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Volumn 76, Issue 6, 2009, Pages 527-536

Purification and multimer formation of allurin, a sperm chemoattractant from Xenopus laevis egg jelly

Author keywords

[No Author keywords available]

Indexed keywords

ALLURIN; BINDING PROTEIN; CHEMOATTRACTANT; MERCAPTOETHANOL; THIOL GROUP; UNCLASSIFIED DRUG;

EID: 65949101224     PISSN: 1040452X     EISSN: 10982795     Source Type: Journal    
DOI: 10.1002/mrd.20969     Document Type: Article
Times cited : (10)

References (57)
  • 1
    • 0032526146 scopus 로고    scopus 로고
    • Xenopus laevis egg jelly releases a sperm chemoattractant during spawning
    • Al-Anzi B, Chandler D. 1998. Xenopus laevis egg jelly releases a sperm chemoattractant during spawning. Dev Biol 198:366-375.
    • (1998) Dev Biol , vol.198 , pp. 366-375
    • Al-Anzi, B.1    Chandler, D.2
  • 2
    • 13844275516 scopus 로고    scopus 로고
    • X-ray structure of Na-ASP-2, a pathogenesis-related-1 protein from the nematode parasite, Necator americanus, and a vaccine antigen for human hookworm infection
    • DOI 10.1016/j.jmb.2004.12.023
    • Asojo OA, Goud G, Dhar K, Loukas A, Zahn B, Deumic V, Lui S, Borgstahl GE, Hotez PJ. 2005. X-ray structure of Na-ASP-2, a pathogenesis-related protein from the nematode parasite, Necator americanus, and a vaccine antigen for human hookworm infection. J Mol Biol 346:801-814. (Pubitemid 40247719)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.3 , pp. 801-814
    • Asojo, O.A.1    Goud, G.2    Dhar, K.3    Loukas, A.4    Zhan, B.5    Deumic, V.6    Liu, S.7    Borgstahl, G.E.O.8    Hotez, P.J.9
  • 4
    • 41149164575 scopus 로고    scopus 로고
    • Xenopus tropicalis allurin: Expression, purification, and characterization of a sperm chemoattractant that exhibits cross-species activity
    • Burnett LA, Boyles S, Spencer C, Bieber AL, Chandler DE. 2008a. Xenopus tropicalis allurin: Expression, purification, and characterization of a sperm chemoattractant that exhibits cross-species activity. Dev Biol 316:408-416.
    • (2008) Dev Biol , vol.316 , pp. 408-416
    • Burnett, L.A.1    Boyles, S.2    Spencer, C.3    Bieber, A.L.4    Chandler, D.E.5
  • 5
    • 54249115958 scopus 로고    scopus 로고
    • Crisp proteins and sperm chemotaxis: Discovery in amphibians and explorations in mammals
    • Burnett LA, Xiang X, Bieber A, Chandler D. 2008b. Crisp proteins and sperm chemotaxis: Discovery in amphibians and explorations in mammals. Int J Dev Biol 52:489-501.
    • (2008) Int J Dev Biol , vol.52 , pp. 489-501
    • Burnett, L.A.1    Xiang, X.2    Bieber, A.3    Chandler, D.4
  • 6
    • 18644375388 scopus 로고    scopus 로고
    • Human testicular protein TPX1/CRISP-2: Localization in spermatozoa, fate after capacitation and relevance for gamete interaction
    • Busso D, Cohen DJ, Hayashi M, Kasahara M, Cuasnicu PS. 2005. Human testicular protein TPX1/CRISP-2: Localization in spermatozoa, fate after capacitation and relevance for gamete interaction. Mol Hum Reprod 11:299-305.
    • (2005) Mol Hum Reprod , vol.11 , pp. 299-305
    • Busso, D.1    Cohen, D.J.2    Hayashi, M.3    Kasahara, M.4    Cuasnicu, P.S.5
  • 7
    • 0026670417 scopus 로고
    • Mammalian sperm-egg fusion: The rat egg has complementary sites for a sperm protein that mediates gamete fusion
    • Cohen D, Munuce MJ, Cuasnicu PS. 1992. Mammalian sperm-egg fusion: The rat egg has complementary sites for a sperm protein that mediates gamete fusion. Dev Biol 153:83-90.
    • (1992) Dev Biol , vol.153 , pp. 83-90
    • Cohen, D.1    Munuce, M.J.2    Cuasnicu, P.S.3
  • 8
    • 0033870427 scopus 로고    scopus 로고
    • Mammalian sperm-egg fusion: Evidence that epididymal protein de plays a role in mouse gamete fusion
    • Cohen DJ, Ellerman DA, Cuasnicu PS. 2000. Mammalian sperm-egg fusion: Evidence that epididymal protein DE plays a role in mouse gamete fusion. Biol Reprod 63:462-468.
    • (2000) Biol Reprod , vol.63 , pp. 462-468
    • Cohen, D.J.1    Ellerman, D.A.2    Cuasnicu, P.S.3
  • 9
    • 34447290640 scopus 로고    scopus 로고
    • Participation of epididymal cysteine-rich secretory proteins in sperm-egg fusion and their potential use for male fertility regulation
    • Cohen DJ, Da Ros VG, Busso D, Ellerman DA, Maldera JA, Goldweic N, Cuasnicu PS. 2007. Participation of epididymal cysteine-rich secretory proteins in sperm-egg fusion and their potential use for male fertility regulation. Asian J Androl 9:528-532.
    • (2007) Asian J Androl , vol.9 , pp. 528-532
    • Cohen, D.J.1    Da Ros, V.G.2    Busso, D.3    Ellerman, D.A.4    Maldera, J.A.5    Goldweic, N.6    Cuasnicu, P.S.7
  • 10
    • 0028845356 scopus 로고
    • Sperm capacitation in humans is transient and correlates with chemotactic responsiveness to follicular factors
    • Cohen-Dayag A, Tur-Caspa I, Dor J, Mashiach S, Eisenbach M. 1995. Sperm capacitation in humans is transient and correlates with chemotactic responsiveness to follicular factors. Proc Natl Acad Sci USA 92:11039-11043.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11039-11043
    • Cohen-Dayag, A.1    Tur-Caspa, I.2    Dor, J.3    Mashiach, S.4    Eisenbach, M.5
  • 12
    • 0032817345 scopus 로고    scopus 로고
    • Mammalian sperm chemotaxis and its association with capacitation
    • Eisenbach M. 1999. Mammalian sperm chemotaxis and its association with capacitation. Dev Genet 25:87-94.
    • (1999) Dev Genet , vol.25 , pp. 87-94
    • Eisenbach, M.1
  • 13
    • 33645756342 scopus 로고    scopus 로고
    • Sperm guidance in mammals - An unpaved road to the egg
    • Eisenbach M, Giojalas L. 2006. Sperm guidance in mammals - An unpaved road to the egg. Nat Rev Mol Cell Biol 7:276-285.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 276-285
    • Eisenbach, M.1    Giojalas, L.2
  • 14
    • 33748061640 scopus 로고    scopus 로고
    • Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family
    • Ellerman DA, Cohen DJ, Da Ros VG, Morgenfeld MM, Busso D, Cuasnicu PS. 2006. Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family. Dev Biol 297:228-237.
    • (2006) Dev Biol , vol.297 , pp. 228-237
    • Ellerman, D.A.1    Cohen, D.J.2    Da Ros, V.G.3    Morgenfeld, M.M.4    Busso, D.5    Cuasnicu, P.S.6
  • 15
    • 85046913038 scopus 로고    scopus 로고
    • The state of the union: The cell biology of fertilization
    • Evans JP, Florman HM. 2002. The state of the union: The cell biology of fertilization. Nat Cell Biol 4:s57-s63.
    • (2002) Nat Cell Biol , vol.4
    • Evans, J.P.1    Florman, H.M.2
  • 17
    • 0029977253 scopus 로고    scopus 로고
    • Autoantigen 1 of the guinea pig sperm acrosome is the homologue of mouse Tpx-1 and human TPX1 and is a member of the cysteine-rich secretory protein (CRISP) family
    • Foster JA, Gerton GA. 1996. Autoantigen 1 of the guinea pig sperm acrosome is the homologue of mouse Tpx-1 and human TPX1 and is a member of the cysteine-rich secretory protein (CRISP) family. Mol Reprod Dev 44:221-229.
    • (1996) Mol Reprod Dev , vol.44 , pp. 221-229
    • Foster, J.A.1    Gerton, G.A.2
  • 18
    • 38449098244 scopus 로고    scopus 로고
    • Cysteine rich secretory proteins in reproduction and venom
    • Gibbs GM, O'Bryan MK. 2007. Cysteine rich secretory proteins in reproduction and venom. Soc Reprod Fertil Suppl 65:261-267.
    • (2007) Soc Reprod Fertil Suppl , vol.65 , pp. 261-267
    • Gibbs, G.M.1    O'Bryan, M.K.2
  • 19
    • 33645232953 scopus 로고    scopus 로고
    • The cystein-rich secretory protein domain of Tpx-1 is related to ion channel toxins and regulates ryanodine receptor calcium signaling
    • Gibbs GM, Scanlon MJ, Swarbrick J, Curtis S, Gallant E, Dulhunty AF, O'Bryan MK. 2006. The cystein-rich secretory protein domain of Tpx-1 is related to ion channel toxins and regulates ryanodine receptor calcium signaling. J Biol Chem 281:4156-4163.
    • (2006) J Biol Chem , vol.281 , pp. 4156-4163
    • Gibbs, G.M.1    Scanlon, M.J.2    Swarbrick, J.3    Curtis, S.4    Gallant, E.5    Dulhunty, A.F.6    O'Bryan, M.K.7
  • 20
    • 16844376656 scopus 로고    scopus 로고
    • Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cystein-rich domain has K+ channel inhibitor-like fold
    • Guo M, Teng M, Niu L, Liu Q, Huang Q, Hao Q. 2005. Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cystein-rich domain has K+ channel inhibitor-like fold. J Biol Chem 280:12405-12412.
    • (2005) J Biol Chem , vol.280 , pp. 12405-12412
    • Guo, M.1    Teng, M.2    Niu, L.3    Liu, Q.4    Huang, Q.5    Hao, Q.6
  • 21
    • 0023940101 scopus 로고
    • Purification and characterization of the primary acrosomal autoantigen of guinea pig epididymal spermatozoa
    • Hardy DM, Huang TT, Driscoll WJ, Tung KK, Wild GC. 1988. Purification and characterization of the primary acrosomal autoantigen of guinea pig epididymal spermatozoa. Biol Reprod 38:423-437.
    • (1988) Biol Reprod , vol.38 , pp. 423-437
    • Hardy, D.M.1    Huang, T.T.2    Driscoll, W.J.3    Tung, K.K.4    Wild, G.C.5
  • 22
    • 0029983024 scopus 로고    scopus 로고
    • Characterization of a human glycoprotein with potential role in sperm-egg fusion: CDNA cloning, immunohistochemical localization, and chromosomal assignment of the gene (AEGL1)
    • Hayahi M, Fujimoto S, Takano H, Ushiki T, Abe K, Ishikura A, Yoshida M, Kirchoff C, Ishibashi T, Kasahara M. 1996. Characterization of a human glycoprotein with potential role in sperm-egg fusion: cDNA cloning, immunohistochemical localization, and chromosomal assignment of the gene (AEGL1). Genomics 32:367-374.
    • (1996) Genomics , vol.32 , pp. 367-374
    • Hayahi, M.1    Fujimoto, S.2    Takano, H.3    Ushiki, T.4    Abe, K.5    Ishikura, A.6    Yoshida, M.7    Kirchoff, C.8    Ishibashi, T.9    Kasahara, M.10
  • 23
    • 0026085725 scopus 로고
    • Structure and function of the extracellular matrix of anuran eggs
    • Hedrick JL, Nishihara T. 1991. Structure and function of the extracellular matrix of anuran eggs. J Electr Micros Tech 17:319-335.
    • (1991) J Electr Micros Tech , vol.17 , pp. 319-335
    • Hedrick, J.L.1    Nishihara, T.2
  • 25
    • 1842843784 scopus 로고    scopus 로고
    • Insights into the molecular basis of sperm-egg recognition in mammals
    • Hoodbury T, Dean J. 2004. Insights into the molecular basis of sperm-egg recognition in mammals. Reproduction 127:417-422.
    • (2004) Reproduction , vol.127 , pp. 417-422
    • Hoodbury, T.1    Dean, J.2
  • 26
    • 0002479532 scopus 로고
    • The role of oviductal secretions in mediating gamete fusion in anuran amphibians
    • Katigiri Ch. 1987. The role of oviductal secretions in mediating gamete fusion in anuran amphibians. Zool Sci 4:1-14.
    • (1987) Zool Sci , vol.4 , pp. 1-14
    • Katigiri, Ch.1
  • 27
    • 33746492173 scopus 로고    scopus 로고
    • Sperm chemtaxis in marine invertebrates - Molecules and mechanisms
    • Kaupp UB, Hildebrand E, Weyand I. 2006. Sperm chemtaxis in marine invertebrates - Molecules and mechanisms. J Cell Physiol 208:487-494.
    • (2006) J Cell Physiol , vol.208 , pp. 487-494
    • Kaupp, U.B.1    Hildebrand, E.2    Weyand, I.3
  • 29
    • 0032499877 scopus 로고    scopus 로고
    • Molecular cloning of the rat Tpx-1 responsible for the interaction between spermatogenic and Sertoli cells
    • Maeda T, Sakashita M, Ohba Y, Nakanishi Y. 1998. Molecular cloning of the rat Tpx-1 responsible for the interaction between spermatogenic and Sertoli cells. Biochem Biophys Res Commun 248:140-146.
    • (1998) Biochem Biophys Res Commun , vol.248 , pp. 140-146
    • Maeda, T.1    Sakashita, M.2    Ohba, Y.3    Nakanishi, Y.4
  • 31
    • 0000513535 scopus 로고
    • Sperm chemo-orientation in the metazoa
    • Metz C, Monroy A, editors. New York: Academic Press
    • Miller R. 1985. Sperm chemo-orientation in the metazoa. In: Metz C, Monroy A, editors. Biology of fertilization, Vol.2. New York: Academic Press. pp. 275-337.
    • (1985) Biology of Fertilization , vol.2 , pp. 275-337
    • Miller, R.1
  • 32
    • 1542330659 scopus 로고    scopus 로고
    • Ligands and receptors mediating signal transduction in sea urchin spermatozoa
    • Neill AT, Vacquier VD. 2004. Ligands and receptors mediating signal transduction in sea urchin spermatozoa. Reproduction 127:141-149.
    • (2004) Reproduction , vol.127 , pp. 141-149
    • Neill, A.T.1    Vacquier, V.D.2
  • 33
    • 0030202724 scopus 로고    scopus 로고
    • Structure and function of asterosaps, sperm-activating peptides from the jelly coat of starfish eggs
    • Nishigaki T, Chiba K, Miki W, Hoshi M. 1996. Structure and function of asterosaps, sperm-activating peptides from the jelly coat of starfish eggs. Zygote 4:237-245.
    • (1996) Zygote , vol.4 , pp. 237-245
    • Nishigaki, T.1    Chiba, K.2    Miki, W.3    Hoshi, M.4
  • 35
    • 0035949509 scopus 로고    scopus 로고
    • Allurin, a 21 kD sperm chemoattractant from Xenopus egg jelly, is homologous to mammalian sperm-binding proteins
    • Olson J, Xiang X, Ziegert T, Kittelson A, Rawls A, Bieber A, Chandler DE. 2001. Allurin, a 21 kD sperm chemoattractant from Xenopus egg jelly, is homologous to mammalian sperm-binding proteins. Proc Natl Acad Sci USA 98:11205-11210.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11205-11210
    • Olson, J.1    Xiang, X.2    Ziegert, T.3    Kittelson, A.4    Rawls, A.5    Bieber, A.6    Chandler, D.E.7
  • 36
    • 0037150651 scopus 로고    scopus 로고
    • Penetration, adhesion, and fusion in mammalian sperm-egg interaction
    • Primakoff P, Myles DG. 2002. Penetration, adhesion, and fusion in mammalian sperm-egg interaction. Science 296:2183-2185.
    • (2002) Science , vol.296 , pp. 2183-2185
    • Primakoff, P.1    Myles, D.G.2
  • 37
    • 0036324568 scopus 로고    scopus 로고
    • Fertilization in the sea: The chemical identity of an abalone sperm attractant
    • Riffell JA, Krug PJ, Zimmer RK. 2002. Fertilization in the sea: The chemical identity of an abalone sperm attractant. J Exp Biol 205:1439-1450.
    • (2002) J Exp Biol , vol.205 , pp. 1439-1450
    • Riffell, J.A.1    Krug, P.J.2    Zimmer, R.K.3
  • 40
    • 0026521538 scopus 로고
    • Redistribution of a rat sperm epididymal glycoprotein after in vivo and in vitro capacitation
    • Rochwerger L, Cuasnicu PS. 1992. Redistribution of a rat sperm epididymal glycoprotein after in vivo and in vitro capacitation. Mol Reprod Dev 31:34-41.
    • (1992) Mol Reprod Dev , vol.31 , pp. 34-41
    • Rochwerger, L.1    Cuasnicu, P.S.2
  • 41
    • 0016160429 scopus 로고
    • Measurement of protein by spectrophotometry at 205 nm
    • Scopes RK. 1974. Measurement of protein by spectrophotometry at 205 nm. Anal Biochem 59:277-282.
    • (1974) Anal Biochem , vol.59 , pp. 277-282
    • Scopes, R.K.1
  • 42
    • 2342453841 scopus 로고    scopus 로고
    • Structural analysis of the human golgi-associated plant pathogenesis related GAPR-1 implicates dimerization as a regulatory mechanism
    • Serrano RL, Kuhn A, Hendricks A, Helms JB, Sinning I, Groves MR. 2004. Structural analysis of the human golgi-associated plant pathogenesis related GAPR-1 implicates dimerization as a regulatory mechanism. J Mol Biol 339:173-183.
    • (2004) J Mol Biol , vol.339 , pp. 173-183
    • Serrano, R.L.1    Kuhn, A.2    Hendricks, A.3    Helms, J.B.4    Sinning, I.5    Groves, M.R.6
  • 45
    • 33646191319 scopus 로고    scopus 로고
    • Odorant receptors and olfactory-like signaling mechanisms in mammalian sperm
    • Spehr M, Schwane K, Riffell JA, Zimmer RK, Hatt H. 2006. Odorant receptors and olfactory-like signaling mechanisms in mammalian sperm. Mol Cell Endocrinol 250:128-136.
    • (2006) Mol Cell Endocrinol , vol.250 , pp. 128-136
    • Spehr, M.1    Schwane, K.2    Riffell, J.A.3    Zimmer, R.K.4    Hatt, H.5
  • 47
    • 0029242430 scopus 로고
    • Structure, function and biosynthesis of sperm-activating peptides and fucose sulfate glycoconjugate in the extracellular coat of sea urchin eggs
    • Suzuki N. 1995. Structure, function and biosynthesis of sperm-activating peptides and fucose sulfate glycoconjugate in the extracellular coat of sea urchin eggs. Zool Sci 12:13-27.
    • (1995) Zool Sci , vol.12 , pp. 13-27
    • Suzuki, N.1
  • 49
    • 0026739991 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. 1992. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Biotechnology 24:145-149.
    • (1992) Biotechnology , vol.24 , pp. 145-149
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 51
    • 16644399785 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary x-ray crystallographic analysis of a cysteine-rich secretory protein (CRISP) from Naja atra venom
    • Wang YL, Goh KX, Wu WG, Chen CJ. 2004. Purification, crystallization and preliminary x-ray crystallographic analysis of a cysteine-rich secretory protein (CRISP) from Naja atra venom. Acta Crystallogr B Biol Crystallogr 60:1912-1915.
    • (2004) Acta Crystallogr B Biol Crystallogr , vol.60 , pp. 1912-1915
    • Wang, Y.L.1    Goh, K.X.2    Wu, W.G.3    Chen, C.J.4
  • 52
    • 0022372552 scopus 로고
    • Chemotaxis of Arbacia punctulata spermatozoa to resact, a peptide from the egg jelly layer
    • Ward GE, Brokaw CJ, Garbers DL, Vacquier VD. 1985. Chemotaxis of Arbacia punctulata spermatozoa to resact, a peptide from the egg jelly layer. J Cell Biol 101:2324-2329.
    • (1985) J Cell Biol , vol.101 , pp. 2324-2329
    • Ward, G.E.1    Brokaw, C.J.2    Garbers, D.L.3    Vacquier, V.D.4
  • 54
    • 12844255606 scopus 로고    scopus 로고
    • The sperm chemoattractant "allurin" is expressed and secreted from the Xenopus oviduct in a hormone regulated manner
    • Xiang X, Burnett LA, Rawls A, Bieber AL, Chandler DE. 2004. The sperm chemoattractant "allurin" is expressed and secreted from the Xenopus oviduct in a hormone regulated manner. Dev Biol 275:343-355.
    • (2004) Dev Biol , vol.275 , pp. 343-355
    • Xiang, X.1    Burnett, L.A.2    Rawls, A.3    Bieber, A.L.4    Chandler, D.E.5
  • 55
    • 12844282198 scopus 로고    scopus 로고
    • Allurin, a 21 kD sperm chemoattractant, is rapidly released from the outermost jelly layer of the Xenopus egg by diffusion and medium convection
    • Xiang X, Kittelson A, Olson J, Bieber A, Chandler D. 2005. Allurin, a 21 kD sperm chemoattractant, is rapidly released from the outermost jelly layer of the Xenopus egg by diffusion and medium convection. Mol Reprod Dev 70:344-360.
    • (2005) Mol Reprod Dev , vol.70 , pp. 344-360
    • Xiang, X.1    Kittelson, A.2    Olson, J.3    Bieber, A.4    Chandler, D.5
  • 56
    • 0037069393 scopus 로고    scopus 로고
    • A chemoattractant for ascidian spermatozoa is a sulfated steroid
    • Yoshida M, Murata M, Inaba K, Morisawa M. 2002. A chemoattractant for ascidian spermatozoa is a sulfated steroid. Proc Natl Acad Sci USA 99:14831-14836.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14831-14836
    • Yoshida, M.1    Murata, M.2    Inaba, K.3    Morisawa, M.4
  • 57
    • 0036888104 scopus 로고    scopus 로고
    • Identification of a novel GPI-anchored CRISP glycoprotein, MAK248, located on the posterior head and equatorial segment of cynomolgus macaque sperm
    • Yudin A, Li MW, Robertson KR, Tollner T, Cherr GN, Overstreet JW. 2002. Identification of a novel GPI-anchored CRISP glycoprotein, MAK248, located on the posterior head and equatorial segment of cynomolgus macaque sperm. Mol Reprod Dev 63:488-499.
    • (2002) Mol Reprod Dev , vol.63 , pp. 488-499
    • Yudin, A.1    Li, M.W.2    Robertson, K.R.3    Tollner, T.4    Cherr, G.N.5    Overstreet, J.W.6


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