메뉴 건너뛰기




Volumn 33, Issue 6, 2010, Pages 775-783

Arrangement of PMCA4 in bovine sperm membrane fractions

Author keywords

Detergent resistant membranes; Lipid raft; PDC 109; Plasma membrane Ca2+ ATPase; Spermatozoa

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CAVEOLIN; PLASMA MEMBRANE CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; PLASMA MEMBRANE CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE 4; PROTEIN PDC 109; SEMINAL PLASMA PROTEIN; UNCLASSIFIED DRUG;

EID: 78650492283     PISSN: 01056263     EISSN: 13652605     Source Type: Journal    
DOI: 10.1111/j.1365-2605.2009.01022.x     Document Type: Article
Times cited : (15)

References (48)
  • 1
    • 38449102038 scopus 로고    scopus 로고
    • The multi-pdz domain protein mupp1 as a lipid raft-associated scaffolding protein controlling the acrosome reaction in mammalian spermatozoa
    • Ackermann, F., Zitranski, N., Heydecke, D., Wilhelm, B., Gudermann, T. & Boekhoff, I. (2008) The multi-pdz domain protein mupp1 as a lipid raft-associated scaffolding protein controlling the acrosome reaction in mammalian spermatozoa. Journal of Cell Physiology 214, 757-768.
    • (2008) Journal of Cell Physiology , vol.214 , pp. 757-768
    • Ackermann, F.1    Zitranski, N.2    Heydecke, D.3    Wilhelm, B.4    Gudermann, T.5    Boekhoff, I.6
  • 2
    • 0031010267 scopus 로고    scopus 로고
    • Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins
    • Bickel, P. E., Scherer, P. E., Schnitzer, J. E., Oh, P., Lisanti, M. P. & Lodish, H. F. (1997) Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins. Journal of Biological Chemistry 272, 13793-13802.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 13793-13802
    • Bickel, P.E.1    Scherer, P.E.2    Schnitzer, J.E.3    Oh, P.4    Lisanti, M.P.5    Lodish, H.F.6
  • 3
    • 30544450854 scopus 로고    scopus 로고
    • Sperm capacitation induces an increase in lipid rafts having zona pellucida binding ability and containing sulfogalactosylglycerolipid
    • Bou Khalil, M., Chakrabandhu, K., Xu, H., Weerachatyanukul, W., Buhr, M., Berger, T. et al. (2006) Sperm capacitation induces an increase in lipid rafts having zona pellucida binding ability and containing sulfogalactosylglycerolipid. Developmental Biology 290, 220-235.
    • (2006) Developmental Biology , vol.290 , pp. 220-235
    • Bou Khalil, M.1    Chakrabandhu, K.2    Xu, H.3    Weerachatyanukul, W.4    Buhr, M.5    Berger, T.6
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0026512314 scopus 로고
    • Sorting of gpi-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D. A. & Rose, J. K. (1992) Sorting of gpi-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 6
    • 0028281031 scopus 로고
    • The plasma membrane calcium pump: functional domains, regulation of the activity, and tissue specificity of isoform expression
    • Carafoli, E. & Stauffer, T. (1994) The plasma membrane calcium pump: functional domains, regulation of the activity, and tissue specificity of isoform expression. Journal of Neurobiology 25, 312-324.
    • (1994) Journal of Neurobiology , vol.25 , pp. 312-324
    • Carafoli, E.1    Stauffer, T.2
  • 8
    • 4544342119 scopus 로고    scopus 로고
    • Reorganization of lipid rafts during capacitation of human sperm
    • Cross, N. L. (2004) Reorganization of lipid rafts during capacitation of human sperm. Biological Reproduction 71, 1367-1373.
    • (2004) Biological Reproduction , vol.71 , pp. 1367-1373
    • Cross, N.L.1
  • 9
    • 0018632834 scopus 로고
    • Studies on the mechanism of capacitation. Ii. Evidence for lipid transfer between plasma membrane of rat sperm and serum albumin during capacitation in vitro
    • Davis, B. K., Byrne, R. & Hungund, B. (1979) Studies on the mechanism of capacitation. Ii. Evidence for lipid transfer between plasma membrane of rat sperm and serum albumin during capacitation in vitro. Biochimca et Biophysica Acta 558, 257-266.
    • (1979) Biochimca et Biophysica Acta , vol.558 , pp. 257-266
    • Davis, B.K.1    Byrne, R.2    Hungund, B.3
  • 10
    • 0026657161 scopus 로고
    • Major proteins of bovine seminal plasma exhibit novel interactions with phospholipid
    • Desnoyers, L. & Manjunath, P. (1992) Major proteins of bovine seminal plasma exhibit novel interactions with phospholipid. Journal Biological Chemistry 267, 10149-10155.
    • (1992) Journal Biological Chemistry , vol.267 , pp. 10149-10155
    • Desnoyers, L.1    Manjunath, P.2
  • 11
    • 0027452708 scopus 로고
    • Calcium pump of the plasma membrane is localized in caveolae
    • Fujimoto, T. (1993) Calcium pump of the plasma membrane is localized in caveolae. Journal of Cell Biology 120, 1147-1157.
    • (1993) Journal of Cell Biology , vol.120 , pp. 1147-1157
    • Fujimoto, T.1
  • 12
    • 0031574069 scopus 로고    scopus 로고
    • Conformational features and thermal stability of bovine seminal plasma protein pdc-109 oligomers and phosphorylcholine-bound complexes
    • Gasset, M., Saiz, J. L., Laynez, J., Sanz, L., Gentzel, M., Topper-Petersen, E. & Calvete, J. J. (1997) Conformational features and thermal stability of bovine seminal plasma protein pdc-109 oligomers and phosphorylcholine-bound complexes. European Journal of Biochemistry 250, 735-744.
    • (1997) European Journal of Biochemistry , vol.250 , pp. 735-744
    • Gasset, M.1    Saiz, J.L.2    Laynez, J.3    Sanz, L.4    Gentzel, M.5    Topper-Petersen, E.6    Calvete, J.J.7
  • 15
    • 43249125248 scopus 로고    scopus 로고
    • Seminal plasma proteins regulate the association of lipids and proteins within detergent-resistant membrane domains of bovine spermatozoa
    • Girouard, J., Frenette, G. & Sullivan, R. (2008) Seminal plasma proteins regulate the association of lipids and proteins within detergent-resistant membrane domains of bovine spermatozoa. Biology Reproduction 78, 921-931.
    • (2008) Biology Reproduction , vol.78 , pp. 921-931
    • Girouard, J.1    Frenette, G.2    Sullivan, R.3
  • 16
    • 0024428942 scopus 로고
    • 2+-transporting atpase that is expressed predominantly in brain and skeletal muscle
    • 2+-transporting atpase that is expressed predominantly in brain and skeletal muscle. Journal of Biological Chemistry 264, 18569-18576.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 18569-18576
    • Greeb, J.1    Shull, G.E.2
  • 17
    • 0025959745 scopus 로고
    • Correlation between changes in rat sperm membrane lipids, protein, and the membrane physical state during epididymal maturation
    • Hall, J. C., Hadley, J. & Doman, T. (1991) Correlation between changes in rat sperm membrane lipids, protein, and the membrane physical state during epididymal maturation. Journal of Andrology 12, 76-87.
    • (1991) Journal of Andrology , vol.12 , pp. 76-87
    • Hall, J.C.1    Hadley, J.2    Doman, T.3
  • 18
    • 0035469893 scopus 로고    scopus 로고
    • Role for lipid rafts in regulating interleukin-2 receptor signaling
    • Marmor, M. D. & Julius, M. (2001) Role for lipid rafts in regulating interleukin-2 receptor signaling. Blood 98, 1489-1497.
    • (2001) Blood , vol.98 , pp. 1489-1497
    • Marmor, M.D.1    Julius, M.2
  • 20
    • 9144272911 scopus 로고    scopus 로고
    • Reduction of glycosphingolipid levels in lipid rafts affects the expression state and function of glycosylphosphatidylinositol-anchored proteins but does not impair signal transduction via the t cell receptor
    • Nagafuku, M., Kabayama, K., Oka, D., Kato, A., Tani-ichi, S., Shimada, Y. et al. (2003) Reduction of glycosphingolipid levels in lipid rafts affects the expression state and function of glycosylphosphatidylinositol-anchored proteins but does not impair signal transduction via the t cell receptor. Journal of Biological Chemistry 278, 51920-51927.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 51920-51927
    • Nagafuku, M.1    Kabayama, K.2    Oka, D.3    Kato, A.4    Tani-ichi, S.5    Shimada, Y.6
  • 21
    • 0019822476 scopus 로고
    • Acidic phospholipids, unsaturated fatty acids, and limited proteolysis mimic the effect of calmodulin on the purified erythrocyte ca2+- atpase
    • Niggli, V., Adunyah, E. S. & Carafoli, E. (1981) Acidic phospholipids, unsaturated fatty acids, and limited proteolysis mimic the effect of calmodulin on the purified erythrocyte ca2+- atpase. Journal of Biological Chemistry 256, 8588-8592.
    • (1981) Journal of Biological Chemistry , vol.256 , pp. 8588-8592
    • Niggli, V.1    Adunyah, E.S.2    Carafoli, E.3
  • 23
    • 4043055834 scopus 로고    scopus 로고
    • Targeted ablation of plasma membrane ca2+-atpase (pmca) 1 and 4 indicates a major housekeeping function for pmca1 and a critical role in hyperactivated sperm motility and male fertility for pmca4
    • Okunade, G. W., Miller, M. L., Pyne, G. J., Sutliff, R. L., O'Connor, K. T., Neumann, J. C. et al. (2004) Targeted ablation of plasma membrane ca2+-atpase (pmca) 1 and 4 indicates a major housekeeping function for pmca1 and a critical role in hyperactivated sperm motility and male fertility for pmca4. Journal of Biological Chemistry 279, 33742-33750.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 33742-33750
    • Okunade, G.W.1    Miller, M.L.2    Pyne, G.J.3    Sutliff, R.L.4    O'Connor, K.T.5    Neumann, J.C.6
  • 24
    • 17644417099 scopus 로고    scopus 로고
    • The characterization of plasma membrane ca2+-atpase in rich sphingomyelin-cholesterol domains
    • Pang, Y., Zhu, H., Wu, P. & Chen, J. (2005) The characterization of plasma membrane ca2+-atpase in rich sphingomyelin-cholesterol domains. FEBS Letters 579, 2397-2403.
    • (2005) FEBS Letters , vol.579 , pp. 2397-2403
    • Pang, Y.1    Zhu, H.2    Wu, P.3    Chen, J.4
  • 25
    • 0024828501 scopus 로고
    • Capacitation of bovine sperm by heparin: Inhibitory effect of glucose and role of intracellular ph
    • Parrish, J. J., Susko-Parrish, J. L. & First, N. L. (1989) Capacitation of bovine sperm by heparin: Inhibitory effect of glucose and role of intracellular ph. Biology of Reproduction 41, 683-699.
    • (1989) Biology of Reproduction , vol.41 , pp. 683-699
    • Parrish, J.J.1    Susko-Parrish, J.L.2    First, N.L.3
  • 26
    • 1242297707 scopus 로고    scopus 로고
    • Interaction of pdc-109, the major secretory protein from bull seminal vesicles, with bovine sperm membrane ca2+-atpase
    • Sanchez-Luengo, S., Aumuller, G., Albrecht, M., Sen, P. C., Rohm, K. & Wilhelm, B. (2004) Interaction of pdc-109, the major secretory protein from bull seminal vesicles, with bovine sperm membrane ca2+-atpase. Journal of Andrology 25, 234-244.
    • (2004) Journal of Andrology , vol.25 , pp. 234-244
    • Sanchez-Luengo, S.1    Aumuller, G.2    Albrecht, M.3    Sen, P.C.4    Rohm, K.5    Wilhelm, B.6
  • 27
  • 29
    • 33644850532 scopus 로고    scopus 로고
    • The plasma membrane ca2+-atpase isoform 4 is localized in lipid rafts of cerebellum synaptic plasma membranes
    • Sepulveda, M. R., Berrocal-Carrillo, M., Gasset, M. & Mata, A. M. (2006) The plasma membrane ca2+-atpase isoform 4 is localized in lipid rafts of cerebellum synaptic plasma membranes. Journal of Biological Chemistry 281, 447-453.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 447-453
    • Sepulveda, M.R.1    Berrocal-Carrillo, M.2    Gasset, M.3    Mata, A.M.4
  • 30
    • 3142724785 scopus 로고    scopus 로고
    • Cholesterol efflux alters lipid raft stability and distribution during capacitation of boar spermatozoa
    • Shadan, S., James, P. S., Howes, E. A. & Jones, R. (2004) Cholesterol efflux alters lipid raft stability and distribution during capacitation of boar spermatozoa. Biology of Reproduction 71, 253-265.
    • (2004) Biology of Reproduction , vol.71 , pp. 253-265
    • Shadan, S.1    James, P.S.2    Howes, E.A.3    Jones, R.4
  • 31
  • 32
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K. & Ikonen, E. (1997) Functional rafts in cell membranes. Nature 387, 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 33
    • 25144513384 scopus 로고    scopus 로고
    • Isolation and proteomic analysis of mouse sperm detergent-resistant membrane fractions: Evidence for dissociation of lipid rafts during capacitation
    • Sleight, S. B., Miranda, P. V., Plaskett, N. W., Maier, B., Lysiak, J., Scrable, H., Herr, J. C. & Visconti, P. E. (2005) Isolation and proteomic analysis of mouse sperm detergent-resistant membrane fractions: Evidence for dissociation of lipid rafts during capacitation. Biology of Reproduction 73, 721-729.
    • (2005) Biology of Reproduction , vol.73 , pp. 721-729
    • Sleight, S.B.1    Miranda, P.V.2    Plaskett, N.W.3    Maier, B.4    Lysiak, J.5    Scrable, H.6    Herr, J.C.7    Visconti, P.E.8
  • 36
    • 0027518196 scopus 로고
    • Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes
    • Stauffer, T. P., Hilfiker, H., Carafoli, E. & Strehler, E. E. (1993) Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. Journal of Biological Chemistry 268, 25993-26003.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 25993-26003
    • Stauffer, T.P.1    Hilfiker, H.2    Carafoli, E.3    Strehler, E.E.4
  • 38
    • 31544453324 scopus 로고    scopus 로고
    • The influence of membrane lipid structure on plasma membrane ca2+-atpase activity
    • Tang, D., Dean, W. L., Borchman, D. & Paterson, C. A. (2006) The influence of membrane lipid structure on plasma membrane ca2+-atpase activity. Cell Calcium 39, 209-216.
    • (2006) Cell Calcium , vol.39 , pp. 209-216
    • Tang, D.1    Dean, W.L.2    Borchman, D.3    Paterson, C.A.4
  • 39
    • 35348837398 scopus 로고    scopus 로고
    • The lipid composition modulates the influence of the bovine seminal plasma protein pdc-109 on membrane stability
    • Tannert, A., Topfer-Petersen, E., Herrmann, A., Muller, K. & Muller, P. (2007) The lipid composition modulates the influence of the bovine seminal plasma protein pdc-109 on membrane stability. Biochemistry 46, 11621-11629.
    • (2007) Biochemistry , vol.46 , pp. 11621-11629
    • Tannert, A.1    Topfer-Petersen, E.2    Herrmann, A.3    Muller, K.4    Muller, P.5
  • 41
    • 0035894526 scopus 로고    scopus 로고
    • Expression and localization of caveolin-1, and the presence of membrane rafts, in mouse and guinea pig spermatozoa
    • Travis, A. J., Merdiushev, T., Vargas, L. A., Jones, B. H., Purdon, M. A., Nipper, R. W. et al. (2001) Expression and localization of caveolin-1, and the presence of membrane rafts, in mouse and guinea pig spermatozoa. Developmental Biology 240, 599-610.
    • (2001) Developmental Biology , vol.240 , pp. 599-610
    • Travis, A.J.1    Merdiushev, T.2    Vargas, L.A.3    Jones, B.H.4    Purdon, M.A.5    Nipper, R.W.6
  • 42
    • 0035976822 scopus 로고    scopus 로고
    • Identification of mouse trp homologs and lipid rafts from spermatogenic cells and sperm
    • Trevino, C. L., Serrano, C. J., Beltran, C., Felix, R. & Darszon, A. (2001) Identification of mouse trp homologs and lipid rafts from spermatogenic cells and sperm. FEBS Letters 509, 119-125.
    • (2001) FEBS Letters , vol.509 , pp. 119-125
    • Trevino, C.L.1    Serrano, C.J.2    Beltran, C.3    Felix, R.4    Darszon, A.5
  • 44
    • 0033570112 scopus 로고    scopus 로고
    • Cholesterol efflux-mediated signal transduction in mammalian sperm: Cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation
    • Visconti, P. E., Ning, X., Fornes, M. W., Alvarez, J. G., Stein, P., Connors, S. A. & Kopf, G. S. (1999) Cholesterol efflux-mediated signal transduction in mammalian sperm: Cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation. Developmental Biology 214, 429-443.
    • (1999) Developmental Biology , vol.214 , pp. 429-443
    • Visconti, P.E.1    Ning, X.2    Fornes, M.W.3    Alvarez, J.G.4    Stein, P.5    Connors, S.A.6    Kopf, G.S.7
  • 47
    • 0031793885 scopus 로고    scopus 로고
    • Regionalized lipid diffusion in the plasma membrane of mammalian spermatozoa
    • Wolfe, C. A., James, P. S., Mackie, A. R., Ladha, S. & Jones, R. (1998) Regionalized lipid diffusion in the plasma membrane of mammalian spermatozoa. Biological Reproduction 59, 1506-1514.
    • (1998) Biological Reproduction , vol.59 , pp. 1506-1514
    • Wolfe, C.A.1    James, P.S.2    Mackie, A.R.3    Ladha, S.4    Jones, R.5
  • 48
    • 58549084350 scopus 로고    scopus 로고
    • Phosphatidylserine externalization in caveolae inhibits Ca2+ efflux through plasma membrane Ca2+-atpase in ecv304
    • Zhang, J., Xiao, P. & Zhang, X. (2009) Phosphatidylserine externalization in caveolae inhibits Ca2+ efflux through plasma membrane Ca2+-atpase in ecv304. Cell Calcium 45, 177-184.
    • (2009) Cell Calcium , vol.45 , pp. 177-184
    • Zhang, J.1    Xiao, P.2    Zhang, X.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.