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Volumn 86, Issue 5, 2007, Pages 265-273

Localization and regulation of plasma membrane Ca2+-ATPase in bovine spermatozoa

Author keywords

PDC 109; Plasma membrane calcium ATPase; PMCA; Seminal vesicle secretion; Spermatozoa

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CYCLIC AMP DEPENDENT PROTEIN KINASE; PDC 109; PHOSPHOTYROSINE; PROTEIN KINASE C; SECRETORY PROTEIN; THAPSIGARGIN; UNCLASSIFIED DRUG;

EID: 34247365501     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2007.02.003     Document Type: Article
Times cited : (19)

References (40)
  • 1
    • 0023936682 scopus 로고
    • Binding of a major secretory protein from bull seminal vesicles to bovine spermatozoa
    • Aumüller G., Vesper M., Seitz J., Kemme M., and Scheit K.H. Binding of a major secretory protein from bull seminal vesicles to bovine spermatozoa. Cell Tissue Res. 252 (1988) 377-384
    • (1988) Cell Tissue Res. , vol.252 , pp. 377-384
    • Aumüller, G.1    Vesper, M.2    Seitz, J.3    Kemme, M.4    Scheit, K.H.5
  • 2
    • 0023645805 scopus 로고
    • 2+] and pH of mammalian sperm by voltage-dependent and pH-sensitive mechanisms
    • 2+] and pH of mammalian sperm by voltage-dependent and pH-sensitive mechanisms. J. Biol. Chem. 262 (1987) 15041-15047
    • (1987) J. Biol. Chem. , vol.262 , pp. 15041-15047
    • Babcock, D.F.1    Pfeiffer, D.R.2
  • 3
    • 0028206947 scopus 로고
    • The zona pellucida-induced acrosome reaction of human spermatozoa is mediated by protein kinases
    • Bielfeld P., Faridi A., Zaneveld L.J., and De Jonge C.J. The zona pellucida-induced acrosome reaction of human spermatozoa is mediated by protein kinases. Fertil. Steril. 61 (1994) 536-541
    • (1994) Fertil. Steril. , vol.61 , pp. 536-541
    • Bielfeld, P.1    Faridi, A.2    Zaneveld, L.J.3    De Jonge, C.J.4
  • 4
    • 0024370729 scopus 로고
    • Plasma membrane calcium pump and 28-kDa calcium binding protein in cells of rat kidney distal tubules
    • Borke J.L., Caride A., Verma A.K., Penniston J.T., and Kumar R. Plasma membrane calcium pump and 28-kDa calcium binding protein in cells of rat kidney distal tubules. Am. J. Physiol. 257 (1989) F842-F849
    • (1989) Am. J. Physiol. , vol.257
    • Borke, J.L.1    Caride, A.2    Verma, A.K.3    Penniston, J.T.4    Kumar, R.5
  • 6
    • 0026609630 scopus 로고
    • 2+ pump of the plasma membrane
    • 2+ pump of the plasma membrane. J. Biol. Chem. 267 (1992) 2115-2118
    • (1992) J. Biol. Chem. , vol.267 , pp. 2115-2118
    • Carafoli, E.1
  • 7
    • 0028113894 scopus 로고
    • Biogenesis: plasma membrane calcium ATPase: 15 years of work on the purified enzyme
    • Carafoli E. Biogenesis: plasma membrane calcium ATPase: 15 years of work on the purified enzyme. FASEB J. 8 (1994) 993-1002
    • (1994) FASEB J. , vol.8 , pp. 993-1002
    • Carafoli, E.1
  • 8
    • 0034124717 scopus 로고    scopus 로고
    • Calcium pumps: structural basis for and mechanism of calcium transmembrane transport
    • Carafoli E., and Brini M. Calcium pumps: structural basis for and mechanism of calcium transmembrane transport. Curr. Opin. Chem. Biol. 4 (2000) 152-161
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 152-161
    • Carafoli, E.1    Brini, M.2
  • 9
    • 0030467311 scopus 로고    scopus 로고
    • The plasma membrane calcium pump: recent developments and future perspectives
    • Carafoli E., Garcia-Martin E., and Guerini D. The plasma membrane calcium pump: recent developments and future perspectives. Experientia 52 (1996) 1091-1100
    • (1996) Experientia , vol.52 , pp. 1091-1100
    • Carafoli, E.1    Garcia-Martin, E.2    Guerini, D.3
  • 11
    • 0031049037 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphorylation during bovine sperm capacitation by a cyclic adenosine 3′5′-monophosphate-dependent pathway
    • Galantino-Homer H.L., Visconti P.E., and Kopf G.S. Regulation of protein tyrosine phosphorylation during bovine sperm capacitation by a cyclic adenosine 3′5′-monophosphate-dependent pathway. Biol. Reprod. 56 (1997) 707-719
    • (1997) Biol. Reprod. , vol.56 , pp. 707-719
    • Galantino-Homer, H.L.1    Visconti, P.E.2    Kopf, G.S.3
  • 12
    • 0032216699 scopus 로고    scopus 로고
    • 2+ exchangers
    • 2+ exchangers. Biometals 11 (1998) 319-330
    • (1998) Biometals , vol.11 , pp. 319-330
    • Guerini, D.1
  • 13
    • 0032130859 scopus 로고    scopus 로고
    • The calcium pump of the plasma membrane: membrane targeting, calcium binding sites, tissue-specific isoform expression
    • Guerini D., Garcia-Martin E., Zecca A., Guidi F., and Carafoli E. The calcium pump of the plasma membrane: membrane targeting, calcium binding sites, tissue-specific isoform expression. Acta Physiol. Scand.-Suppl. 643 (1998) 265-273
    • (1998) Acta Physiol. Scand.-Suppl. , vol.643 , pp. 265-273
    • Guerini, D.1    Garcia-Martin, E.2    Zecca, A.3    Guidi, F.4    Carafoli, E.5
  • 14
    • 0034002037 scopus 로고    scopus 로고
    • Involvement of protein kinase A and A kinase anchoring protein in the progesterone-initiated human sperm acrosome reaction
    • Harrison D.A., Carr D.W., and Meizel S. Involvement of protein kinase A and A kinase anchoring protein in the progesterone-initiated human sperm acrosome reaction. Biol. Reprod. 62 (2000) 811-820
    • (2000) Biol. Reprod. , vol.62 , pp. 811-820
    • Harrison, D.A.1    Carr, D.W.2    Meizel, S.3
  • 15
    • 0029792629 scopus 로고    scopus 로고
    • Cyclic adenosine 3′,5′monophosphate-dependent regulation of protein tyrosine phosphorylation in relation to human sperm capacitation and motility
    • Leclerc P., de Lamirande E., and Gagnon C. Cyclic adenosine 3′,5′monophosphate-dependent regulation of protein tyrosine phosphorylation in relation to human sperm capacitation and motility. Biol. Reprod. 55 (1996) 684-692
    • (1996) Biol. Reprod. , vol.55 , pp. 684-692
    • Leclerc, P.1    de Lamirande, E.2    Gagnon, C.3
  • 16
    • 0036270879 scopus 로고    scopus 로고
    • Role of seminal plasma phospholipid-binding proteins in sperm membrane lipid modification that occurs during capacitation
    • Manjunath P., and Therien I. Role of seminal plasma phospholipid-binding proteins in sperm membrane lipid modification that occurs during capacitation. J. Reprod. Immunol. 53 (2002) 109-119
    • (2002) J. Reprod. Immunol. , vol.53 , pp. 109-119
    • Manjunath, P.1    Therien, I.2
  • 17
    • 0034710607 scopus 로고    scopus 로고
    • Characteristics of the cholesterol efflux induced by novel seminal phospholipid-binding proteins
    • Moreau R., and Manjunath P. Characteristics of the cholesterol efflux induced by novel seminal phospholipid-binding proteins. Biochim. Biophys. Acta 1487 (2000) 24-32
    • (2000) Biochim. Biophys. Acta , vol.1487 , pp. 24-32
    • Moreau, R.1    Manjunath, P.2
  • 18
    • 0033583560 scopus 로고    scopus 로고
    • Seminal plasma choline phospholipid-binding proteins stimulate cellular cholesterol and phospholipid efflux
    • Moreau R., Frank P.G., Perreault C., Marcel Y.L., and Manjunath P. Seminal plasma choline phospholipid-binding proteins stimulate cellular cholesterol and phospholipid efflux. Biochim. Biophys. Acta 1438 (1999) 38-46
    • (1999) Biochim. Biophys. Acta , vol.1438 , pp. 38-46
    • Moreau, R.1    Frank, P.G.2    Perreault, C.3    Marcel, Y.L.4    Manjunath, P.5
  • 20
    • 0031453259 scopus 로고    scopus 로고
    • Protein kinase C and mammalian spermatozoa acrosome reaction
    • Naor Z., and Breitbart H. Protein kinase C and mammalian spermatozoa acrosome reaction. Trends Endocrinol. Metab. 8 (1997) 337-342
    • (1997) Trends Endocrinol. Metab. , vol.8 , pp. 337-342
    • Naor, Z.1    Breitbart, H.2
  • 22
    • 0032732658 scopus 로고    scopus 로고
    • Regulation of human sperm capacitation by a cholesterol efflux-stimulated signal transduction pathway leading to protein kinase A-mediated up-regulation of protein tyrosine phosphorylation
    • Osheroff J.E., Visconti P.E., Valenzuela J.P., Travis A.J., Alvarez J., and Kopf G.S. Regulation of human sperm capacitation by a cholesterol efflux-stimulated signal transduction pathway leading to protein kinase A-mediated up-regulation of protein tyrosine phosphorylation. Mol. Hum. Reprod. 5 (1999) 1017-1026
    • (1999) Mol. Hum. Reprod. , vol.5 , pp. 1017-1026
    • Osheroff, J.E.1    Visconti, P.E.2    Valenzuela, J.P.3    Travis, A.J.4    Alvarez, J.5    Kopf, G.S.6
  • 23
    • 0034026935 scopus 로고    scopus 로고
    • Ca(2+) entry through store-operated channels in mouse sperm is initiated by egg ZP3 and drives the acrosome reaction
    • O'Toole C.M., Arnoult C., Darszon A., Steinhardt R.A., and Florman H.M. Ca(2+) entry through store-operated channels in mouse sperm is initiated by egg ZP3 and drives the acrosome reaction. Mol. Biol. Cell 11 (2000) 1571-1584
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1571-1584
    • O'Toole, C.M.1    Arnoult, C.2    Darszon, A.3    Steinhardt, R.A.4    Florman, H.M.5
  • 26
    • 0032589206 scopus 로고    scopus 로고
    • 2+ channels and the acrosome reaction: which channels are present and what do they do?
    • 2+ channels and the acrosome reaction: which channels are present and what do they do?. Hum. Reprod. 14 (1999) 873-879
    • (1999) Hum. Reprod. , vol.14 , pp. 873-879
    • Publicover, S.J.1    Barratt, C.L.2
  • 29
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 31
    • 0025753477 scopus 로고
    • Biochemical characterization of a calcium ion stimulated-ATPase from goat spermatozoa
    • Sikdar R., Ganguly U., Pal P., Mazumder B., and Sen P.C. Biochemical characterization of a calcium ion stimulated-ATPase from goat spermatozoa. Mol. Cell. Biochem. 103 (1991) 121-130
    • (1991) Mol. Cell. Biochem. , vol.103 , pp. 121-130
    • Sikdar, R.1    Ganguly, U.2    Pal, P.3    Mazumder, B.4    Sen, P.C.5
  • 32
    • 0036008839 scopus 로고    scopus 로고
    • Mutation of the C alpha subunit of PKA leads to growth retardation and sperm dysfunction
    • Skalhegg B.S., Huang Y., Su T., Idzerda R.L., McKnight G.S., and Burton K.A. Mutation of the C alpha subunit of PKA leads to growth retardation and sperm dysfunction. Mol. Endocrinol. 16 (2002) 630-639
    • (2002) Mol. Endocrinol. , vol.16 , pp. 630-639
    • Skalhegg, B.S.1    Huang, Y.2    Su, T.3    Idzerda, R.L.4    McKnight, G.S.5    Burton, K.A.6
  • 33
    • 0035137205 scopus 로고    scopus 로고
    • Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps
    • Strehler E.E., and Zacharias D.A. Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. Physiol. Rev. 81 (2001) 21-50
    • (2001) Physiol. Rev. , vol.81 , pp. 21-50
    • Strehler, E.E.1    Zacharias, D.A.2
  • 34
    • 1942421320 scopus 로고    scopus 로고
    • Calcium pumps of plasma membrane and cell interior
    • Strehler E.E., and Treiman M. Calcium pumps of plasma membrane and cell interior. Curr. Mol. Med. 4 (2004) 323-335
    • (2004) Curr. Mol. Med. , vol.4 , pp. 323-335
    • Strehler, E.E.1    Treiman, M.2
  • 35
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa, II: protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti P.E., Moore G.D., Bailey J.L., Leclerc P., Connors S.A., Pan D., Olds-Clarke P., and Kopf G.S. Capacitation of mouse spermatozoa, II: protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 121 (1995) 1139-1150
    • (1995) Development , vol.121 , pp. 1139-1150
    • Visconti, P.E.1    Moore, G.D.2    Bailey, J.L.3    Leclerc, P.4    Connors, S.A.5    Pan, D.6    Olds-Clarke, P.7    Kopf, G.S.8
  • 37
    • 0036223099 scopus 로고    scopus 로고
    • Sperm coating mechanism from the 1.8 Å crystal structure of PDC-109-phosphorylcholine complex
    • Wah D.A., Fernandez-Tornero C., Sanz L., Romero A., and Calvete J.J. Sperm coating mechanism from the 1.8 Å crystal structure of PDC-109-phosphorylcholine complex. Structure (Cambridge) 10 (2002) 505-514
    • (2002) Structure (Cambridge) , vol.10 , pp. 505-514
    • Wah, D.A.1    Fernandez-Tornero, C.2    Sanz, L.3    Romero, A.4    Calvete, J.J.5
  • 38
    • 0037488140 scopus 로고    scopus 로고
    • Calcium clearance mechanisms of mouse sperm
    • Wennemuth G., Babcock D.F., and Hille B. Calcium clearance mechanisms of mouse sperm. J. Gen. Physiol. 122 (2003) 115-128
    • (2003) J. Gen. Physiol. , vol.122 , pp. 115-128
    • Wennemuth, G.1    Babcock, D.F.2    Hille, B.3
  • 40
    • 0347504937 scopus 로고    scopus 로고
    • Effects of Ca-ATPase inhibitors on the intracellular calcium activity and motility of human spermatozoa
    • Williams K.M., and Ford W.C. Effects of Ca-ATPase inhibitors on the intracellular calcium activity and motility of human spermatozoa. Int. J. Androl. 26 (2003) 366-375
    • (2003) Int. J. Androl. , vol.26 , pp. 366-375
    • Williams, K.M.1    Ford, W.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.