation. J Exp Biol 209: 577-589, 2006.
    • (2006) J Exp Biol , vol.209 , pp. 577-589
    • Beyenbach, K.W.1    Wieczorek, H.2
  • 12
    • 10444262920 scopus 로고    scopus 로고
    • Polyphosphoinositides-dependent regulation of the osteoclast actin cytoskeleton and bone resorption (Abstract)
    • Biswas RS, Baker de A, Hruska KA, Chellaiah MA. Polyphosphoinositides-dependent regulation of the osteoclast actin cytoskeleton and bone resorption (Abstract). BMC Cell Biol 5: 19, 2004.
    • (2004) BMC Cell Biol , vol.5 , pp. 19
    • Biswas, R.S.1    Baker de, A.2    Hruska, K.A.3    Chellaiah, M.A.4
  • 13
    • 0024461376 scopus 로고
    • Osteoclastic bone resorption by a polarized vacuolar proton pump
    • Blair H, Teitelbaum S, Ghiselli R, Gluck S. Osteoclastic bone resorption by a polarized vacuolar proton pump. Science 245: 855-857, 1989.
    • (1989) Science , vol.245 , pp. 855-857
    • Blair, H.1    Teitelbaum, S.2    Ghiselli, R.3    Gluck, S.4
  • 16
    • 0031889725 scopus 로고    scopus 로고
    • Cold-induced microtubule disruption and relocalization of membrane proteins in kidney epithelial cells
    • Breton S, Brown D. Cold-induced microtubule disruption and relocalization of membrane proteins in kidney epithelial cells. J Am Soc Nephrol 9: 155-166, 1998.
    • (1998) J Am Soc Nephrol , vol.9 , pp. 155-166
    • Breton, S.1    Brown, D.2
  • 18
    • 0342696782 scopus 로고    scopus 로고
    • Distribution of the vesicle-associated proteins, b-COP and cellubrevin in the kidney and epididymis (Abstract)
    • Breton S, Heller E, Brown D. Distribution of the vesicle-associated proteins, b-COP and cellubrevin in the kidney and epididymis (Abstract). J Am Soc Nephrol 8: 58A, 1997.
    • (1997) J Am Soc Nephrol , vol.8
    • Breton, S.1    Heller, E.2    Brown, D.3
  • 20
    • 0034033704 scopus 로고    scopus 로고
    • Tetanus toxin-mediated cleavage of cellubrevin inhibits proton secretion in the male reproductive tract
    • Breton S, Nsumu N, Galli T, Sabolic I, smith P, Brown D. Tetanus toxin-mediated cleavage of cellubrevin inhibits proton secretion in the male reproductive tract. Am J Physiol Renal Physiol 278: F717-F725, 2000.
    • (2000) Am J Physiol Renal Physiol , vol.278
    • Breton, S.1    Nsumu, N.2    Galli, T.3    Sabolic, I.4    smith, P.5    Brown, D.6
  • 25
    • 0033981348 scopus 로고    scopus 로고
    • + V-ATPase-dependent luminal acidification in the kidney collecting duct and the epididymis/vas deferens: Vesicle recycling and transcytotic pathways
    • + V-ATPase-dependent luminal acidification in the kidney collecting duct and the epididymis/vas deferens: vesicle recycling and transcytotic pathways. J Exp Biol 203: 137-145, 2000.
    • (2000) J Exp Biol , vol.203 , pp. 137-145
    • Brown, D.1    Breton, S.2
  • 26
    • 0030294128 scopus 로고    scopus 로고
    • Mitochondria-rich, proton-secreting epithelial cells
    • Brown D, Breton S. Mitochondria-rich, proton-secreting epithelial cells. J Exp Biol 199: 2345-2358, 1996.
    • (1996) J Exp Biol , vol.199 , pp. 2345-2358
    • Brown, D.1    Breton, S.2
  • 27
    • 0001480782 scopus 로고    scopus 로고
    • +V-ATPase/proton pump)
    • edited by Seldin DW and Giebisch G. Philadelphia, PA: Lippincott Williams & Wilkins
    • +V-ATPase/proton pump). In: The Kidney, Physiology and Pathophysiology, edited by Seldin DW and Giebisch G. Philadelphia, PA: Lippincott Williams & Wilkins, 2000, p. 171-191.
    • (2000) The Kidney, Physiology and Pathophysiology , pp. 171-191
    • Brown, D.1    Breton, S.2
  • 29
    • 0024240241 scopus 로고
    • Localization of a proton-pumping ATPase in rat kidney
    • Brown D, Hirsch S, Gluck S. Localization of a proton-pumping ATPase in rat kidney. J Clin Invest: 2114-2126, 1988.
    • (1988) J Clin Invest , vol.82 , Issue.6 , pp. 2114-2126
    • Brown, D.1    Hirsch, S.2    Gluck, S.3
  • 30
    • 0026795802 scopus 로고
    • A plasma membrane proton ATPase in specialized cells of rat epididymis
    • Brown D, Lui B, Gluck S, Sabolic I. A plasma membrane proton ATPase in specialized cells of rat epididymis. Am J Physiol Cell Physiol 263: C913-C916, 1992.
    • (1992) Am J Physiol Cell Physiol , vol.263
    • Brown, D.1    Lui, B.2    Gluck, S.3    Sabolic, I.4
  • 31
    • 0022494872 scopus 로고
    • The "coat" of kidney intercalated cell tubulovesicles does not contain clathrin
    • Brown D, Orci L. The "coat" of kidney intercalated cell tubulovesicles does not contain clathrin. Am J Physiol Cell Physiol 250: C605-C608, 1986.
    • (1986) Am J Physiol Cell Physiol , vol.250
    • Brown, D.1    Orci, L.2
  • 32
    • 0025913065 scopus 로고
    • Colchicine-induced redistribution of proton pumps in kidney epithelial cells
    • Brown D, Sabolic I, Gluck S. Colchicine-induced redistribution of proton pumps in kidney epithelial cells. Kidney Int Suppl 33: S79-S83, 1991.
    • (1991) Kidney Int Suppl , vol.33
    • Brown, D.1    Sabolic, I.2    Gluck, S.3
  • 33
    • 0030938766 scopus 로고    scopus 로고
    • Role of V-ATPase-rich cells in acidification of the male reproductive tract
    • Brown D, Smith P, Breton S. Role of V-ATPase-rich cells in acidification of the male reproductive tract. J Exp Biol 200: 257-262, 1997.
    • (1997) J Exp Biol , vol.200 , pp. 257-262
    • Brown, D.1    Smith, P.2    Breton, S.3
  • 34
    • 0026078796 scopus 로고
    • Cadmium-induced changes in luminal fluid pH in testis and epididymis of the rat in vivo
    • Caflisch CR, DuBose TDJ. Cadmium-induced changes in luminal fluid pH in testis and epididymis of the rat in vivo. J Toxicol Environ Health 32: 49-57, 1991.
    • (1991) J Toxicol Environ Health , vol.32 , pp. 49-57
    • Caflisch, C.R.1    DuBose, T.D.J.2
  • 35
    • 85133357355 scopus 로고    scopus 로고
    • +-ATPase. J Biol Chem 275: 37232-37239, 2000.
    • +-ATPase. J Biol Chem 275: 37232-37239, 2000.
  • 39
    • 85133390927 scopus 로고    scopus 로고
    • +-ATPase. J Biol Chem 277: 8979-8988, 2002.
    • +-ATPase. J Biol Chem 277: 8979-8988, 2002.
  • 40
    • 0028914182 scopus 로고
    • A regulatory role for ARF6 in receptor-mediated endocytosis
    • D'Souza-Schorey C, Li G, Colombo MI, Stahl PD. A regulatory role for ARF6 in receptor-mediated endocytosis. Science 267: 1175-1178, 1995.
    • (1995) Science , vol.267 , pp. 1175-1178
    • D'Souza-Schorey, C.1    Li, G.2    Colombo, M.I.3    Stahl, P.D.4
  • 41
    • 29144533534 scopus 로고    scopus 로고
    • The SNARE proteins SNAP-23 and Syntaxin 3 are expressed in epithelial cells of the epididymis (Abstract)
    • Da Silva N, Beaulieu V, Knepper M, Breton S. The SNARE proteins SNAP-23 and Syntaxin 3 are expressed in epithelial cells of the epididymis (Abstract). J Am Soc Nephrol 13: 486A, 2002.
    • (2002) J Am Soc Nephrol , vol.13
    • Da Silva, N.1    Beaulieu, V.2    Knepper, M.3    Breton, S.4
  • 42
    • 0142211351 scopus 로고    scopus 로고
    • Multiple roles for Arf6: Sorting, structuring, and signaling at the plasma membrane
    • Donaldson JG. Multiple roles for Arf6: sorting, structuring, and signaling at the plasma membrane. J Biol Chem 278: 41573-41576, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 41573-41576
    • Donaldson, J.G.1
  • 44
    • 0025002977 scopus 로고
    • Reclamation of filtered bicarbonate
    • DuBose TD Jr. Reclamation of filtered bicarbonate. Kidney Int 38: 584-589, 1990.
    • (1990) Kidney Int , vol.38 , pp. 584-589
    • DuBose Jr., T.D.1
  • 47
    • 0029664522 scopus 로고    scopus 로고
    • The V0 sector of the V-ATPase, synaptobrevin, and synaptophysin are associated on synaptic vesicles in a Triton X-100-resistant, freeze-thawing sensitive, complex
    • Galli T, McPherson PS, De Camilli P. The V0 sector of the V-ATPase, synaptobrevin, and synaptophysin are associated on synaptic vesicles in a Triton X-100-resistant, freeze-thawing sensitive, complex. J Biol Chem 271: 2193-2198, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 2193-2198
    • Galli, T.1    McPherson, P.S.2    De Camilli, P.3
  • 48
    • 0037047282 scopus 로고    scopus 로고
    • Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery
    • Geyer M, Yu H, Mandic R, Linnemann T, Zheng YH, Fackler OT, Peterlin BM. Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery. J Biol Chem 277: 28521-28529, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 28521-28529
    • Geyer, M.1    Yu, H.2    Mandic, R.3    Linnemann, T.4    Zheng, Y.H.5    Fackler, O.T.6    Peterlin, B.M.7
  • 49
    • 2942684947 scopus 로고
    • Properties of kidney plasma membrane vacuolar H+-ATPase: Proton pumps responsible for bicarbonate transport, urinary acidification, and acid-base homeostasis
    • Gluck SL, Nelson R, Lee B, Holliday L, Iyori M. Properties of kidney plasma membrane vacuolar H+-ATPase: proton pumps responsible for bicarbonate transport, urinary acidification, and acid-base homeostasis. Organellar Proton ATPases, 1995.
    • (1995) Organellar Proton ATPases
    • Gluck, S.L.1    Nelson, R.2    Lee, B.3    Holliday, L.4    Iyori, M.5
  • 54
    • 0028914096 scopus 로고
    • Epididymal epithelium: Its contribution to the formation of luminal fluid microenvironment
    • Hinton B, Palladino M. Epididymal epithelium: its contribution to the formation of luminal fluid microenvironment. Microsc Res Tech 30: 67-81, 1995.
    • (1995) Microsc Res Tech , vol.30 , pp. 67-81
    • Hinton, B.1    Palladino, M.2
  • 56
    • 3042542722 scopus 로고    scopus 로고
    • The subapical compartment: A traffic center in membrane polarity development
    • Hoekstra D, Tyteca D, van ISC. The subapical compartment: a traffic center in membrane polarity development. J Cell Sci 117: 2183-2192, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 2183-2192
    • Hoekstra, D.1    Tyteca, D.2    van, I.S.C.3
  • 59
    • 0036259317 scopus 로고    scopus 로고
    • Molecular basis of proximal renal tubular acidosis
    • Igarashi T, Sekine T, Watanabe H. Molecular basis of proximal renal tubular acidosis. J Nephrol 15, Suppl 5: S135-S141, 2002.
    • (2002) J Nephrol , vol.15 , Issue.SUPPL. 5
    • Igarashi, T.1    Sekine, T.2    Watanabe, H.3
  • 61
    • 0023157142 scopus 로고
    • Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate
    • Janmey PA, Stossel TP. Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. Nature 325: 362-364, 1987.
    • (1987) Nature , vol.325 , pp. 362-364
    • Janmey, P.A.1    Stossel, T.P.2
  • 62
    • 18444379365 scopus 로고    scopus 로고
    • Semen quality and reproductive endocrine function with regard to blood cadmium in Croatian male subjects
    • Jurasovic J, Cvitkovic P, Pizent A, Colak B, Telisman S. Semen quality and reproductive endocrine function with regard to blood cadmium in Croatian male subjects. Biometals 17: 735-743, 2004.
    • (2004) Biometals , vol.17 , pp. 735-743
    • Jurasovic, J.1    Cvitkovic, P.2    Pizent, A.3    Colak, B.4    Telisman, S.5
  • 65
    • 0038730346 scopus 로고    scopus 로고
    • Proton translocation driven by ATP hydrolysis in V-ATPases
    • Kawasaki-Nishi S, Nishi T, Forgac M. Proton translocation driven by ATP hydrolysis in V-ATPases. FEBS Lett 545: 76-85, 2003.
    • (2003) FEBS Lett , vol.545 , pp. 76-85
    • Kawasaki-Nishi, S.1    Nishi, T.2    Forgac, M.3
  • 66
    • 0035947711 scopus 로고    scopus 로고
    • Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation
    • Kawasaki-Nishi S, Nishi T, Forgac M. Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation. J Biol Chem 276: 17941-17948, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 17941-17948
    • Kawasaki-Nishi, S.1    Nishi, T.2    Forgac, M.3
  • 67
    • 1542287665 scopus 로고    scopus 로고
    • Occupational exposure associated with reproductive dysfunction
    • Kumar S. Occupational exposure associated with reproductive dysfunction. J Occup Health 46: 1-19, 2004.
    • (2004) J Occup Health , vol.46 , pp. 1-19
    • Kumar, S.1
  • 68
    • 0022899222 scopus 로고
    • Age-related dose response of selected reproductive parameters to acute cadmium chloride exposure in the male Long-Evans rat
    • Laskey JW, Rehnberg GL, Laws SC, Hein JF. Age-related dose response of selected reproductive parameters to acute cadmium chloride exposure in the male Long-Evans rat. J Toxicol Environ Health 19: 393-401, 1986.
    • (1986) J Toxicol Environ Health , vol.19 , pp. 393-401
    • Laskey, J.W.1    Rehnberg, G.L.2    Laws, S.C.3    Hein, J.F.4
  • 71
    • 0035839499 scopus 로고    scopus 로고
    • +-ATPase: Evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump
    • +-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump. J Biol Chem 276: 30407-30413, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 30407-30413
    • Lu, M.1    Holliday, L.S.2    Zhang, L.3    Dunn Jr, W.A.4    Gluck, S.L.5
  • 73
    • 0032447082 scopus 로고    scopus 로고
    • The actin-binding proteins adseverin and gelsolin are both highly expressed but differentially localized in kidney and intestine
    • Lueck A, Brown D, Kwiatkowski DJ. The actin-binding proteins adseverin and gelsolin are both highly expressed but differentially localized in kidney and intestine. J Cell Sci 111: 3633-3643, 1998.
    • (1998) J Cell Sci , vol.111 , pp. 3633-3643
    • Lueck, A.1    Brown, D.2    Kwiatkowski, D.J.3
  • 74
    • 0034091885 scopus 로고    scopus 로고
    • Mechanisms of nephrotoxicity from metal combinations: A review
    • Madden EF, Fowler BA. Mechanisms of nephrotoxicity from metal combinations: a review. Drug Chem Toxicol 23: 1-12, 2000.
    • (2000) Drug Chem Toxicol , vol.23 , pp. 1-12
    • Madden, E.F.1    Fowler, B.A.2
  • 75
    • 0025827262 scopus 로고
    • Morphological adaptation of the collecting duct to acid-base disturbances
    • Madsen KM, Verlander JW, Kim J, Tisher CC. Morphological adaptation of the collecting duct to acid-base disturbances. Kidney Int Suppl 33: S57-S63, 1991.
    • (1991) Kidney Int Suppl , vol.33
    • Madsen, K.M.1    Verlander, J.W.2    Kim, J.3    Tisher, C.C.4
  • 76
    • 0017370683 scopus 로고
    • Use of pharmacological inhibitors in physiological studies of carbonic anhydrase
    • Mahren T. Use of pharmacological inhibitors in physiological studies of carbonic anhydrase. Am J Physiol Renal Fluid Electrolyte Physiol 232: F291-F297, 1977.
    • (1977) Am J Physiol Renal Fluid Electrolyte Physiol , vol.232
    • Mahren, T.1
  • 79
    • 0027255716 scopus 로고
    • +-ATPase associates with and is phosphorylated by the 50-kDa polypeptide of the clathrin assembly protein AP-2
    • +-ATPase associates with and is phosphorylated by the 50-kDa polypeptide of the clathrin assembly protein AP-2. J Biol Chem 268: 9184-9186, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 9184-9186
    • Myers, M.1    Forgac, M.2
  • 82
    • 0032946360 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane proton-adenotriphosphatases
    • Nelson N, Harvey W. Vacuolar and plasma membrane proton-adenotriphosphatases. Physiol Rev 79: 361-385, 1999.
    • (1999) Physiol Rev , vol.79 , pp. 361-385
    • Nelson, N.1    Harvey, W.2
  • 85
    • 0036481562 scopus 로고    scopus 로고
    • +-ATPases - nature's most versatile proton pumps
    • +-ATPases - nature's most versatile proton pumps. Nat Rev Mol Cell Biol 3: 94-103, 2002.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 94-103
    • Nishi, T.1    Forgac, M.2
  • 86
    • 0344443771 scopus 로고    scopus 로고
    • Expression and function of the mouse V-ATPase d subunit isoforms
    • Nishi T, Kawasaki-Nishi S, Forgac M. Expression and function of the mouse V-ATPase d subunit isoforms. J Biol Chem 278: 46396-46402, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 46396-46402
    • Nishi, T.1    Kawasaki-Nishi, S.2    Forgac, M.3
  • 87
    • 33747371955 scopus 로고    scopus 로고
    • The E and G subunits of the yeast V-ATPase interact tightly and are both present at more than one copy per V1 complex
    • Ohira M, Smardon AM, Charsky CM, Liu J, Tarsio M, Kane PM. The E and G subunits of the yeast V-ATPase interact tightly and are both present at more than one copy per V1 complex. J Biol Chem 281: 22752-22760, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 22752-22760
    • Ohira, M.1    Smardon, A.M.2    Charsky, C.M.3    Liu, J.4    Tarsio, M.5    Kane, P.M.6
  • 89
    • 0027722042 scopus 로고
    • Concentrations of lead, cadmium and zinc in the tissues of reproductive organs of men
    • Oldereid NB, Thomassen Y, Attramadal A, Olaisen B, Purvis K. Concentrations of lead, cadmium and zinc in the tissues of reproductive organs of men. J Reprod Fertil 99: 421-425., 1993.
    • (1993) J Reprod Fertil , vol.99 , pp. 421-425
    • Oldereid, N.B.1    Thomassen, Y.2    Attramadal, A.3    Olaisen, B.4    Purvis, K.5
  • 92
    • 0000534328 scopus 로고
    • Sterilization of the male by cadmium salts
    • Parizek J. Sterilization of the male by cadmium salts. J Reprod Fertil 1: 194-209, 1960.
    • (1960) J Reprod Fertil , vol.1 , pp. 194-209
    • Parizek, J.1
  • 93
    • 0031597366 scopus 로고    scopus 로고
    • +-ATPase is an unconventional glucose-induced effect
    • +-ATPase is an unconventional glucose-induced effect. Mol Cell Biol 18: 7064-7074, 1998.
    • (1998) Mol Cell Biol , vol.18 , pp. 7064-7074
    • Parra, K.J.1    Kane, P.M.2
  • 94
    • 0034647941 scopus 로고    scopus 로고
    • The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes
    • Parra KJ, Keenan KL, Kane PM. The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes. J Biol Chem 275: 21761-21767, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 21761-21767
    • Parra, K.J.1    Keenan, K.L.2    Kane, P.M.3
  • 96
    • 29144451321 scopus 로고    scopus 로고
    • Role of acid/base transporters in the male reproductive tract and potential consequences of their malfunction
    • Pastor-Soler N, Pietrement C, Breton S. Role of acid/base transporters in the male reproductive tract and potential consequences of their malfunction. Physiology (Bethesda) 20: 417-428, 2005.
    • (2005) Physiology (Bethesda) , vol.20 , pp. 417-428
    • Pastor-Soler, N.1    Pietrement, C.2    Breton, S.3
  • 98
    • 0028238357 scopus 로고
    • Alternative mRNA splicing generates tissue-specific isoforms of 116-kDa polypeptide of vacuolar proton pump
    • Peng SB, Crider BP, Xie X, Stone DK. Alternative mRNA splicing generates tissue-specific isoforms of 116-kDa polypeptide of vacuolar proton pump. J Biol Chem 269: 17262-17266, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 17262-17266
    • Peng, S.B.1    Crider, B.P.2    Xie, X.3    Stone, D.K.4
  • 99
    • 0033593434 scopus 로고    scopus 로고
    • Identification and reconstitution of an isoform of the 116-kDa subunit of the vacuolar proton translocating ATPase
    • Peng SB, Li X, Crider BP, Zhou Z, Andersen P, Tsai SJ, Xie XS, Stone DK. Identification and reconstitution of an isoform of the 116-kDa subunit of the vacuolar proton translocating ATPase. J Biol Chem 274: 2549-2555, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 2549-2555
    • Peng, S.B.1    Li, X.2    Crider, B.P.3    Zhou, Z.4    Andersen, P.5    Tsai, S.J.6    Xie, X.S.7    Stone, D.K.8
  • 100
    • 0035252348 scopus 로고    scopus 로고
    • Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion
    • Peters C, Bayer MJ, Buhler S, Andersen JS, Mann M, Mayer A. Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion. Nature 409: 581-588, 2001.
    • (2001) Nature , vol.409 , pp. 581-588
    • Peters, C.1    Bayer, M.J.2    Buhler, S.3    Andersen, J.S.4    Mann, M.5    Mayer, A.6
  • 107
    • 11844260070 scopus 로고    scopus 로고
    • +-ATPase assembly, translocation, and acidification of intracellular compartments in renal epithelial cells
    • +-ATPase assembly, translocation, and acidification of intracellular compartments in renal epithelial cells. Mol Cell Biol 25: 575-589, 2005.
    • (2005) Mol Cell Biol , vol.25 , pp. 575-589
    • Sautin, Y.Y.1    Lu, M.2    Gaugler, A.3    Zhang, L.4    Gluck, S.L.5
  • 108
    • 0021825353 scopus 로고
    • + pumps in isolated perfused proximal and collecting tubules
    • + pumps in isolated perfused proximal and collecting tubules. J Clin Invest 75: 1638-1644, 1985.
    • (1985) J Clin Invest , vol.75 , pp. 1638-1644
    • Schwartz, G.J.1    Al-Awqati, Q.2
  • 109
    • 20844452859 scopus 로고    scopus 로고
    • Role of hensin in mediating the adaptation of the cortical collecting duct to metabolic acidosis
    • Schwartz GJ, Al-Awqati Q. Role of hensin in mediating the adaptation of the cortical collecting duct to metabolic acidosis. Curr Opin Nephrol Hypertens 14: 383-388, 2005.
    • (2005) Curr Opin Nephrol Hypertens , vol.14 , pp. 383-388
    • Schwartz, G.J.1    Al-Awqati, Q.2
  • 110
    • 0022412843 scopus 로고
    • Plasticity of functional epithelial polarity
    • Schwartz GJ, Barasch J, Al-Awqati Q. Plasticity of functional epithelial polarity. Nature 318: 368-371, 1985.
    • (1985) Nature , vol.318 , pp. 368-371
    • Schwartz, G.J.1    Barasch, J.2    Al-Awqati, Q.3
  • 111
    • 10344240424 scopus 로고    scopus 로고
    • Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivo dissociation
    • Shao E, Forgac M. Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivo dissociation. J Biol Chem 279: 48663-48670, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 48663-48670
    • Shao, E.1    Forgac, M.2
  • 112
    • 0037019817 scopus 로고    scopus 로고
    • +-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis
    • +-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis. Gene 297: 169-177, 2002.
    • (2002) Gene , vol.297 , pp. 169-177
    • Smith, A.1    Borthwick, K.J.2    Karet, F.E.3
  • 119
    • 0035930581 scopus 로고    scopus 로고
    • A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers
    • Sterling D, Reithmeier RA, Casey JR. A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers. J Biol Chem 276: 47886-47894, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 47886-47894
    • Sterling, D.1    Reithmeier, R.A.2    Casey, J.R.3
  • 120
    • 18744379726 scopus 로고    scopus 로고
    • Stover E, Borthwick K, Bavalia C, Eady N, Fritz D, Rungroj N, Giersch A, Morton C, Axon P, Akil I, Al-Sabban E, Baguley D, Bianca S, Bakkaloglu A, Bircan Z, Chauveau D, Clermont M, Guala A, Hulton S, Kroes H, Li Volti G, Mir S, Mocan H, Nayir A, Ozen S, Rodriguez Soriano J, Sanjad S, VT, Taylor C, Topaloglu R, Smith A, Karet F. Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal renal tubular acidosis with new evidence for hearing loss. J Med Genet 39: 796-803, 2002.
    • Stover E, Borthwick K, Bavalia C, Eady N, Fritz D, Rungroj N, Giersch A, Morton C, Axon P, Akil I, Al-Sabban E, Baguley D, Bianca S, Bakkaloglu A, Bircan Z, Chauveau D, Clermont M, Guala A, Hulton S, Kroes H, Li Volti G, Mir S, Mocan H, Nayir A, Ozen S, Rodriguez Soriano J, Sanjad S, VT, Taylor C, Topaloglu R, Smith A, Karet F. Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal renal tubular acidosis with new evidence for hearing loss. J Med Genet 39: 796-803, 2002.
  • 121
  • 122
    • 0242414411 scopus 로고    scopus 로고
    • Mouse proton pump ATPase C subunit isoforms (C2-a and C2-b) specifically expressed in kidney and lung
    • Sun-wada GH, Murata Y, Namba M, Yamamoto A, Wada Y, Futai M. Mouse proton pump ATPase C subunit isoforms (C2-a and C2-b) specifically expressed in kidney and lung. J Biol Chem 278: 44843-44851, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 44843-44851
    • Sun-wada, G.H.1    Murata, Y.2    Namba, M.3    Yamamoto, A.4    Wada, Y.5    Futai, M.6
  • 123
    • 0037413670 scopus 로고    scopus 로고
    • Diversity of mouse proton-translocating ATPase: Presence of multiple isoforms of the C, d and G subunits
    • Sun-wada GH, Yoshimizu T, Imai-Senga Y, Wada Y, Futai M. Diversity of mouse proton-translocating ATPase: presence of multiple isoforms of the C, d and G subunits. Gene 302: 147-153, 2003.
    • (2003) Gene , vol.302 , pp. 147-153
    • Sun-wada, G.H.1    Yoshimizu, T.2    Imai-Senga, Y.3    Wada, Y.4    Futai, M.5
  • 124
    • 0037124047 scopus 로고    scopus 로고
    • A proton pump ATPase with testis-specific E1-subunit isoform required for acrosome acidification
    • Sun-Wada GH, Imai-Senga Y, Yamamoto A, Murata Y, Hirata T, Wada Y, Futai M. A proton pump ATPase with testis-specific E1-subunit isoform required for acrosome acidification. J Biol Chem 277: 18098-18105, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 18098-18105
    • Sun-Wada, G.H.1    Imai-Senga, Y.2    Yamamoto, A.3    Murata, Y.4    Hirata, T.5    Wada, Y.6    Futai, M.7
  • 125
    • 3542998744 scopus 로고    scopus 로고
    • Diverse and essential roles of mammalian vacuolar-type proton pump ATPase: Toward the physiological understanding of inside acidic compartments
    • Sun-Wada GH, Wada Y, Futai M. Diverse and essential roles of mammalian vacuolar-type proton pump ATPase: toward the physiological understanding of inside acidic compartments. Biochim Biophys Acta 1658: 106-114, 2004.
    • (2004) Biochim Biophys Acta , vol.1658 , pp. 106-114
    • Sun-Wada, G.H.1    Wada, Y.2    Futai, M.3
  • 126
    • 0346014856 scopus 로고    scopus 로고
    • Nephrotoxicity and the proximal tubule. Insights from cadmium
    • 93: p87-p93
    • Thevenod F. Nephrotoxicity and the proximal tubule. Insights from cadmium. Nephron Physiol 93: p87-p93, 2003.
    • (2003) Nephron Physiol
    • Thevenod, F.1
  • 136
    • 85133308537 scopus 로고    scopus 로고
    • +-ATPase plays a role in coupling of proton transport and ATP hydrolysis. J Biol Chem 275: 22075-22081, 2000.
    • +-ATPase plays a role in coupling of proton transport and ATP hydrolysis. J Biol Chem 275: 22075-22081, 2000.
  • 138
    • 33745852662 scopus 로고    scopus 로고
    • +-ATPase B1 subunit mutations that cause inherited distal renal tubular acidosis affect proton pump assembly and trafficking in inner medullary collecting duct cells
    • +-ATPase B1 subunit mutations that cause inherited distal renal tubular acidosis affect proton pump assembly and trafficking in inner medullary collecting duct cells. J Am Soc Nephrol 17: 1858-1866, 2006.
    • (2006) J Am Soc Nephrol , vol.17 , pp. 1858-1866
    • Yang, Q.1    Li, G.2    Singh, S.K.3    Alexander, E.A.4    Schwartz, J.H.5
  • 139
    • 0018667209 scopus 로고
    • Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein
    • Yin HL, Stossel TP. Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein. Nature 281: 583-586, 1979.
    • (1979) Nature , vol.281 , pp. 583-586
    • Yin, H.L.1    Stossel, T.P.2
  • 140
    • 13444288261 scopus 로고    scopus 로고
    • Environmental and occupational factors affecting fertility and IVF success
    • Younglai EV, Holloway AC, Foster WG. Environmental and occupational factors affecting fertility and IVF success. Hum Reprod Update 11: 43-57, 2005.
    • (2005) Hum Reprod Update , vol.11 , pp. 43-57
    • Younglai, E.V.1    Holloway, A.C.2    Foster, W.G.3


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