메뉴 건너뛰기




Volumn 119, Issue 3, 2003, Pages 179-187

Evidence for the capacitation-associated membrane priming of mouse spermatozoa

Author keywords

Acid glycohydrolases; Acrosome reaction; Mammalian fertilization; Mammalian spermatozoa; Sperm capacitation; Sperm priming

Indexed keywords

CALCIUM; CALCIUM BINDING PROTEIN; CALMODULIN; GLYCOSIDASE;

EID: 0037363251     PISSN: 09486143     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00418-003-0504-9     Document Type: Article
Times cited : (21)

References (40)
  • 1
    • 0034661419 scopus 로고    scopus 로고
    • Mammalian sperm acrosome: Formation, contents and function
    • Abou-Haila A, Tulsiani DRP (2000) Mammalian sperm acrosome: formation, contents and function. Arch Biochem Biophys 379:173-182
    • (2000) Arch Biochem Biophys , vol.379 , pp. 173-182
    • Abou-Haila, A.1    Tulsiani, D.R.P.2
  • 2
    • 0344631632 scopus 로고    scopus 로고
    • Characterization and immunolocalization of β-d-glucuronidase in mouse testicular germ cells and spermatozoa
    • Abou-Haila A, Fouquet J-P, Tulsiani DRP (1999) Characterization and immunolocalization of β-d-glucuronidase in mouse testicular germ cells and spermatozoa. Exp Cell Res 247:48-60
    • (1999) Exp Cell Res , vol.247 , pp. 48-60
    • Abou-Haila, A.1    Fouquet, J.-P.2    Tulsiani, D.R.P.3
  • 3
  • 4
    • 76949114656 scopus 로고
    • Observations on the penetration of the sperm into mammalian egg
    • Austin CR (1951) Observations on the penetration of the sperm into mammalian egg. Aust J Sci Res 4:581-596
    • (1951) Aust J Sci Res , vol.4 , pp. 581-596
    • Austin, C.R.1
  • 5
    • 0035370448 scopus 로고    scopus 로고
    • Calmodulin signals capacitation and triggers the agonists-induced acrosome reaction in mouse spermatozoa
    • Bendahmane M, Lynch C, Tulsiani DRP (2001) Calmodulin signals capacitation and triggers the agonists-induced acrosome reaction in mouse spermatozoa. Arch Biochem Biophys 390:1-8
    • (2001) Arch Biochem Biophys , vol.390 , pp. 1-8
    • Bendahmane, M.1    Lynch, C.2    Tulsiani, D.R.P.3
  • 6
    • 0027756146 scopus 로고
    • Head-specific mannose-ligand receptor expression in human spermatozoa is dependent on capacitation-associated membrane cholesterol loss
    • Benoff S, Hurley I, Cooper GW, Mandel FS, Rosenfeld DL, Hershlag A (1993) Head-specific mannose-ligand receptor expression in human spermatozoa is dependent on capacitation-associated membrane cholesterol loss. Hum Reprod 8:12141-12154
    • (1993) Hum Reprod , vol.8 , pp. 12141-12154
    • Benoff, S.1    Hurley, I.2    Cooper, G.W.3    Mandel, F.S.4    Rosenfeld, D.L.5    Hershlag, A.6
  • 8
    • 0030051050 scopus 로고    scopus 로고
    • Synaptic vesicle biogenesis, docking and fusion: A molecular description
    • Calakos N, Scheller B (1996) Synaptic vesicle biogenesis, docking and fusion: a molecular description. Physiol Rev 76:1-29
    • (1996) Physiol Rev , vol.76 , pp. 1-29
    • Calakos, N.1    Scheller, B.2
  • 9
    • 0001274348 scopus 로고
    • Fertilizing capacity of spermatozoa deposited in fallopian tubes
    • Chang A (1951) Fertilizing capacity of spermatozoa deposited in fallopian tubes. Nature 168:997-998
    • (1951) Nature , vol.168 , pp. 997-998
    • Chang, A.1
  • 10
    • 0033838536 scopus 로고    scopus 로고
    • Biosynthesis, processing and subcellular localization of rat sperm β-d-galactosidase
    • Chayko CA, Orgebin-Crist M-C, Skudlarek MD, Tulsiani DR (2000) Biosynthesis, processing and subcellular localization of rat sperm β-d-galactosidase. Biol Reprod 63:688-696
    • (2000) Biol Reprod , vol.63 , pp. 688-696
    • Chayko, C.A.1    Orgebin-Crist, M.-C.2    Skudlarek, M.D.3    Tulsiani, D.R.4
  • 11
    • 0031776647 scopus 로고    scopus 로고
    • Role of cholesterol in sperm capacitation
    • Cross NL (1998) Role of cholesterol in sperm capacitation. Biol Reprod 59:7-11
    • (1998) Biol Reprod , vol.59 , pp. 7-11
    • Cross, N.L.1
  • 12
    • 0024383609 scopus 로고
    • Direct contact is required between serum albumin and hamster spermatozoa for capacitation in vitro
    • Dow MP, Bavister BD (1989) Direct contact is required between serum albumin and hamster spermatozoa for capacitation in vitro. Gamete Res 23:171-180
    • (1989) Gamete Res , vol.23 , pp. 171-180
    • Dow, M.P.1    Bavister, B.D.2
  • 13
    • 0025249857 scopus 로고
    • Characterization of a decapacitation factor associated with epididymal mouse spermatozoa
    • Fraser LR, Harrison RAP, Herod JE (1990) Characterization of a decapacitation factor associated with epididymal mouse spermatozoa. J Reprod Fertil 89:135-148
    • (1990) J Reprod Fertil , vol.89 , pp. 135-148
    • Fraser, L.R.1    Harrison, R.A.P.2    Herod, J.E.3
  • 14
    • 0036082781 scopus 로고    scopus 로고
    • Capacitation induces cyclic adenosine 3′, 5′-monophosphate-dependent, but apoptosis-unrelated exposure of aminophospholipids at the apical head plasma membrane of boar sperm cells
    • Gadella BM, Harrison RAP (2002) Capacitation induces cyclic adenosine 3′, 5′-monophosphate-dependent, but apoptosis-unrelated exposure of aminophospholipids at the apical head plasma membrane of boar sperm cells. Biol Reprod 67:340-350
    • (2002) Biol Reprod , vol.67 , pp. 340-350
    • Gadella, B.M.1    Harrison, R.A.P.2
  • 15
    • 0023258569 scopus 로고
    • Calmodulin-mediated adenylate cyclase from mammalian sperm
    • Gross MK, Toscano DG, Toscano WA (1987) Calmodulin-mediated adenylate cyclase from mammalian sperm. J Biol Chem 262:8672-8676
    • (1987) J Biol Chem , vol.262 , pp. 8672-8676
    • Gross, M.K.1    Toscano, D.G.2    Toscano, W.A.3
  • 16
    • 0033168842 scopus 로고    scopus 로고
    • Identification of Rab3A GTPase as an acrosome-associated small GTP-binding protein in rat sperm
    • Ida H, Yoshinaga Y, Tanaka S, Toshimori K, Mori T (1999) Identification of Rab3A GTPase as an acrosome-associated small GTP-binding protein in rat sperm. Dev Biol 211:144-155
    • (1999) Dev Biol , vol.211 , pp. 144-155
    • Ida, H.1    Yoshinaga, Y.2    Tanaka, S.3    Toshimori, K.4    Mori, T.5
  • 18
    • 0025834043 scopus 로고
    • Localization of calmodulin in perinuclear structures of spermatids and spermatozoa: A comparison of six mammalian species
    • Kahn M-L, Feinberg J, Rainteau D, Dadoune JP, Weinman S, Fouquet J-P (1991) Localization of calmodulin in perinuclear structures of spermatids and spermatozoa: a comparison of six mammalian species. Anat Rec 230:481-488
    • (1991) Anat Rec , vol.230 , pp. 481-488
    • Kahn, M.-L.1    Feinberg, J.2    Rainteau, D.3    Dadoune, J.P.4    Weinman, S.5    Fouquet, J.-P.6
  • 19
    • 0021251345 scopus 로고
    • Characterization of a calmodulin stimulated adenylate cyclase from abalone spermatozoa
    • Kopf GS, Vacquier VD (1984) Characterization of a calmodulin stimulated adenylate cyclase from abalone spermatozoa. J Biol Chem 259:7590-7596
    • (1984) J Biol Chem , vol.259 , pp. 7590-7596
    • Kopf, G.S.1    Vacquier, V.D.2
  • 20
    • 0033061672 scopus 로고    scopus 로고
    • Simple histochemical stain for acrosomes on sperm from several species
    • Larson JL, Miller DJ (1999) Simple histochemical stain for acrosomes on sperm from several species. Mol Reprod Dev 52:445-449
    • (1999) Mol Reprod Dev , vol.52 , pp. 445-449
    • Larson, J.L.1    Miller, D.J.2
  • 21
    • 0032941207 scopus 로고    scopus 로고
    • The role of carbohydrates in the reduction of the acrosome reaction in mouse spermatozoa
    • Loeser CR, Tulsiani DRP (1999) The role of carbohydrates in the reduction of the acrosome reaction in mouse spermatozoa. Biol Reprod 60:94-101
    • (1999) Biol Reprod , vol.60 , pp. 94-101
    • Loeser, C.R.1    Tulsiani, D.R.P.2
  • 22
    • 0032766878 scopus 로고    scopus 로고
    • A plasma membrane-associated hyaluronidase is localized to the posterior acrosomal region of stallion sperm and is associated with spermatozoal function
    • Meyers SA, Rosenberger AE (1999) A plasma membrane-associated hyaluronidase is localized to the posterior acrosomal region of stallion sperm and is associated with spermatozoal function. Biol Reprod 61:444-451
    • (1999) Biol Reprod , vol.61 , pp. 444-451
    • Meyers, S.A.1    Rosenberger, A.E.2
  • 23
    • 0027096398 scopus 로고
    • The exocytotic fusion pore
    • Monck JR, Fernandez JM (1992) The exocytotic fusion pore. J Cell Biol 119:1395-1404
    • (1992) J Cell Biol , vol.119 , pp. 1395-1404
    • Monck, J.R.1    Fernandez, J.M.2
  • 24
    • 0027464973 scopus 로고
    • Immunoelectron microscopic localization of calmodulin and calmodulin-binding proteins in the mouse germ cells during spermatogenesis and maturation
    • Moriya M, Katagiri C, Yagi K (1993) Immunoelectron microscopic localization of calmodulin and calmodulin-binding proteins in the mouse germ cells during spermatogenesis and maturation. Cell Tissue Res 271:441-451
    • (1993) Cell Tissue Res , vol.271 , pp. 441-451
    • Moriya, M.1    Katagiri, C.2    Yagi, K.3
  • 25
    • 0036470112 scopus 로고    scopus 로고
    • The Vtc proteins in vacuole fusion: Coupling NSF activity to Vo trans-complex formation
    • Müller O, Bayer MJ, Peters C, Anderson JS, Mann M, Mayer A (2002) The Vtc proteins in vacuole fusion: coupling NSF activity to Vo trans-complex formation. EMBO J 21:259-269
    • (2002) EMBO J , vol.21 , pp. 259-269
    • Müller, O.1    Bayer, M.J.2    Peters, C.3    Anderson, J.S.4    Mann, M.5    Mayer, A.6
  • 27
    • 0018502644 scopus 로고
    • Mouse gamete interaction during fertilization in vitro: Chlorotetracycline as a fluorescent probe for the mouse sperm acrosome reaction
    • Saling PM, Storey BT (1979) Mouse gamete interaction during fertilization in vitro: chlorotetracycline as a fluorescent probe for the mouse sperm acrosome reaction. J Exp Zool 209:229-238
    • (1979) J Exp Zool , vol.209 , pp. 229-238
    • Saling, P.M.1    Storey, B.T.2
  • 29
    • 0034715944 scopus 로고    scopus 로고
    • Rat spermatogenic cell β-d-galactosidase: Characterization, biosynthesis, and immunolocalization
    • Skudlarek MD, Abou-Haila A, Tulsiani DRP (2000) Rat spermatogenic cell β-d-galactosidase: characterization, biosynthesis, and immunolocalization. Exp Cell Res 261:139-149
    • (2000) Exp Cell Res , vol.261 , pp. 139-149
    • Skudlarek, M.D.1    Abou-Haila, A.2    Tulsiani, D.R.P.3
  • 30
    • 0026655990 scopus 로고
    • A cell free system reveals that capacitation is a prerequisite for membrane fusion during the acrosome reaction
    • Spungin B, Levinshal T, Rubinstein S, Breibart H (1992) A cell free system reveals that capacitation is a prerequisite for membrane fusion during the acrosome reaction. FEBS Lett 311:155-160
    • (1992) FEBS Lett , vol.311 , pp. 155-160
    • Spungin, B.1    Levinshal, T.2    Rubinstein, S.3    Breibart, H.4
  • 31
    • 0025114177 scopus 로고
    • Acrosin activation follows its surface exposure and precedes membrane fusion in human sperm acrosome reaction
    • Tesarik J, Drahorad J, Testart J, Mendoza C (1990) Acrosin activation follows its surface exposure and precedes membrane fusion in human sperm acrosome reaction. Development 110:391-400
    • (1990) Development , vol.110 , pp. 391-400
    • Tesarik, J.1    Drahorad, J.2    Testart, J.3    Mendoza, C.4
  • 32
    • 0035260708 scopus 로고    scopus 로고
    • Mammalian sperm molecules that are potentially important in interaction with female genital tract and egg vestments
    • Tulsiani DRP, Abou-Haila A (2001) Mammalian sperm molecules that are potentially important in interaction with female genital tract and egg vestments. Zygote 9:51-69
    • (2001) Zygote , vol.9 , pp. 51-69
    • Tulsiani, D.R.P.1    Abou-Haila, A.2
  • 33
    • 0030872253 scopus 로고    scopus 로고
    • Mammalian fertilization: A carbohydrate-mediated event
    • Tulsiani DRP, Yoshida-Komiya H, Araki Y (1997) Mammalian fertilization: a carbohydrate-mediated event. Biol Reprod 57:487-494
    • (1997) Biol Reprod , vol.57 , pp. 487-494
    • Tulsiani, D.R.P.1    Yoshida-Komiya, H.2    Araki, Y.3
  • 34
    • 0031826659 scopus 로고    scopus 로고
    • The biological and functional significance of the sperm acrosome and acrosomal enzymes in mammalian fertilization
    • Tulsiani DRP, Abou-Haila A, Loeser CR, Pereira BM (1998) The biological and functional significance of the sperm acrosome and acrosomal enzymes in mammalian fertilization. Exp Cell Res 240:151-164
    • (1998) Exp Cell Res , vol.240 , pp. 151-164
    • Tulsiani, D.R.P.1    Abou-Haila, A.2    Loeser, C.R.3    Pereira, B.M.4
  • 35
    • 0031778295 scopus 로고    scopus 로고
    • Regulation of protein phosphorylation during capacitation
    • Visconti PE, Kopf GS (1998) Regulation of protein phosphorylation during capacitation. Biol Reprod 59:1-6
    • (1998) Biol Reprod , vol.59 , pp. 1-6
    • Visconti, P.E.1    Kopf, G.S.2
  • 36
    • 0021160724 scopus 로고
    • Determination of the time course of capacitation in mouse spermatozoa using chlortetracycline fluorescence assay
    • Ward CR, Storey B (1984) Determination of the time course of capacitation in mouse spermatozoa using chlortetracycline fluorescence assay. Dev Biol 104:287-296
    • (1984) Dev Biol , vol.104 , pp. 287-296
    • Ward, C.R.1    Storey, B.2
  • 37
    • 0032990170 scopus 로고    scopus 로고
    • The monomeric GTP binding protein, rab3, is associated with the acrosome in mouse sperm
    • Ward CR, Faundes D, Foster JA (1999) The monomeric GTP binding protein, rab3, is associated with the acrosome in mouse sperm. Mol Reprod Dev 53:413-421
    • (1999) Mol Reprod Dev , vol.53 , pp. 413-421
    • Ward, C.R.1    Faundes, D.2    Foster, J.A.3
  • 38
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil E, Neil JD (eds). Raven, New York
    • Yanagimachi R (1994) Mammalian fertilization. In: Knobil E, Neil JD (eds) Physiology of reproduction. Raven, New York, pp 189-317
    • (1994) Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 39
    • 0037077705 scopus 로고    scopus 로고
    • Rab3A and calmodulin regulate acrosomal exocytosis by mechanisms that do not require a direct interaction
    • Yunes R, Tomas C, Michaut M, De Blas G, Rodriguez F, Regazzi R, Mayorga LS (2002) Rab3A and calmodulin regulate acrosomal exocytosis by mechanisms that do not require a direct interaction. FEBS Lett 525:126-130
    • (2002) FEBS Lett , vol.525 , pp. 126-130
    • Yunes, R.1    Tomas, C.2    Michaut, M.3    De Blas, G.4    Rodriguez, F.5    Regazzi, R.6    Mayorga, L.S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.