메뉴 건너뛰기




Volumn 28, Issue SUPPL. 3, 2010, Pages 1886-1894

Differential involvement of rat sperm choline glycerophospholipids and sphingomyelin in capacitation and the acrosomal reaction

Author keywords

Acrosome reaction; Capacitation; Ceramides; Cholesterol; Glycerophospholipids; Sphingomyelins

Indexed keywords

CHOLESTEROL; CYCLIC AMP DEPENDENT PROTEIN KINASE; FATTY ACID; PHOSPHATIDYLCHOLINE; SPHINGOMYELIN; VERY LONG CHAIN FATTY ACID; CALCIUM IONOPHORE; CERAMIDE; DIACYLGLYCEROL; LYSOPHOSPHATIDYLCHOLINE; POLYENE FATTY ACID; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

EID: 78649886156     PISSN: 0213005X     EISSN: 15781852     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.08.015     Document Type: Article
Times cited : (18)

References (49)
  • 1
    • 0003178422 scopus 로고
    • The capacitation of mammalian sperm
    • C. Austin The capacitation of mammalian sperm Nature 170 1952 326
    • (1952) Nature , vol.170 , pp. 326
    • Austin, C.1
  • 2
    • 36949091315 scopus 로고
    • Fertilizing capacity of spermatozoa deposited into the fallopian tubes
    • M.C. Chang Fertilizing capacity of spermatozoa deposited into the fallopian tubes Nature 168 1951 697 698
    • (1951) Nature , vol.168 , pp. 697-698
    • Chang, M.C.1
  • 3
    • 59949089652 scopus 로고    scopus 로고
    • Germ cell research: A personal perspective
    • R. Yanagimachi Germ cell research: a personal perspective Biol. Reprod. 80 2009 204 218
    • (2009) Biol. Reprod. , vol.80 , pp. 204-218
    • Yanagimachi, R.1
  • 5
    • 79961199040 scopus 로고    scopus 로고
    • Current concepts of molecular events during bovine and porcine spermatozoa capacitation
    • M.L. Vadnais, H.L. Galantino-Homer, and G.C. Althouse Current concepts of molecular events during bovine and porcine spermatozoa capacitation Arch. Androl. 53 2007 109 123
    • (2007) Arch. Androl. , vol.53 , pp. 109-123
    • Vadnais, M.L.1    Galantino-Homer, H.L.2    Althouse, G.C.3
  • 6
    • 0028985057 scopus 로고
    • 2 is not required for zona pellucida- or progesterone-induced acrosomal exocytosis of mouse spermatozoa but is essential for capacitation
    • 2 is not required for zona pellucida- or progesterone-induced acrosomal exocytosis of mouse spermatozoa but is essential for capacitation Biol. Reprod. 52 1995 540 546
    • (1995) Biol. Reprod. , vol.52 , pp. 540-546
    • Shi, Q.X.1    Roldan, E.R.2
  • 7
    • 0028957362 scopus 로고
    • Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation
    • P.E. Visconti, J.L. Bailey, G.D. Moore, D. Pan, P. Olds-Clarke, and G.S. Kopf Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation Development 121 1995 1129 1137
    • (1995) Development , vol.121 , pp. 1129-1137
    • Visconti, P.E.1    Bailey, J.L.2    Moore, G.D.3    Pan, D.4    Olds-Clarke, P.5    Kopf, G.S.6
  • 8
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • P.E. Visconti, G.D. Moore, J.L. Bailey, P. Leclerc, S.A. Connors, D. Pan, P. Olds-Clarke, and G.S. Kopf 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
  • 9
    • 0031776647 scopus 로고    scopus 로고
    • Role of cholesterol in sperm capacitation
    • N.L. Cross Role of cholesterol in sperm capacitation Biol. Reprod. 59 1998 7 11
    • (1998) Biol. Reprod. , vol.59 , pp. 7-11
    • Cross, N.L.1
  • 10
    • 0036740048 scopus 로고    scopus 로고
    • The role of cholesterol efflux in regulating the fertilization potential of mammalian spermatozoa
    • A.J. Travis, and G.S. Kopf The role of cholesterol efflux in regulating the fertilization potential of mammalian spermatozoa J. Clin. Invest. 110 2002 731 736
    • (2002) J. Clin. Invest. , vol.110 , pp. 731-736
    • Travis, A.J.1    Kopf, G.S.2
  • 11
    • 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
    • DOI 10.1006/dbio.1999.9428
    • P.E. Visconti, X. Ning, M.W. Fornes, J.G. Alvarez, P. Stein, S.A. Connors, and G.S. Kopf Cholesterol efflux-mediated signal transduction in mammalian sperm: cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation Dev. Biol. 214 1999 429 443 (Pubitemid 29483103)
    • (1999) Developmental Biology , vol.214 , Issue.2 , 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
  • 12
    • 0033613867 scopus 로고    scopus 로고
    • Cholesterol efflux-mediated signal transduction in mammalian sperm: β- Cyclodextrins initiate transmembrane signaling leading to an increase in protein tyrosine phosphorylation and capacitation
    • DOI 10.1074/jbc.274.5.3235
    • P.E. Visconti, H. Galantino-Homer, X. Ning, G.D. Moore, J.P. Valenzuela, C.J. Jorgez, J.G. Alvarez, and G.S. Kopf Cholesterol efflux-mediated signal transduction in mammalian sperm. Beta-cyclodextrins initiate transmembrane signaling leading to an increase in protein tyrosine phosphorylation and capacitation J. Biol. Chem. 274 1999 3235 3242 (Pubitemid 29075414)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.5 , pp. 3235-3242
    • Visconti, P.E.1    Galantino-Homer, H.2    Ning, X.3    Moore, G.D.4    Valenzuela, J.P.5    Jorgez, C.J.6    Alvarez, J.G.7    Kopf, G.S.8
  • 14
    • 0037150651 scopus 로고    scopus 로고
    • Penetration, adhesion, and fusion in mammalian sperm-egg interaction
    • P. Primakoff, and D.G. Myles Penetration, adhesion, and fusion in mammalian sperm-egg interaction Science 296 2002 2183 2185
    • (2002) Science , vol.296 , pp. 2183-2185
    • Primakoff, P.1    Myles, D.G.2
  • 15
    • 0028650360 scopus 로고
    • Exocytosis in spermatozoa in response to progesterone and zona pellucida
    • E.R. Roldan, T. Murase, and Q.X. Shi Exocytosis in spermatozoa in response to progesterone and zona pellucida Science 266 1994 1578 1581
    • (1994) Science , vol.266 , pp. 1578-1581
    • Roldan, E.R.1    Murase, T.2    Shi, Q.X.3
  • 16
    • 0030810986 scopus 로고    scopus 로고
    • Regulation of membrane stability and the acrosome reaction in mammalian sperm
    • J.P. Nolan, and R.H. Hammerstedt Regulation of membrane stability and the acrosome reaction in mammalian sperm FASEB J. 11 1997 670 682
    • (1997) FASEB J. , vol.11 , pp. 670-682
    • Nolan, J.P.1    Hammerstedt, R.H.2
  • 18
    • 68049126532 scopus 로고    scopus 로고
    • Acrosomal swelling and membrane docking are required for hybrid vesicle formation during the human sperm acrosome reaction
    • N. Zanetti, and L.S. Mayorga Acrosomal swelling and membrane docking are required for hybrid vesicle formation during the human sperm acrosome reaction Biol. Reprod. 81 2009 396 405
    • (2009) Biol. Reprod. , vol.81 , pp. 396-405
    • Zanetti, N.1    Mayorga, L.S.2
  • 19
    • 0026589486 scopus 로고
    • Lipid remodelling during epididymal maturation of rat spermatozoa. Enrichment in plasmenylcholines containing long-chain polyenoic fatty acids of the n-9 series
    • M.I. Aveldano, N.P. Rotstein, and N.T. Vermouth Lipid remodelling during epididymal maturation of rat spermatozoa. Enrichment in plasmenylcholines containing long-chain polyenoic fatty acids of the n-9 series Biochem. J. 283 Pt 1 1992 235 241
    • (1992) Biochem. J. , vol.283 , Issue.PART 1 , pp. 235-241
    • Aveldano, M.I.1    Rotstein, N.P.2    Vermouth, N.T.3
  • 20
    • 0026541438 scopus 로고
    • Novel molecular species of sphingomyelin containing 2-hydroxylated polyenoic very-long-chain fatty acids in mammalian testes and spermatozoa
    • B.S. Robinson, D.W. Johnson, and A. Poulos Novel molecular species of sphingomyelin containing 2-hydroxylated polyenoic very-long-chain fatty acids in mammalian testes and spermatozoa J. Biol. Chem. 267 1992 1746 1751
    • (1992) J. Biol. Chem. , vol.267 , pp. 1746-1751
    • Robinson, B.S.1    Johnson, D.W.2    Poulos, A.3
  • 21
    • 78649831016 scopus 로고    scopus 로고
    • Ceramides with 2-hydroxylated, very long chain polyenoic fatty acids in rodents: From testis to fertilization-competent spermatozoa
    • S.R. Zanetti, M.A. Monclus, D.E. Rensetti, M.W. Fornés, M.I. Aveldaño, Ceramides with 2-hydroxylated, very long chain polyenoic fatty acids in rodents: from testis to fertilization-competent spermaozoa, Biochimie 92 (2010) 1778-1786.
    • (2010) Biochimie , vol.92 , pp. 1778-1786
    • Zanetti, S.R.1
  • 23
    • 0036683808 scopus 로고    scopus 로고
    • Assessment of acrosomal status in rat spermatozoa: Studies on carbohydrate and non-carbohydrate agonists
    • M. Bendahmane, H.T. Zeng, and D.R. Tulsiani Assessment of acrosomal status in rat spermatozoa: studies on carbohydrate and non-carbohydrate agonists Arch. Biochem. Biophys. 404 2002 38 47
    • (2002) Arch. Biochem. Biophys. , vol.404 , pp. 38-47
    • Bendahmane, M.1    Zeng, H.T.2    Tulsiani, D.R.3
  • 24
    • 0026671640 scopus 로고
    • Distinction between true acrosome reaction and degenerative acrosome loss by a one-step staining method using Pisum sativum agglutinin
    • C. Mendoza, A. Carreras, J. Moos, and J. Tesarik Distinction between true acrosome reaction and degenerative acrosome loss by a one-step staining method using Pisum sativum agglutinin J. Reprod. Fertil. 95 1992 755 763
    • (1992) J. Reprod. Fertil. , vol.95 , pp. 755-763
    • Mendoza, C.1    Carreras, A.2    Moos, J.3    Tesarik, J.4
  • 25
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • E.G. Bligh, and W.J. Dyer A rapid method of total lipid extraction and purification Can. J. Biochem. Physiol. 37 1959 911 917
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 26
    • 0014779155 scopus 로고
    • Two dimensional then layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
    • G. Rouser, S. Fkeischer, and A. Yamamoto Two dimensional then layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots Lipids 5 1970 494 496
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fkeischer, S.2    Yamamoto, A.3
  • 27
    • 0014279424 scopus 로고
    • Structural and metabolic heterogeneity of rat liver glycerophosphatides
    • G.A.E. Arvidson Structural and metabolic heterogeneity of rat liver glycerophosphatides Eur. J. Biochem. 4 1968 478 486
    • (1968) Eur. J. Biochem. , vol.4 , pp. 478-486
    • Arvidson, G.A.E.1
  • 28
    • 34547125599 scopus 로고    scopus 로고
    • Very long-chain polyunsaturated fatty acids are the major acyl groups of sphingomyelins and ceramides in the head of mammalian spermatozoa
    • N.E. Furland, G.M. Oresti, S.S. Antollini, A. Venturino, E.N. Maldonado, and M.I. Aveldano Very long-chain polyunsaturated fatty acids are the major acyl groups of sphingomyelins and ceramides in the head of mammalian spermatozoa J. Biol. Chem. 282 2007 18151 18161
    • (2007) J. Biol. Chem. , vol.282 , pp. 18151-18161
    • Furland, N.E.1    Oresti, G.M.2    Antollini, S.S.3    Venturino, A.4    Maldonado, E.N.5    Aveldano, M.I.6
  • 29
    • 0345169713 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of HSP-90 during mammalian sperm capacitation
    • H. Ecroyd, R.C. Jones, and R.J. Aitken Tyrosine phosphorylation of HSP-90 during mammalian sperm capacitation Biol. Reprod. 69 2003 1801 1807
    • (2003) Biol. Reprod. , vol.69 , pp. 1801-1807
    • Ecroyd, H.1    Jones, R.C.2    Aitken, R.J.3
  • 30
    • 0031049037 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphorylation during bovine sperm capacitation by a cyclic adenosine 3′5′-monophosphate-dependent pathway
    • H.L. Galantino-Homer, P.E. Visconti, and G.S. Kopf 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
  • 31
    • 77956816358 scopus 로고    scopus 로고
    • Differentiation-related changes in lipid classes with long-chain and very long-chain polyenoic fatty acids in rat spermatogenic cells
    • G.M. Oresti, J.G. Reyes, J.M. Luquez, N. Osses, N.E. Furland, and M.I. Aveldano Differentiation-related changes in lipid classes with long-chain and very long-chain polyenoic fatty acids in rat spermatogenic cells J. Lipid Res. 51 2010 2909 2921
    • (2010) J. Lipid Res. , vol.51 , pp. 2909-2921
    • Oresti, G.M.1    Reyes, J.G.2    Luquez, J.M.3    Osses, N.4    Furland, N.E.5    Aveldano, M.I.6
  • 32
    • 0037285863 scopus 로고    scopus 로고
    • Protein phosphorylation in mammalian spermatozoa
    • F. Urner, and D. Sakkas Protein phosphorylation in mammalian spermatozoa Reproduction 125 2003 17 26
    • (2003) Reproduction , vol.125 , pp. 17-26
    • Urner, F.1    Sakkas, D.2
  • 33
    • 0030569051 scopus 로고    scopus 로고
    • 2 induces rapid activation of phospholipase A2 and renders boar spermatozoa capable of undergoing acrosomal exocytosis in response to progesterone
    • 2 induces rapid activation of phospholipase A2 and renders boar spermatozoa capable of undergoing acrosomal exocytosis in response to progesterone FEBS Lett. 396 1996 227 232
    • (1996) FEBS Lett. , vol.396 , pp. 227-232
    • Roldan, E.R.1    Vazquez, J.M.2
  • 34
    • 0034759226 scopus 로고    scopus 로고
    • Bicarbonate stimulated phospholipid scrambling induces cholesterol redistribution and enables cholesterol depletion in the sperm plasma membrane
    • F.M. Flesch, J.F. Brouwers, P.F. Nievelstein, A.J. Verkleij, L.M. van Golde, B. Colenbrander, and B.M. Gadella Bicarbonate stimulated phospholipid scrambling induces cholesterol redistribution and enables cholesterol depletion in the sperm plasma membrane J. Cell Sci. 114 2001 3543 3555
    • (2001) J. Cell Sci. , vol.114 , pp. 3543-3555
    • Flesch, F.M.1    Brouwers, J.F.2    Nievelstein, P.F.3    Verkleij, A.J.4    Van Golde, L.M.5    Colenbrander, B.6    Gadella, B.M.7
  • 35
    • 0034083188 scopus 로고    scopus 로고
    • The capacitating agent bicarbonate induces protein kinase A-dependent changes in phospholipid transbilayer behavior in the sperm plasma membrane
    • B.M. Gadella, and R.A. Harrison The capacitating agent bicarbonate induces protein kinase A-dependent changes in phospholipid transbilayer behavior in the sperm plasma membrane Development 127 2000 2407 2420
    • (2000) Development , vol.127 , pp. 2407-2420
    • Gadella, B.M.1    Harrison, R.A.2
  • 36
    • 0023774245 scopus 로고
    • Identification of sterol acceptors that stimulate cholesterol efflux from human spermatozoa during in vitro capacitation
    • J. Langlais, F.W. Kan, L. Granger, L. Raymond, G. Bleau, and K.D. Roberts Identification of sterol acceptors that stimulate cholesterol efflux from human spermatozoa during in vitro capacitation Gamete Res. 20 1988 185 201
    • (1988) Gamete Res. , vol.20 , pp. 185-201
    • Langlais, J.1    Kan, F.W.2    Granger, L.3    Raymond, L.4    Bleau, G.5    Roberts, K.D.6
  • 37
    • 34249816501 scopus 로고    scopus 로고
    • Sperm phospholipases and acrosomal exocytosis
    • E.R. Roldan, and Q.X. Shi Sperm phospholipases and acrosomal exocytosis Front Biosci. 12 2007 89 104
    • (2007) Front Biosci. , vol.12 , pp. 89-104
    • Roldan, E.R.1    Shi, Q.X.2
  • 38
    • 0027936037 scopus 로고
    • Polyphosphoinositide-derived diacylglycerol stimulates the hydrolysis of phosphatidylcholine by phospholipase C during exocytosis of the ram sperm acrosome. Effect is not mediated by protein kinase C
    • E.R. Roldan, and T. Murase Polyphosphoinositide-derived diacylglycerol stimulates the hydrolysis of phosphatidylcholine by phospholipase C during exocytosis of the ram sperm acrosome. Effect is not mediated by protein kinase C J. Biol. Chem. 269 1994 23583 23589
    • (1994) J. Biol. Chem. , vol.269 , pp. 23583-23589
    • Roldan, E.R.1    Murase, T.2
  • 40
    • 70350704734 scopus 로고    scopus 로고
    • Removal of acrosomal membrane from sperm head improves development of rat zygotes derived from intracytoplasmic sperm injection
    • Y. Seita, J. Ito, and N. Kashiwazaki Removal of acrosomal membrane from sperm head improves development of rat zygotes derived from intracytoplasmic sperm injection J. Reprod. Dev. 55 2009 475 479
    • (2009) J. Reprod. Dev. , vol.55 , pp. 475-479
    • Seita, Y.1    Ito, J.2    Kashiwazaki, N.3
  • 42
  • 43
    • 0033806720 scopus 로고    scopus 로고
    • Sphingomyelin modulates capacitation of human sperm in vitro
    • N.L. Cross Sphingomyelin modulates capacitation of human sperm in vitro Biol. Reprod. 63 2000 1129 1134
    • (2000) Biol. Reprod. , vol.63 , pp. 1129-1134
    • Cross, N.L.1
  • 44
    • 18244398637 scopus 로고    scopus 로고
    • Ceramide enhances acrosomal exocytosis triggered by calcium and the calcium ionophore A23187 in boar spermatozoa
    • T. Murase, N. Imaeda, N. Kondoh, and T. Tsubota Ceramide enhances acrosomal exocytosis triggered by calcium and the calcium ionophore A23187 in boar spermatozoa J. Reprod. Dev. 50 2004 667 674
    • (2004) J. Reprod. Dev. , vol.50 , pp. 667-674
    • Murase, T.1    Imaeda, N.2    Kondoh, N.3    Tsubota, T.4
  • 45
    • 33646179776 scopus 로고    scopus 로고
    • Detergent-resistant, ceramide-enriched domains in sphingomyelin/ceramide bilayers
    • J. Sot, L.A. Bagatolli, F.M. Goni, and A. Alonso Detergent-resistant, ceramide-enriched domains in sphingomyelin/ceramide bilayers Biophys. J. 90 2006 903 914
    • (2006) Biophys. J. , vol.90 , pp. 903-914
    • Sot, J.1    Bagatolli, L.A.2    Goni, F.M.3    Alonso, A.4
  • 46
    • 0031056802 scopus 로고    scopus 로고
    • Protein kinase C isoforms undergo quantitative variations during rat spermatogenesis and are selectively retained at specific spermatozoon sites
    • N. Zini, A. Matteucci, P. Sabatelli, A. Valmori, E. Caramelli, and N.M. Maraldi Protein kinase C isoforms undergo quantitative variations during rat spermatogenesis and are selectively retained at specific spermatozoon sites Eur. J. Cell Biol. 72 1997 142 150
    • (1997) Eur. J. Cell Biol. , vol.72 , pp. 142-150
    • Zini, N.1    Matteucci, A.2    Sabatelli, P.3    Valmori, A.4    Caramelli, E.5    Maraldi, N.M.6
  • 47
    • 0029069765 scopus 로고
    • Ceramide triggers meiotic cell cycle progression in Xenopus oocytes. A potential mediator of progesterone-induced maturation
    • J.C. Strum, K.I. Swenson, J.E. Turner, and R.M. Bell Ceramide triggers meiotic cell cycle progression in Xenopus oocytes. A potential mediator of progesterone-induced maturation J. Biol. Chem. 270 1995 13541 13547
    • (1995) J. Biol. Chem. , vol.270 , pp. 13541-13547
    • Strum, J.C.1    Swenson, K.I.2    Turner, J.E.3    Bell, R.M.4
  • 49
    • 26444531909 scopus 로고    scopus 로고
    • Incorporation of the acrosome into the oocyte during intracytoplasmic sperm injection could be potentially hazardous to embryo development
    • K. Morozumi, and R. Yanagimachi Incorporation of the acrosome into the oocyte during intracytoplasmic sperm injection could be potentially hazardous to embryo development Proc. Natl. Acad. Sci. U.S.A. 102 2005 14209 14214
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 14209-14214
    • Morozumi, K.1    Yanagimachi, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.