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Volumn , Issue , 2012, Pages 53-72

Roles and regulatory mechanism of proton pumping V-ATPase in spermatozoa and epididymis physiology

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EID: 84864645945     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (2)

References (114)
  • 1
    • 14844318508 scopus 로고    scopus 로고
    • Modulation of the actin cytoskeleton via gelsolin regulates vacuolar H+ATPase (V-ATPase) recycling
    • Beaulieu, V., Da Silva, N., Pastor-Soler, N., Brown, C. R., Smith, P. J., Brown, D. & Breton, S. (2005). Modulation of the actin cytoskeleton via gelsolin regulates vacuolar H+ATPase (V-ATPase) recycling. J Biol Chem, 280, 8452-8463.
    • (2005) J Biol Chem , vol.280 , pp. 8452-8463
    • Beaulieu, V.1    Da Silva, N.2    Pastor-Soler, N.3    Brown, C.R.4    Smith, P.J.5    Brown, D.6    Breton, S.7
  • 2
    • 77950222578 scopus 로고    scopus 로고
    • Role of purinergic signaling pathways in V-ATPase recruitment to apical membrane of acidifying epididymal clear cells
    • Belleannee, C., Da Silva, N., Shum W. W., Brown, D. & Breton, S. (2010). Role of purinergic signaling pathways in V-ATPase recruitment to apical membrane of acidifying epididymal clear cells. Am J Physiol Cell Physiol, 298, C817-830.
    • (2010) Am J Physiol Cell Physiol , vol.298
    • Belleannee, C.1    Da Silva, N.2    Shum, W.W.3    Brown, D.4    Breton, S.5
  • 3
    • 33644935227 scopus 로고    scopus 로고
    • The V-type H+ ATPase: molecular structure and function, physiological roles and regulation
    • Beyenbach, K. W. & Wieczorek, H. (2006). The V-type H+ ATPase: molecular structure and function, physiological roles and regulation. J Exp Biol, 209, 577-589.
    • (2006) J Exp Biol , vol.209 , pp. 577-589
    • Beyenbach, K.W.1    Wieczorek, H.2
  • 4
    • 33748352765 scopus 로고    scopus 로고
    • Epididymal expression of the forkhead transcription factor Foxi1 is required for male fertility
    • Blomqvist, S. R., Vidarsson, H., Soder, O. & Enerbäck, S. (2006). Epididymal expression of the forkhead transcription factor Foxi1 is required for male fertility. EMBO J, 25, 4131-4141.
    • (2006) EMBO J , vol.25 , pp. 4131-4141
    • Blomqvist, S.R.1    Vidarsson, H.2    Soder, O.3    Enerbäck, S.4
  • 5
    • 0031722644 scopus 로고    scopus 로고
    • Proton secretion in the male reproductive tract: involvement of Cl-- independent HCO3- transport
    • Breton, S., Hammar, K., Smith, P. J. & Brown, D. (1998). Proton secretion in the male reproductive tract: involvement of Cl-- independent HCO3- transport. Am J Physiol, 275, C1134-1142.
    • (1998) Am J Physiol , vol.275
    • Breton, S.1    Hammar, K.2    Smith, P.J.3    Brown, D.4
  • 6
    • 0034033704 scopus 로고    scopus 로고
    • Tetanus toxin-mediated cleavage of cellubrevin inhibits proton secretion in the male reproductive tract
    • Breton, S., Nsumu, N. N., Galli, T., Sabolic, I., Smith, P. J. & Brown, D. (2000). Tetanus toxin-mediated cleavage of cellubrevin inhibits proton secretion in the male reproductive tract. Am J Physiol Renal Physiol, 278, F717-725.
    • (2000) Am J Physiol Renal Physiol , vol.278
    • Breton, S.1    Nsumu, N.N.2    Galli, T.3    Sabolic, I.4    Smith, P.J.5    Brown, D.6
  • 7
    • 0029898733 scopus 로고    scopus 로고
    • Acidification of the male reproductive tract by a proton pumping H+- ATPase
    • Breton, S., Smith, P. J., Lui, B. & Brown, D. (1996). Acidification of the male reproductive tract by a proton pumping H+- ATPase. Nat Med, 2, 470-472.
    • (1996) Nat Med , vol.2 , pp. 470-472
    • Breton, S.1    Smith, P.J.2    Lui, B.3    Brown, D.4
  • 8
    • 0034674677 scopus 로고    scopus 로고
    • The B1 subunit of the H+ATPase is a PDZ domain-binding protein Colocalization with NHE-RF in renal B-intercalated cells
    • Breton, S., Wiederhold, T., Marshansky, V., Nsumu, N. N., Ramesh, V. & Brown, D. (2000). The B1 subunit of the H+ATPase is a PDZ domain-binding protein. Colocalization with NHE-RF in renal B-intercalated cells. J Biol Chem, 275, 18219-18224.
    • (2000) J Biol Chem , vol.275 , pp. 18219-18224
    • Breton, S.1    Wiederhold, T.2    Marshansky, V.3    Nsumu, N.N.4    Ramesh, V.5    Brown, D.6
  • 9
    • 0024240241 scopus 로고
    • Localization of a proton-pumping ATPase in rat kidney
    • Brown, D., Hirsch, S. & Gluck, S. (1988). Localization of a proton-pumping ATPase in rat kidney. J Clin Invest, 82, 2114-2126.
    • (1988) J Clin Invest , vol.82 , pp. 2114-2126
    • Brown, D.1    Hirsch, S.2    Gluck, S.3
  • 10
    • 0026795802 scopus 로고
    • A plasma membrane proton ATPase in specialized cells of rat epididymis
    • Brown, D., Lui, B., Gluck, S. & Sabolic, I. (1992). A plasma membrane proton ATPase in specialized cells of rat epididymis. Am J Physiol, 263, C913-916.
    • (1992) Am J Physiol , vol.263
    • Brown, D.1    Lui, B.2    Gluck, S.3    Sabolic, I.4
  • 11
    • 66449088593 scopus 로고    scopus 로고
    • Regulation of the V-ATPase in kidney epithelial cells: dual role in acid-base homeostasis and vesicle trafficking
    • Brown, D., Paunescu, T. G., Breton, S. & Marshansky, V. (2009). Regulation of the V-ATPase in kidney epithelial cells: dual role in acid-base homeostasis and vesicle trafficking. J Exp Biol, 212, 1762-1772.
    • (2009) J Exp Biol , vol.212 , pp. 1762-1772
    • Brown, D.1    Paunescu, T.G.2    Breton, S.3    Marshansky, V.4
  • 12
    • 0026721818 scopus 로고
    • Acidification of testicular and epididymal fluids in the rat after surgically-induced varicocele
    • Caflisch, C. R. (1992). Acidification of testicular and epididymal fluids in the rat after surgically-induced varicocele. Int J Androl, 15, 238-245.
    • (1992) Int J Androl , vol.15 , pp. 238-245
    • Caflisch, C.R.1
  • 13
    • 0026078796 scopus 로고
    • Cadmium-induced changes in luminal fluid pH in testis and epididymis of the rat in vivo
    • Caflisch, C. R. & DuBose T. D. Jr. (1991). Cadmium-induced changes in luminal fluid pH in testis and epididymis of the rat in vivo. J Toxicol Environ Health, 32, 49-57.
    • (1991) J Toxicol Environ Health , vol.32 , pp. 49-57
    • Caflisch, C.R.1    DuBose Jr., T.D.2
  • 14
    • 0037369764 scopus 로고    scopus 로고
    • Adenosine stimulates anion secretion across cultured and native adult human vas deferens epithelia
    • Carlin, R. W., Lee, J. H., Marcus, D. C. & Schultz, B. D. (2003). Adenosine stimulates anion secretion across cultured and native adult human vas deferens epithelia. Biol Reprod, 68, 1027-1034.
    • (2003) Biol Reprod , vol.68 , pp. 1027-1034
    • Carlin, R.W.1    Lee, J.H.2    Marcus, D.C.3    Schultz, B.D.4
  • 15
    • 10744233422 scopus 로고    scopus 로고
    • Vacuolar H+-ATPase binding to microfilaments: regulation in response to phosphatidylinositol 3-kinase activity and detailed characterization of the actin-binding site in subunit B
    • Chen, S. H., Bubb, M. R., Yarmola, E. G., Zuo, J., Jiang, J., Lee, B. S., Lu, M., Gluck, S. L., Hurst, I. R. & Holliday, L. S. (2004). Vacuolar H+-ATPase binding to microfilaments: regulation in response to phosphatidylinositol 3-kinase activity and detailed characterization of the actin-binding site in subunit B. J Biol Chem, 279, 7988-7998.
    • (2004) J Biol Chem , vol.279 , pp. 7988-7998
    • Chen, S.H.1    Bubb, M.R.2    Yarmola, E.G.3    Zuo, J.4    Jiang, J.5    Lee, B.S.6    Lu, M.7    Gluck, S.L.8    Hurst, I.R.9    Holliday, L.S.10
  • 16
    • 18544364336 scopus 로고    scopus 로고
    • Cell-cell interaction underlies formation of fluid in the male reproductive tract of the rat
    • Cheung, K. H., Leung, G. P., Leung, M. C., Shum, W. W., Zhou, W. L. & Wong, P. Y. (2005). Cell-cell interaction underlies formation of fluid in the male reproductive tract of the rat. J Gen Physiol, 125, 443-454.
    • (2005) J Gen Physiol , vol.125 , pp. 443-454
    • Cheung, K.H.1    Leung, G.P.2    Leung, M.C.3    Shum, W.W.4    Zhou, W.L.5    Wong, P.Y.6
  • 17
    • 60149095270 scopus 로고    scopus 로고
    • New insights into epididymal biology and function
    • Cornwall, G. A. (2009). New insights into epididymal biology and function. Hum Reprod Update, 15, 213-227.
    • (2009) Hum Reprod Update , vol.15 , pp. 213-227
    • Cornwall, G.A.1
  • 19
    • 34447275923 scopus 로고    scopus 로고
    • Regulation of vacuolar proton pumping ATPase-dependent luminal acidification in the epididymis
    • Da Silva, N., Shum, W. W. & Breton, S. (2007). Regulation of vacuolar proton pumping ATPase-dependent luminal acidification in the epididymis. Asian J Androl, 9, 476-482.
    • (2007) Asian J Androl , vol.9 , pp. 476-482
    • Da Silva, N.1    Shum, W.W.2    Breton, S.3
  • 20
    • 34447272956 scopus 로고    scopus 로고
    • Relocalization of the V-ATPase B2 subunit to the apical membrane of epididymal clear cells of mice deficient in the B1 subunit
    • Da Silva, N., Shum, W. W., El-Annan, J., Paunescu, T. G., McKee, M., Smith, P. J., Brown, D. & Breton, S. (2007). Relocalization of the V-ATPase B2 subunit to the apical membrane of epididymal clear cells of mice deficient in the B1 subunit. Am J Physiol Cell Physiol, 293, C199-210.
    • (2007) Am J Physiol Cell Physiol , vol.293
    • Da Silva, N.1    Shum, W.W.2    El-Annan, J.3    Paunescu, T.G.4    McKee, M.5    Smith, P.J.6    Brown, D.7    Breton, S.8
  • 21
    • 77955405903 scopus 로고    scopus 로고
    • Cytosolic pH is a second messenger for glucose and regulates the PKA pathway through V-ATPase
    • Dechant, R., Binda, M., Lee, S. S., Pelet, S., Winderickx, J. & Peter, M. (2010). Cytosolic pH is a second messenger for glucose and regulates the PKA pathway through V-ATPase. EMBO J, 29, 2515-2526.
    • (2010) EMBO J , vol.29 , pp. 2515-2526
    • Dechant, R.1    Binda, M.2    Lee, S.S.3    Pelet, S.4    Winderickx, J.5    Peter, M.6
  • 22
    • 67649405059 scopus 로고    scopus 로고
    • Subunit interactions and requirements for inhibition of the yeast V1-ATPase
    • Diab, H., Ohira, M., Liu, M., Cobb, E. & Kane, P. M. (2009). Subunit interactions and requirements for inhibition of the yeast V1-ATPase. J Biol Chem, 284, 13316-13325.
    • (2009) J Biol Chem , vol.284 , pp. 13316-13325
    • Diab, H.1    Ohira, M.2    Liu, M.3    Cobb, E.4    Kane, P.M.5
  • 23
    • 0029925360 scopus 로고    scopus 로고
    • Mice lacking angiotensin-converting enzyme have low blood pressure, renal pathology, and reduced male fertility
    • Esther, C. R., Jr., Howard, T. E., Marino, E. M., Goddard, J. M., Capecchi, M. R. & Bernstein, K. E. (1996). Mice lacking angiotensin-converting enzyme have low blood pressure, renal pathology, and reduced male fertility. Lab Invest, 74, 953-965.
    • (1996) Lab Invest , vol.74 , pp. 953-965
    • Esther Jr., C.R.1    Howard, T.E.2    Marino, E.M.3    Goddard, J.M.4    Capecchi, M.R.5    Bernstein, K.E.6
  • 24
    • 0033983475 scopus 로고    scopus 로고
    • Luminal acidification of diverse organelles by V-ATPase in animal cells
    • Futai, M., Oka, T., Sun-Wada, G.-H., Moriyama, Y., Kanazawa, H. & Wada, Y. (2000). Luminal acidification of diverse organelles by V-ATPase in animal cells. J Exp Biol, 203, 107-116.
    • (2000) J Exp Biol , vol.203 , pp. 107-116
    • Futai, M.1    Oka, T.2    Sun-Wada, G.-H.3    Moriyama, Y.4    Kanazawa, H.5    Wada, Y.6
  • 25
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
    • Forgac, M. (2007). Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat Rev Mol Cell Biol, 8, 917-929.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 917-929
    • Forgac, M.1
  • 26
    • 0032982423 scopus 로고    scopus 로고
    • A 105- to 94-kilodalton protein in the epididymal fluids of domestic mammals is angiotensin I- converting enzyme (ACE); evidence that sperm are the source of this ACE
    • Gatti, J. L., Druart, X., Guerin, Y., Dacheux, F., & Dacheux, J. L. (1999). A 105- to 94-kilodalton protein in the epididymal fluids of domestic mammals is angiotensin I- converting enzyme (ACE); evidence that sperm are the source of this ACE. Biol Reprod, 60, 937-945.
    • (1999) Biol Reprod , vol.60 , pp. 937-945
    • Gatti, J.L.1    Druart, X.2    Guerin, Y.3    Dacheux, F.4    Dacheux, J.L.5
  • 28
    • 34548213572 scopus 로고    scopus 로고
    • Oxytocin and vasopressin stimulate anion secretion by human and porcine vas deferens epithelia
    • Hagedorn, T. M., Carlin, R. W. & Schultz, B. D. (2007). Oxytocin and vasopressin stimulate anion secretion by human and porcine vas deferens epithelia. Biol Reprod, 77, 416-424.
    • (2007) Biol Reprod , vol.77 , pp. 416-424
    • Hagedorn, T.M.1    Carlin, R.W.2    Schultz, B.D.3
  • 29
    • 52949115271 scopus 로고    scopus 로고
    • Defective assembly of a hybrid vacuolar H+-ATPase containing the mouse testis-specific E1 isoform and yeast subunits
    • Hayashi, K., Sun-Wada, G.-H., Wada, Y., Nakanishi-Matsui, M. & Futai, M. (2008). Defective assembly of a hybrid vacuolar H+-ATPase containing the mouse testis-specific E1 isoform and yeast subunits. Biochim Biophys Acta, 1777, 1370-1377.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 1370-1377
    • Hayashi, K.1    Sun-Wada, G.-H.2    Wada, Y.3    Nakanishi-Matsui, M.4    Futai, M.5
  • 30
    • 0035001041 scopus 로고    scopus 로고
    • Distribution of the vacuolar H+ATPase along the rat and human male reproductive tract
    • Herak-Kramberger, C. M., Breton, S., Brown, D., Kraus, O. & Sabolic, I. (2001). Distribution of the vacuolar H+ATPase along the rat and human male reproductive tract. Biol Reprod, 64, 1699-1707.
    • (2001) Biol Reprod , vol.64 , pp. 1699-1707
    • Herak-Kramberger, C.M.1    Breton, S.2    Brown, D.3    Kraus, O.4    Sabolic, I.5
  • 34
    • 0038606551 scopus 로고    scopus 로고
    • Subunit rotation of vacuolar-type proton pumping ATPase: relative rotation of the G and c subunits
    • Hirata, T., Iwamoto-Kihara, A., Sun-Wada, G.-H., Okajima, T., Wada, Y. & Futai, M. (2003). Subunit rotation of vacuolar-type proton pumping ATPase: relative rotation of the G and c subunits. J Biol Chem, 278, 23714-23719.
    • (2003) J Biol Chem , vol.278 , pp. 23714-23719
    • Hirata, T.1    Iwamoto-Kihara, A.2    Sun-Wada, G.-H.3    Okajima, T.4    Wada, Y.5    Futai, M.6
  • 35
    • 0034644703 scopus 로고    scopus 로고
    • The amino-terminal domain of the B subunit of vacuolar H+-ATPase contains a filamentous actin binding site
    • Holliday, L. S., Lu, M., Lee, B. S., Nelson, R. D., Solivan, S., Zhang, L. & Gluck, S. L. (2000). The amino-terminal domain of the B subunit of vacuolar H+-ATPase contains a filamentous actin binding site. J Biol Chem, 275, 32331-32337.
    • (2000) J Biol Chem , vol.275 , pp. 32331-32337
    • Holliday, L.S.1    Lu, M.2    Lee, B.S.3    Nelson, R.D.4    Solivan, S.5    Zhang, L.6    Gluck, S.L.7
  • 36
    • 0036572831 scopus 로고    scopus 로고
    • A human gene, ATP6E1, encoding a testis-specific isoform of H+-ATPase subunit E
    • Imai-Senga, Y., Sun-Wada, G.-H., Wada, Y. & Futai, M. (2002). A human gene, ATP6E1, encoding a testis-specific isoform of H+-ATPase subunit E. Gene, 289, 7-12.
    • (2002) Gene , vol.289 , pp. 7-12
    • Imai-Senga, Y.1    Sun-Wada, G.-H.2    Wada, Y.3    Futai, M.4
  • 37
    • 0032726897 scopus 로고    scopus 로고
    • Targeted disruption of the gene encoding the preteolipid subunit of mouse vacuolar H+-ATPase leads to early embryonic lethality
    • Inoue, H., Noumi, T., Nagata, M., Murakami, H. & Kanazawa, H. (1999). Targeted disruption of the gene encoding the preteolipid subunit of mouse vacuolar H+-ATPase leads to early embryonic lethality. Biochim Biophys Acta, 1413, 130-138.
    • (1999) Biochim Biophys Acta , vol.1413 , pp. 130-138
    • Inoue, H.1    Noumi, T.2    Nagata, M.3    Murakami, H.4    Kanazawa, H.5
  • 38
    • 0029842595 scopus 로고    scopus 로고
    • Regulation of the motility and metabolism of spermatozoa for storage in the epididymis of eutherian and marsupial mammals
    • Jones, R. C. & Murdoch, R. N. (1996). Regulation of the motility and metabolism of spermatozoa for storage in the epididymis of eutherian and marsupial mammals. Reprod Fertil, Dev 8, 553-568.
    • (1996) Reprod Fertil, Dev , vol.8 , pp. 553-568
    • Jones, R.C.1    Murdoch, R.N.2
  • 39
    • 77954497964 scopus 로고    scopus 로고
    • A site-directed cross-linking approach to the characterization of subunit E-subunit G contacts in the vacuolar H+-ATPase stator
    • Jones, R. P, Durose, L. J., Phillips, C., Keen, J. N., Findlay, J. B. & Harrison, M. A. (2010). A site-directed cross-linking approach to the characterization of subunit E-subunit G contacts in the vacuolar H+-ATPase stator. Mol Membr Biol, 27, 147-159.
    • (2010) Mol Membr Biol , vol.27 , pp. 147-159
    • Jones R.P Durose, L.J.1    Phillips, C.2    Keen, J.N.3    Findlay, J.B.4    Harrison, M.A.5
  • 40
    • 14844349013 scopus 로고    scopus 로고
    • Defined sites of interaction between subunits E (Vma4p), C (Vma5p), and G (Vma10p) within the stator structure of the vacuolar H+-ATPase
    • Jones, R. P, Durose, L. J., Findlay, J. B. & Harrison, M. A. (2005). Defined sites of interaction between subunits E (Vma4p), C (Vma5p), and G (Vma10p) within the stator structure of the vacuolar H+-ATPase. Biochemistry, 44, 3933-3941.
    • (2005) Biochemistry , vol.44 , pp. 3933-3941
    • Jones R.P Durose, L.J.1    Findlay, J.B.2    Harrison, M.A.3
  • 42
    • 0029063512 scopus 로고
    • Disassembly and reassembly of the yeast vacuolar H+-ATPase in vivo
    • Kane, P. M. (1995). Disassembly and reassembly of the yeast vacuolar H+-ATPase in vivo. J Biol Chem, 270, 17025-17032.
    • (1995) J Biol Chem , vol.270 , pp. 17025-17032
    • Kane, P.M.1
  • 43
    • 33645119556 scopus 로고    scopus 로고
    • The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase
    • Kane, P. M. (2006). The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase. Microbiol Mol Biol Rev, 70, 177-191.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 177-191
    • Kane, P.M.1
  • 44
    • 0142089024 scopus 로고    scopus 로고
    • Assembly and regulation of the yeast vacuolar H+-ATPase
    • Kane, P. M. & Smardon, A. M. (2003). Assembly and regulation of the yeast vacuolar H+-ATPase. J Bioenerg Biomembr, 35, 313-321.
    • (2003) J Bioenerg Biomembr , vol.35 , pp. 313-321
    • Kane, P.M.1    Smardon, A.M.2
  • 47
    • 0030041317 scopus 로고    scopus 로고
    • Osteoclasts express the B2 isoform of vacuolar H+-ATPase intracellularly and on their plasma membranes
    • Lee, B. S., Holliday, L. S., Ojikutu, B., Krits, I. & Gluck, S. L. (1996). Osteoclasts express the B2 isoform of vacuolar H+-ATPase intracellularly and on their plasma membranes. Am J Physiol, 270, C382-388.
    • (1996) Am J Physiol , vol.270
    • Lee, B.S.1    Holliday, L.S.2    Ojikutu, B.3    Krits, I.4    Gluck, S.L.5
  • 49
    • 0026715099 scopus 로고
    • Characterization of adrenoceptors involved in the electrogenic chloride secretion by cultured rat epididymal epithelium
    • Leung, A. Y., Yip, W. K., & Wong, P. Y. (1992). Characterization of adrenoceptors involved in the electrogenic chloride secretion by cultured rat epididymal epithelium. Br J Pharmacol, 107, 146-151.
    • (1992) Br J Pharmacol , vol.107 , pp. 146-151
    • Leung, A.Y.1    Yip, W.K.2    Wong, P.Y.3
  • 50
    • 1942500852 scopus 로고    scopus 로고
    • Regulation of epididymal principal cell functions by basal cells: role of transient receptor potential (Trp) proteins and cyclooxygenase-1 (COX-1)
    • Leung, G. P., Cheung, K. H., Leung, C. T., Tsang, M. W. & Wong, P. Y. (2004). Regulation of epididymal principal cell functions by basal cells: role of transient receptor potential (Trp) proteins and cyclooxygenase-1 (COX-1). Mol Cell Endocrinol, 216, 5-13.
    • (2004) Mol Cell Endocrinol , vol.216 , pp. 5-13
    • Leung, G.P.1    Cheung, K.H.2    Leung, C.T.3    Tsang, M.W.4    Wong, P.Y.5
  • 51
    • 0033962314 scopus 로고    scopus 로고
    • Activation of cystic fibrosis transmembrane conductance regulator in rat epididymal epithelium by genistein
    • Leung, G. P. & Wong, P. Y. (2000). Activation of cystic fibrosis transmembrane conductance regulator in rat epididymal epithelium by genistein. Biol Reprod, 62, 143-149.
    • (2000) Biol Reprod , vol.62 , pp. 143-149
    • Leung, G.P.1    Wong, P.Y.2
  • 52
    • 0038006748 scopus 로고    scopus 로고
    • The renin-angiotensin system and male reproduction: new functions for old hormones
    • Leung, P. S. & Sernia, C. (2003). The renin-angiotensin system and male reproduction: new functions for old hormones. J Mol Endocrinol, 30, 263-270.
    • (2003) J Mol Endocrinol , vol.30 , pp. 263-270
    • Leung, P.S.1    Sernia, C.2
  • 53
    • 0015026414 scopus 로고
    • Micropuncture studies of the electrochemical aspects of fluid and electrolyte transport in individual seminiferous tubules, the epididymis and the vas deferens in rats
    • Levine, N. & Marsh, D. J. (1971). Micropuncture studies of the electrochemical aspects of fluid and electrolyte transport in individual seminiferous tubules, the epididymis and the vas deferens in rats. J Physiol, 213, 557-570.
    • (1971) J Physiol , vol.213 , pp. 557-570
    • Levine, N.1    Marsh, D.J.2
  • 54
    • 0032748995 scopus 로고    scopus 로고
    • Atp6i-deficient mice exhibit severe osteopetrosis due to loss of osteoclast-mediated extracellular acidification
    • Li, Y.-P., Chen, W., Liang, Y., Li, E. & Stashenko, P. (1999). Atp6i-deficient mice exhibit severe osteopetrosis due to loss of osteoclast-mediated extracellular acidification. Nat Genet, 23, 447-451.
    • (1999) Nat Genet , vol.23 , pp. 447-451
    • Li, Y.-P.1    Chen, W.2    Liang, Y.3    Li, E.4    Stashenko, P.5
  • 55
    • 34548300007 scopus 로고    scopus 로고
    • Physical interaction between aldolase and vacuolar H+-ATPase is essential for the assembly and activity of the proton pump
    • Lu, M., Ammar, D., Ives, H., Albrecht, F. & Gluck, S. L. (2007). Physical interaction between aldolase and vacuolar H+-ATPase is essential for the assembly and activity of the proton pump. J Biol Chem, 282, 24495-24503.
    • (2007) J Biol Chem , vol.282 , pp. 24495-24503
    • Lu, M.1    Ammar, D.2    Ives, H.3    Albrecht, F.4    Gluck, S.L.5
  • 56
    • 0035839499 scopus 로고    scopus 로고
    • Interaction between aldolase and vacuolar H+-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump
    • Lu, M., Holliday L. S., Zhang, L., Dunn, W. A. Jr. & Gluck, S. L. (2001). Interaction between aldolase and vacuolar H+-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump. J Biol Chem, 276, 30407-30413.
    • (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
  • 57
    • 0037064113 scopus 로고    scopus 로고
    • The amino-terminal domain of the E subunit of vacuolar H+-ATPase (V-ATPase) interacts with the H subunit and is required for V-ATPase function
    • Lu, M., Vergara, S., Zhang, L., Holliday L. S., Aris, J. & Gluck, S. L. (2002). The amino-terminal domain of the E subunit of vacuolar H+-ATPase (V-ATPase) interacts with the H subunit and is required for V-ATPase function. J Biol Chem, 277, 38409-38415.
    • (2002) J Biol Chem , vol.277 , pp. 38409-38415
    • Lu, M.1    Vergara, S.2    Zhang, L.3    Holliday, L.S.4    Aris, J.5    Gluck, S.L.6
  • 58
    • 0036893121 scopus 로고    scopus 로고
    • Germinal angiotensin I-converting enzyme is totally shed from the rodent sperm membrane during epididymal maturation
    • Metayer, S., Dacheux, F., Dacheux, J. L., & Gatti, J. L. (2002). Germinal angiotensin I-converting enzyme is totally shed from the rodent sperm membrane during epididymal maturation. Biol Reprod, 67, 1763-1767.
    • (2002) Biol Reprod , vol.67 , pp. 1763-1767
    • Metayer, S.1    Dacheux, F.2    Dacheux, J.L.3    Gatti, J.L.4
  • 59
    • 0026950284 scopus 로고
    • The role of V-ATPase in neuronal and endocrine systems
    • Moriyama, Y., Maeda, M. & Futai, M. (1992). The role of V-ATPase in neuronal and endocrine systems. J Exp Biol, 172, 171-178.
    • (1992) J Exp Biol , vol.172 , pp. 171-178
    • Moriyama, Y.1    Maeda, M.2    Futai, M.3
  • 60
    • 0037184028 scopus 로고    scopus 로고
    • Differential localization of the vacuolar H+ pump with G subunit isoforms (G1 and G2) in mouse neurons
    • Murata, Y., Sun-Wada, G.-H., Yoshimizu, T., Yamamoto, A., Wada, Y. & Futai, M. (2002) Differential localization of the vacuolar H+ pump with G subunit isoforms (G1 and G2) in mouse neurons. J Biol Chem, 277, 36296-36303.
    • (2002) J Biol Chem , vol.277 , pp. 36296-36303
    • Murata, Y.1    Sun-Wada, G.-H.2    Yoshimizu, T.3    Yamamoto, A.4    Wada, Y.5    Futai, M.6
  • 61
    • 79960112075 scopus 로고    scopus 로고
    • Structural divergence of the rotary ATPases
    • Muench, S. P., Trinick, J. & Harrison, M. A. (2011). Structural divergence of the rotary ATPases. Q Rev Biophys, 44, 311-356.
    • (2011) Q Rev Biophys , vol.44 , pp. 311-356
    • Muench, S.P.1    Trinick, J.2    Harrison, M.A.3
  • 62
    • 33745087807 scopus 로고    scopus 로고
    • Stochastic proton pumping ATPases: from single molecules to diverse physiological roles
    • Nakanishi-Matsui, M. & Futai, M. (2006). Stochastic proton pumping ATPases: from single molecules to diverse physiological roles. IUBMB Life, 58, 318-322.
    • (2006) IUBMB Life , vol.58 , pp. 318-322
    • Nakanishi-Matsui, M.1    Futai, M.2
  • 64
    • 0032946360 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane proton-adenosinetriphosphatases
    • Nelson, N. & Harvey, W. R. (1999). Vacuolar and plasma membrane proton-adenosinetriphosphatases. Physiol Rev, 79, 361-385.
    • (1999) Physiol Rev , vol.79 , pp. 361-385
    • Nelson, N.1    Harvey, W.R.2
  • 65
    • 0026554164 scopus 로고
    • Selectively amplified expression of an isoform of the vacuolar H+-ATPase 56-kilodalton subunit in renal intercalated cells
    • Nelson, R. D., Guo, X. L., Masood, K., Brown, D., Kalkbrenner, M. & Gluck, S. (1992). Selectively amplified expression of an isoform of the vacuolar H+-ATPase 56-kilodalton subunit in renal intercalated cells. Proc Natl Acad Sci U S A, 89, 3541-3545.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 3541-3545
    • Nelson, R.D.1    Guo, X.L.2    Masood, K.3    Brown, D.4    Kalkbrenner, M.5    Gluck, S.6
  • 66
    • 0344443771 scopus 로고    scopus 로고
    • Expression and function of the mouse V-ATPase d subunit isoforms
    • Nishi, T., Kawasaki-Nishi, S. & Forgac, M. (2003). Expression and function of the mouse V-ATPase d subunit isoforms. J Biol Chem, 278, 46396-46402.
    • (2003) J Biol Chem , vol.278 , pp. 46396-46402
    • Nishi, T.1    Kawasaki-Nishi, S.2    Forgac, M.3
  • 68
    • 77955298786 scopus 로고    scopus 로고
    • Domain characterization and intercation of the yeast vacuolar ATPase subunit C with the peripheral stator stalk subunits E and G
    • Oot, R. A. & Wilkens, S. (2010). Domain characterization and intercation of the yeast vacuolar ATPase subunit C with the peripheral stator stalk subunits E and G. J Biol Chem, 285, 24654-24664.
    • (2010) J Biol Chem , vol.285 , pp. 24654-24664
    • Oot, R.A.1    Wilkens, S.2
  • 69
    • 29144452984 scopus 로고    scopus 로고
    • The Epididymis in the Post-Genome Era
    • B. T. Hinton, & T. T. Turner (Eds.), Charlottesville, VA: The Van Doren Company.
    • Orgebin-Crist, M.-C. (2003). The Epididymis in the Post-Genome Era. In B. T. Hinton, & T. T. Turner (Eds.), The Third International Conference on the Epididymis (pp. 2-22). Charlottesville, VA: The Van Doren Company.
    • (2003) The Third International Conference on the Epididymis , pp. 2-22
    • Orgebin-Crist, M.-C.1
  • 71
    • 39349095242 scopus 로고    scopus 로고
    • Alkaline pH- and cAMP-induced V-ATPase membrane accumulation is mediated by protein kinase A in epididymal clear cells
    • Pastor-Soler, N., Hallows, K. R., Smolak, C., Gong, F., Brown, D. & Breton, S. (2008). Alkaline pH- and cAMP-induced V-ATPase membrane accumulation is mediated by protein kinase A in epididymal clear cells. Am J Physiol Cell Physiol, 294, C488-C494.
    • (2008) Am J Physiol Cell Physiol , vol.294
    • Pastor-Soler, N.1    Hallows, K.R.2    Smolak, C.3    Gong, F.4    Brown, D.5    Breton, S.6
  • 72
    • 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. (2005). Role of acid/base transporters in the male reproductive tract and potential consequences of their malfunction. Physiology (Bethesda), 20, 417-428.
    • (2005) Physiology (Bethesda) , vol.20 , pp. 417-428
    • Pastor-Soler, N.1    Pietrement, C.2    Breton, S.3
  • 74
    • 77950346420 scopus 로고    scopus 로고
    • Porcine vas deferens luminal pH is acutely increased by systemic xylazine administration
    • Pierucci-Alves, F., Duncan, C. L., Lillich, J. D. & Schultz, B. D. (2010). Porcine vas deferens luminal pH is acutely increased by systemic xylazine administration. Biol Reprod, 82, 132-135.
    • (2010) Biol Reprod , vol.82 , pp. 132-135
    • Pierucci-Alves, F.1    Duncan, C.L.2    Lillich, J.D.3    Schultz, B.D.4
  • 75
    • 50849101658 scopus 로고    scopus 로고
    • Bradykinin-stimulated cyclooxygenase activity stimulates vas deferens epithelial anion secretion in vitro in swine and humans
    • Pierucci-Alves, F. & Schultz, B. D. (2008). Bradykinin-stimulated cyclooxygenase activity stimulates vas deferens epithelial anion secretion in vitro in swine and humans. Biol Reprod, 79, 501-509.
    • (2008) Biol Reprod , vol.79 , pp. 501-509
    • Pierucci-Alves, F.1    Schultz, B.D.2
  • 79
    • 84895355557 scopus 로고    scopus 로고
    • Involvement of CFTR in ATP and HCO3- secretion in epididymal principal cells
    • Ruan, Y. C., Da Silva, N., Belleannee, C., Shum, W. W. C. & Breton, S. (2011). Involvement of CFTR in ATP and HCO3- secretion in epididymal principal cells. FASEB J, 25, 1039-1011.
    • (2011) FASEB J , vol.25 , pp. 1039-1011
    • Ruan, Y.C.1    Da Silva, N.2    Belleannee, C.3    Shum, W.W.C.4    Breton, S.5
  • 80
    • 1242297702 scopus 로고    scopus 로고
    • Immunolocalization and regulation of cystic fibrosis transmembrane conductance regulator in the adult rat epididymis
    • Ruz, R., Andonian, S. & Hermo, L. (2004). Immunolocalization and regulation of cystic fibrosis transmembrane conductance regulator in the adult rat epididymis. J Androl, 25, 265-273.
    • (2004) J Androl , vol.25 , pp. 265-273
    • Ruz, R.1    Andonian, S.2    Hermo, L.3
  • 81
    • 4143124567 scopus 로고    scopus 로고
    • Vasectomy-dependent dysregulation of a local renin-angiotensin system in the epididymis of the cynomolgus monkey (Macaca fascicularis)
    • Saez, F., Legare, C., Laflamme, J. & Sullivan, R. (2004). Vasectomy-dependent dysregulation of a local renin-angiotensin system in the epididymis of the cynomolgus monkey (Macaca fascicularis). J Androl, 25, 784-796.
    • (2004) J Androl , vol.25 , pp. 784-796
    • Saez, F.1    Legare, C.2    Laflamme, J.3    Sullivan, R.4
  • 82
    • 66449120515 scopus 로고    scopus 로고
    • The little we know on the structure and machinery of V-ATPase
    • Saroussi, S. & Nelson, N. (2009). The little we know on the structure and machinery of V-ATPase. J Exp Biol, 212, 1604-1610.
    • (2009) J Exp Biol , vol.212 , pp. 1604-1610
    • Saroussi, S.1    Nelson, N.2
  • 83
    • 0034819652 scopus 로고    scopus 로고
    • Neurotransmitter-stimulated ion transport by cultured porcine vas deferens epithelium
    • Sedlacek, R. L., Carlin, R. W., Singh, A. K. & Schultz, B. D. (2001). Neurotransmitter-stimulated ion transport by cultured porcine vas deferens epithelium. Am J Physiol Renal Physiol, 281, F557-570.
    • (2001) Am J Physiol Renal Physiol , vol.281
    • Sedlacek, R.L.1    Carlin, R.W.2    Singh, A.K.3    Schultz, B.D.4
  • 84
    • 79959851524 scopus 로고    scopus 로고
    • Regulation of V-ATPase recycling via a RhoA- and ROCKII-dependent pathway in epididymal clear cells
    • Shum, W. W., Da Silva, N., Belleannee, C., McKee, M., Brown, D. & Breton, S. (2011). Regulation of V-ATPase recycling via a RhoA- and ROCKII-dependent pathway in epididymal clear cells. Am J Physiol Cell Physiol, 301, C31-43.
    • (2011) Am J Physiol Cell Physiol , vol.301
    • Shum, W.W.1    Da Silva, N.2    Belleannee, C.3    McKee, M.4    Brown, D.5    Breton, S.6
  • 85
    • 66449115242 scopus 로고    scopus 로고
    • Regulation of luminal acidification in the male reproductive tract via cell-cell crosstalk
    • Shum, W. W., Da Silva, N., Brown, D. & Breton, S. (2009). Regulation of luminal acidification in the male reproductive tract via cell-cell crosstalk. J Exp Biol, 212, 1753-1761.
    • (2009) J Exp Biol , vol.212 , pp. 1753-1761
    • Shum, W.W.1    Da Silva, N.2    Brown, D.3    Breton, S.4
  • 86
    • 57149125826 scopus 로고    scopus 로고
    • Transepithelial projections from basal cells are luminal sensors in pseudostratified epithelia
    • Shum, W. W., Da Silva, N., McKee, M., Smith, P. J. S., Brown, D. & Breton, S. (2008). Transepithelial projections from basal cells are luminal sensors in pseudostratified epithelia. Cell, 135, 1108-1117.
    • (2008) Cell , vol.135 , pp. 1108-1117
    • Shum, W.W.1    Da Silva, N.2    McKee, M.3    Smith, P.J.S.4    Brown, D.5    Breton, S.6
  • 87
    • 80455129706 scopus 로고    scopus 로고
    • Establishment of cell-cell cross talk in the epididymis: control of luminal acidification
    • Shum, W. W., Ruan, Y. C., Da Silva, N. & Breton, S. (2011). Establishment of cell-cell cross talk in the epididymis: control of luminal acidification. J Androl, 32, 576-586.
    • (2011) J Androl , vol.32 , pp. 576-586
    • Shum, W.W.1    Ruan, Y.C.2    Da Silva, N.3    Breton, S.4
  • 88
    • 0037134525 scopus 로고    scopus 로고
    • The RAVE complex is essential for stable assembly of the yeast V-ATPase
    • Smardon, A. M., Tarsio, M. & Kane, P. M. (2002). The RAVE complex is essential for stable assembly of the yeast V-ATPase. J Biol Chem, 277, 13831-13839.
    • (2002) J Biol Chem , vol.277 , pp. 13831-13839
    • Smardon, A.M.1    Tarsio, M.2    Kane, P.M.3
  • 89
    • 34548826217 scopus 로고    scopus 로고
    • RAVE is essential for the efficient assembly of the C subunit with the vacuolar H+-ATPase
    • Smardon, A. M. & Kane, P. M. (2007). RAVE is essential for the efficient assembly of the C subunit with the vacuolar H+-ATPase. J Biol Chem, 282, 26185-26194.
    • (2007) J Biol Chem , vol.282 , pp. 26185-26194
    • Smardon, A.M.1    Kane, P.M.2
  • 92
    • 0028898233 scopus 로고
    • Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits
    • Sumner, J.-P., Dow, J. A. T., Earley, F. G. P., Klein, U., Jäger, D. & Wieczorek, H. (1995). Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits. J Biol Chem, 270, 5649-5653.
    • (1995) J Biol Chem , vol.270 , pp. 5649-5653
    • Sumner, J.-P.1    Dow, J.A.T.2    Earley, F.G.P.3    Klein, U.4    Jäger, D.5    Wieczorek, H.6
  • 93
    • 0037124047 scopus 로고    scopus 로고
    • A proton pump ATPase with testis-specific E1-subunit isoform required for acrosome acidification
    • Sun-Wada, G.-H., Imai-Senga, Y., Yamamoto, A., Murata, Y., Hirata, T., Wada, Y. & Futai, M. (2002). A proton pump ATPase with testis-specific E1-subunit isoform required for acrosome acidification. J Biol Chem, 277, 18098-18105.
    • (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
  • 94
    • 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, G.-H., Murata, Y., Namba, M., Yamamoto, A., Wada, Y. & Futai, M. (2003). 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) 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
  • 95
    • 0034671585 scopus 로고    scopus 로고
    • Acidic endomembrane organelles are required for mouse postimplantation development
    • Sun-Wada, G., Murata, Y., Yamamoto, A., Kanazawa, H., Wada, Y. & Futai, M. (2000). Acidic endomembrane organelles are required for mouse postimplantation development. Dev Biol, 228, 315-325.
    • (2000) Dev Biol , vol.228 , pp. 315-325
    • Sun-Wada, G.1    Murata, Y.2    Yamamoto, A.3    Kanazawa, H.4    Wada, Y.5    Futai, M.6
  • 96
    • 34347376734 scopus 로고    scopus 로고
    • Differential expression of a subunit isoforms of the vacuolar-type proton pump ATPase in mouse endocrine tissues
    • Sun-Wada, G.-H., Tabata, H., Futai, M. & Wada, Y. (2007). Differential expression of a subunit isoforms of the vacuolar-type proton pump ATPase in mouse endocrine tissues. Cell Tissue Res, 329, 239-248.
    • (2007) Cell Tissue Res , vol.329 , pp. 239-248
    • Sun-Wada, G.-H.1    Tabata, H.2    Futai, M.3    Wada, Y.4
  • 97
    • 1342310842 scopus 로고    scopus 로고
    • Lysosome and lysosome-related organelles responsible for specialized functions in higher organisms, with special emphasis on vacuolar-type proton ATPase
    • Sun-Wada, G.-H., Wada, Y. & Futai, M. (2003). Lysosome and lysosome-related organelles responsible for specialized functions in higher organisms, with special emphasis on vacuolar-type proton ATPase. Cell Struct Funct, 28, 455-463.
    • (2003) Cell Struct Funct , vol.28 , pp. 455-463
    • Sun-Wada, G.-H.1    Wada, Y.2    Futai, M.3
  • 98
    • 3542998744 scopus 로고    scopus 로고
    • Diverse and essential roles of mammalian vacuolar-type proton pump ATPase: towards the physiological understanding of inside acidic compartments
    • Sun-Wada, G.-H., Wada, Y. & Futai, M. (2004). Diverse and essential roles of mammalian vacuolar-type proton pump ATPase: towards the physiological understanding of inside acidic compartments. Biochim Biophys Acta, 1658, 106-114.
    • (2004) Biochim Biophys Acta , vol.1658 , pp. 106-114
    • Sun-Wada, G.-H.1    Wada, Y.2    Futai, M.3
  • 99
    • 0037413670 scopus 로고    scopus 로고
    • Diversity of mouse proton-translocating ATPase: presence of multiple isoforms of the C, d, and G subunits
    • Sun-Wada, G.-H., Yoshimizu, T., Imai-Senga, Y., Wada, Y. & Futai, M. (2003). Diversity of mouse proton-translocating ATPase: presence of multiple isoforms of the C, d, and G subunits. Gene, 302, 147-153.
    • (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
  • 100
    • 27144497523 scopus 로고    scopus 로고
    • Shedding of the germinal angiotensin I-converting enzyme (gACE) involves a serine protease and is activated by epididymal fluid
    • Thimon, V., Metayer, S., Belghazi, M., Dacheux, F., Dacheux, J. L. & Gatti, J. L. (2005). Shedding of the germinal angiotensin I-converting enzyme (gACE) involves a serine protease and is activated by epididymal fluid. Biol Reprod, 73, 881-890.
    • (2005) Biol Reprod , vol.73 , pp. 881-890
    • Thimon, V.1    Metayer, S.2    Belghazi, M.3    Dacheux, F.4    Dacheux, J.L.5    Gatti, J.L.6
  • 101
    • 77953255215 scopus 로고    scopus 로고
    • Regulation and isoform function of the V-ATPases
    • Toei, M., Saum, R. & Forgac, M. (2010). Regulation and isoform function of the V-ATPases. Biochemistry, 49, 4715-4723.
    • (2010) Biochemistry , vol.49 , pp. 4715-4723
    • Toei, M.1    Saum, R.2    Forgac, M.3
  • 102
    • 0037936890 scopus 로고    scopus 로고
    • From lysosome to the plasma membrane: localization of vacuolar-type H+-ATPase with the a3 isoform during osteoclast differentiation
    • Toyomura, T., Mutara, Y., Yamamoto, A., Oka, T., Sun-Wada, G.-H., Wada, Y. & Futai, M. (2003). From lysosome to the plasma membrane: localization of vacuolar-type H+-ATPase with the a3 isoform during osteoclast differentiation. J Biol Chem, 278, 22023-22030.
    • (2003) J Biol Chem , vol.278 , pp. 22023-22030
    • Toyomura, T.1    Mutara, Y.2    Yamamoto, A.3    Oka, T.4    Sun-Wada, G.-H.5    Wada, Y.6    Futai, M.7
  • 103
    • 0034708665 scopus 로고    scopus 로고
    • Three subunit a isoforms of mouse vacuolar H+-ATPase Preferential expression of the a3 isoform during osteoclast differentiation
    • Toyomura, T., Oka, T., Yamaguchi, C., Wada, Y. & Futai, M. (2000). Three subunit a isoforms of mouse vacuolar H+-ATPase. Preferential expression of the a3 isoform during osteoclast differentiation. J Biol Chem, 275, 8760-8765.
    • (2000) J Biol Chem , vol.275 , pp. 8760-8765
    • Toyomura, T.1    Oka, T.2    Yamaguchi, C.3    Wada, Y.4    Futai, M.5
  • 104
    • 0029883545 scopus 로고    scopus 로고
    • Cystic fibrosis mutation screening in healthy men with reduced sperm quality
    • van der Ven, K., Messer L, van der Ven, H., Jeyendran, R. S. & Ober, C. (1996). Cystic fibrosis mutation screening in healthy men with reduced sperm quality. Hum Reprod, 11, 513-517.
    • (1996) Hum Reprod , vol.11 , pp. 513-517
    • Van der Ven, K.1    Messer, L.2    Van der Ven, H.3    Jeyendran, R.S.4    Ober, C.5
  • 105
    • 84887212452 scopus 로고    scopus 로고
    • The forkhead transcription factor Foxi1 is a master regulator of vacuolar H+-ATPase proton pump subunits in the inner ear, kidney and epididymis
    • Vidarsson, H., Westergren, R., Heglind, M., Blomqvist, S. R., Breton, S. & Enerbäck, S. (2009). The forkhead transcription factor Foxi1 is a master regulator of vacuolar H+-ATPase proton pump subunits in the inner ear, kidney and epididymis. PLoS One, 4, e4471.
    • (2009) PLoS One , vol.4
    • Vidarsson, H.1    Westergren, R.2    Heglind, M.3    Blomqvist, S.R.4    Breton, S.5    Enerbäck, S.6
  • 106
    • 0038043266 scopus 로고    scopus 로고
    • A novel role for subunit C in mediating binding of the H+-V-ATPase to the actin cytoskeleton
    • Vitavska, O., Wieczorek, H. & Merzendorfer, H. (2003). A novel role for subunit C in mediating binding of the H+-V-ATPase to the actin cytoskeleton. J Biol Chem, 278, 18499-18505.
    • (2003) J Biol Chem , vol.278 , pp. 18499-18505
    • Vitavska, O.1    Wieczorek, H.2    Merzendorfer, H.3
  • 108
    • 0031906403 scopus 로고    scopus 로고
    • CFTR gene and male fertility
    • Wong, P. Y. (1998). CFTR gene and male fertility. Mol Hum Reprod, 4, 107-110.
    • (1998) Mol Hum Reprod , vol.4 , pp. 107-110
    • Wong, P.Y.1
  • 109
    • 0025368643 scopus 로고
    • The role of angiotensin-converting enzyme in the rat epididymis
    • Wong, P. Y. & Uchendu, C. N. (1990). The role of angiotensin-converting enzyme in the rat epididymis. J Endocrinol, 125, 457-465.
    • (1990) J Endocrinol , vol.125 , pp. 457-465
    • Wong, P.Y.1    Uchendu, C.N.2
  • 111
    • 2342628669 scopus 로고    scopus 로고
    • Increase in luminal pH in the epididymis of the infertile c-ros knock-out mice: putative role of sodium-hydrogen exchangers and vacuolar H+-ATPase
    • Yeung, C.-H., Breton, S., Stetiawan, I., Xu, Y., Lang, F. & Cooper, T. G. (2004). Increase in luminal pH in the epididymis of the infertile c-ros knock-out mice: putative role of sodium-hydrogen exchangers and vacuolar H+-ATPase. Mol Reprod and Development, 68, 159-168.
    • (2004) Mol Reprod and Development , vol.68 , pp. 159-168
    • Yeung, C.-H.1    Breton, S.2    Stetiawan, I.3    Xu, Y.4    Lang, F.5    Cooper, T.G.6
  • 112
    • 0010495847 scopus 로고    scopus 로고
    • Acquisition and development of sperm motility upon maturation in the epididymis
    • B. Robaire, & B. T. Hinton (Eds.), New York, NY: Kluwer Academic/Plenum Publishers.
    • Yeung, C.-H. & Cooper, T. G. (2002). Acquisition and development of sperm motility upon maturation in the epididymis. In B. Robaire, & B. T. Hinton (Eds.), The Epididymis. From molecules to clinical practice (pp. 417-434). New York, NY: Kluwer Academic/Plenum Publishers.
    • (2002) The Epididymis. From molecules to clinical practice , pp. 417-434
    • Yeung, C.-H.1    Cooper, T.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.