메뉴 건너뛰기




Volumn 79, Issue 6, 2008, Pages 1046-1053

Association of the protein D and protein E forms of rat CRISP1 with epididymal sperm

Author keywords

Acrosome reaction; CRISP1; Epididymis; Male reproductive tract; Protein DE; Sperm; Sperm capacitation

Indexed keywords

CELL PROTEIN; PROTEIN CRISP1; UNCLASSIFIED DRUG;

EID: 56749130727     PISSN: 00063363     EISSN: 15297268     Source Type: Journal    
DOI: 10.1095/biolreprod.108.070664     Document Type: Article
Times cited : (14)

References (41)
  • 1
    • 33645232953 scopus 로고    scopus 로고
    • The cysteine-rich secretory protein domain of Tpx-1 is related to ion channel toxins and regulates ryanodine receptor Ca2+ signaling
    • Gibbs GM, Scanlon MJ, Swarbrick J, Curtis S, Gallant E, Dulhunty AF, O'Bryan MK. The cysteine-rich secretory protein domain of Tpx-1 is related to ion channel toxins and regulates ryanodine receptor Ca2+ signaling. J Biol Chem 2006; 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
  • 2
    • 16844376656 scopus 로고    scopus 로고
    • Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K+ channel inhibitor-like fold
    • Guo M, Teng M, Niu L, Liu Q, Huang Q, Hao Q. Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K+ channel inhibitor-like fold. J Biol Chem 2005; 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
  • 3
    • 20544476609 scopus 로고    scopus 로고
    • Crystal structure of a CRISP family Ca2+ -channel blocker derived from snake venom
    • Shikamoto Y, Suto K, Yamazaki Y, Morita T, Mizuno H. Crystal structure of a CRISP family Ca2+ -channel blocker derived from snake venom. J Mol Biol 2005; 350:735-743.
    • (2005) J Mol Biol , vol.350 , pp. 735-743
    • Shikamoto, Y.1    Suto, K.2    Yamazaki, Y.3    Morita, T.4    Mizuno, H.5
  • 5
    • 23044468262 scopus 로고    scopus 로고
    • Blocking effect and crystal structure of natrin toxin, a cysteine-rich secretory protein from Naja atra venom that targets the BKCa channel
    • Wang J, Shen B, Guo M, Lou X, Duan Y, Cheng XP, Teng M, Niu L, Liu Q, Huang Q, Hao Q. Blocking effect and crystal structure of natrin toxin, a cysteine-rich secretory protein from Naja atra venom that targets the BKCa channel. Biochemistry 2005; 44:10145-10152.
    • (2005) Biochemistry , vol.44 , pp. 10145-10152
    • Wang, J.1    Shen, B.2    Guo, M.3    Lou, X.4    Duan, Y.5    Cheng, X.P.6    Teng, M.7    Niu, L.8    Liu, Q.9    Huang, Q.10    Hao, Q.11
  • 6
    • 0033582176 scopus 로고    scopus 로고
    • Pseudechetoxin: A peptide blocker of cyclic nucleotide-gated ion channels
    • Brown RL, Haley TL, West KA, Crabb JW. Pseudechetoxin: a peptide blocker of cyclic nucleotide-gated ion channels. Proc Natl Acad Sci U S A 1999; 96:754-759.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 754-759
    • Brown, R.L.1    Haley, T.L.2    West, K.A.3    Crabb, J.W.4
  • 9
    • 0030001460 scopus 로고    scopus 로고
    • Helothermine, a lizard venom toxin, inhibits calcium current in cerebellar granules
    • Nobile M, Noceti F, Prestipino G, Possani LD. Helothermine, a lizard venom toxin, inhibits calcium current in cerebellar granules. Exp Brain Res 1996; 110:15-20.
    • (1996) Exp Brain Res , vol.110 , pp. 15-20
    • Nobile, M.1    Noceti, F.2    Prestipino, G.3    Possani, L.D.4
  • 10
    • 0037167616 scopus 로고    scopus 로고
    • Purification and cloning of toxins from elapid venoms that target cyclic nucleotide-gated ion channels
    • Yamazaki Y, Brown RL, Morita T. Purification and cloning of toxins from elapid venoms that target cyclic nucleotide-gated ion channels. Biochemistry 2002; 41:11331-11337.
    • (2002) Biochemistry , vol.41 , pp. 11331-11337
    • Yamazaki, Y.1    Brown, R.L.2    Morita, T.3
  • 11
    • 0029983024 scopus 로고    scopus 로고
    • Characterization of a human glycoprotein with a potential role in sperm-egg fusion: CDNA cloning, immunohistochemical localization, and chromosomal assignment of the gene (AEGL1)
    • Hayashi M, Fujimoto S, Takano H, Ushiki T, Abe K, Ishikura H, Yoshida MC, Kirchhoff C, Ishibashi T, Kasahara M. Characterization of a human glycoprotein with a potential role in sperm-egg fusion: cDNA cloning, immunohistochemical localization, and chromosomal assignment of the gene (AEGL1). Genomics 1996; 32:367-374.
    • (1996) Genomics , vol.32 , pp. 367-374
    • Hayashi, M.1    Fujimoto, S.2    Takano, H.3    Ushiki, T.4    Abe, K.5    Ishikura, H.6    Yoshida, M.C.7    Kirchhoff, C.8    Ishibashi, T.9    Kasahara, M.10
  • 12
    • 17444362229 scopus 로고    scopus 로고
    • Mouse cysteine-rich secretory protein 4 (CRISP4): A member of the Crisp family exclusively expressed in the epididymis in an androgen-dependent manner
    • Jalkanen J, Huhtaniemi I, Poutanen M. Mouse cysteine-rich secretory protein 4 (CRISP4): a member of the Crisp family exclusively expressed in the epididymis in an androgen-dependent manner. Biol Reprod 2005; 72:1268-1274.
    • (2005) Biol Reprod , vol.72 , pp. 1268-1274
    • Jalkanen, J.1    Huhtaniemi, I.2    Poutanen, M.3
  • 15
    • 0031434712 scopus 로고    scopus 로고
    • Differential androgen regulation of the murine genes for cysteine-rich secretory proteins (CRISP)
    • Haendler B, Habenicht UF, Schwidetzky U, Schuttke I, Schleuning WD. Differential androgen regulation of the murine genes for cysteine-rich secretory proteins (CRISP). Eur J Biochem 1997; 250:440-446.
    • (1997) Eur J Biochem , vol.250 , pp. 440-446
    • Haendler, B.1    Habenicht, U.F.2    Schwidetzky, U.3    Schuttke, I.4    Schleuning, W.D.5
  • 16
    • 0032931891 scopus 로고    scopus 로고
    • Expression of transcripts for cysteine-rich secretory proteins (CRISPs) in the murine lacrimal gland
    • Haendler B, Toda I, Sullivan DA, Schleuning WD. Expression of transcripts for cysteine-rich secretory proteins (CRISPs) in the murine lacrimal gland. J Cell Physiol 1999; 178:371-378.
    • (1999) J Cell Physiol , vol.178 , pp. 371-378
    • Haendler, B.1    Toda, I.2    Sullivan, D.A.3    Schleuning, W.D.4
  • 17
    • 0024742682 scopus 로고
    • Cloning and mapping of a testis-specific gene with sequence similarity to a sperm-coating glycoprotein gene
    • Kasahara M, Gutknecht J, Brew K, Spurr N, Goodfellow PN. Cloning and mapping of a testis-specific gene with sequence similarity to a sperm-coating glycoprotein gene. Genomics 1989; 5:527-534.
    • (1989) Genomics , vol.5 , pp. 527-534
    • Kasahara, M.1    Gutknecht, J.2    Brew, K.3    Spurr, N.4    Goodfellow, P.N.5
  • 18
    • 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. Human testicular protein TPX1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction. Mol Hum Reprod 2005; 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
  • 20
    • 0026788322 scopus 로고
    • Mouse submandibular glands express an androgen-regulated transcript encoding an acidic epididymal glycoprotein-like molecule
    • Mizuki N, Kasahara M. Mouse submandibular glands express an androgen-regulated transcript encoding an acidic epididymal glycoprotein-like molecule. Mol Cell Endocrinol 1992; 89:25-32.
    • (1992) Mol Cell Endocrinol , vol.89 , pp. 25-32
    • Mizuki, N.1    Kasahara, M.2
  • 23
    • 18244387198 scopus 로고    scopus 로고
    • Characterization and localization of cysteine-rich secretory protein 3 (CRISP-3) in the human male reproductive tract
    • Udby L, Bjartell A, Malm J, Egesten A, Lundwall A, Cowland JB, Borregaard N, Kjeldsen L. Characterization and localization of cysteine-rich secretory protein 3 (CRISP-3) in the human male reproductive tract. J Androl 2005; 26:333-342.
    • (2005) J Androl , vol.26 , pp. 333-342
    • Udby, L.1    Bjartell, A.2    Malm, J.3    Egesten, A.4    Lundwall, A.5    Cowland, J.B.6    Borregaard, N.7    Kjeldsen, L.8
  • 24
    • 0017067054 scopus 로고
    • Androgen-controlled specific proteins in rat epididymis
    • Cameo MS, Blaquier JA. Androgen-controlled specific proteins in rat epididymis. J Endocrinol 1976; 69:47-55.
    • (1976) J Endocrinol , vol.69 , pp. 47-55
    • Cameo, M.S.1    Blaquier, J.A.2
  • 25
    • 0028289142 scopus 로고
    • Rat epididymis-specific sperm maturation antigens. I. Evidence that the 26 kD 4E9 antigen found on rat caudal epididymal sperm tail is derived from a protein secreted by the epididymis
    • Moore A, Ensrud KM, White TW, Frethem CD, Hamilton DW. Rat epididymis-specific sperm maturation antigens. I. Evidence that the 26 kD 4E9 antigen found on rat caudal epididymal sperm tail is derived from a protein secreted by the epididymis. Mol Reprod Dev 1994; 37:181-194.
    • (1994) Mol Reprod Dev , vol.37 , pp. 181-194
    • Moore, A.1    Ensrud, K.M.2    White, T.W.3    Frethem, C.D.4    Hamilton, D.W.5
  • 26
    • 0031018080 scopus 로고    scopus 로고
    • The 26 kD protein recognized on rat cauda epididymal sperm by monoclonal antibody 4E9 has internal peptide sequence that is identical to the secreted form of epididymal protein E
    • Xu W, Ensrud KM, Hamilton DW. The 26 kD protein recognized on rat cauda epididymal sperm by monoclonal antibody 4E9 has internal peptide sequence that is identical to the secreted form of epididymal protein E. Mol Reprod Dev 1997; 46:377-382.
    • (1997) Mol Reprod Dev , vol.46 , pp. 377-382
    • Xu, W.1    Ensrud, K.M.2    Hamilton, D.W.3
  • 27
    • 0029989271 scopus 로고    scopus 로고
    • Identification of the rat epididymis-secreted 4E9 antigen as protein E: Further biochemical characterization of the highly homologous epididymal secretory proteins D and E
    • Xu W, Hamilton DW. Identification of the rat epididymis-secreted 4E9 antigen as protein E: further biochemical characterization of the highly homologous epididymal secretory proteins D and E. Mol Reprod Dev 1996; 43:347-357.
    • (1996) Mol Reprod Dev , vol.43 , pp. 347-357
    • Xu, W.1    Hamilton, D.W.2
  • 28
    • 0035992843 scopus 로고    scopus 로고
    • A comparative analysis of expression and processing of the rat epididymal fluid and sperm-bound forms of proteins D and E
    • Roberts KP, Ensrud KM, Hamilton DW. A comparative analysis of expression and processing of the rat epididymal fluid and sperm-bound forms of proteins D and E. Biol Reprod 2002; 67:525-533.
    • (2002) Biol Reprod , vol.67 , pp. 525-533
    • Roberts, K.P.1    Ensrud, K.M.2    Hamilton, D.W.3
  • 29
    • 0035025744 scopus 로고    scopus 로고
    • A rapid and efficient method for purification of protein D/E from the rat epididymis: Biochemical characterization of a protein involved in the fertilitzation process
    • Tubbs CE, Hall JC, Scott RO, Copeland C, Cooper R. A rapid and efficient method for purification of protein D/E from the rat epididymis: biochemical characterization of a protein involved in the fertilitzation process. Int J Biochromatography 2001; 6:572-581.
    • (2001) Int J Biochromatography , vol.6 , pp. 572-581
    • Tubbs, C.E.1    Hall, J.C.2    Scott, R.O.3    Copeland, C.4    Cooper, R.5
  • 30
    • 0037623742 scopus 로고    scopus 로고
    • Inhibition of capacitation-associated tyrosine phosphorylation signaling in rat sperm by epididymal protein Crisp-1
    • Roberts KP, Wamstad JA, Ensrud KM, Hamilton DW. Inhibition of capacitation-associated tyrosine phosphorylation signaling in rat sperm by epididymal protein Crisp-1. Biol Reprod 2003; 69:572-581.
    • (2003) Biol Reprod , vol.69 , pp. 572-581
    • Roberts, K.P.1    Wamstad, J.A.2    Ensrud, K.M.3    Hamilton, D.W.4
  • 32
    • 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. Mammalian sperm-egg fusion: evidence that epididymal protein DE plays a role in mouse gamete fusion. Biol Reprod 2000; 63:462-468.
    • (2000) Biol Reprod , vol.63 , pp. 462-468
    • Cohen, D.J.1    Ellerman, D.A.2    Cuasnicu, P.S.3
  • 33
    • 0029834990 scopus 로고    scopus 로고
    • Mammalian sperm-egg fusion: The development of rat oolemma fusibility during oogenesis involves the appearance of binding sites for sperm protein "DE
    • Cohen DJ, Munuce MJ, Cuasnicu PS. Mammalian sperm-egg fusion: the development of rat oolemma fusibility during oogenesis involves the appearance of binding sites for sperm protein "DE". Biol Reprod 1996; 55:200-206.
    • (1996) Biol Reprod , vol.55 , pp. 200-206
    • Cohen, D.J.1    Munuce, M.J.2    Cuasnicu, P.S.3
  • 34
    • 0036785275 scopus 로고    scopus 로고
    • Expression and structure-function analysis of de, a sperm cysteine-rich secretory protein that mediates gamete fusion
    • Ellerman DA, Da Ros VG, Cohen DJ, Busso D, Morgenfeld MM, Cuasnicu PS. Expression and structure-function analysis of de, a sperm cysteine-rich secretory protein that mediates gamete fusion. Biol Reprod 2002; 67:1225-1231.
    • (2002) Biol Reprod , vol.67 , pp. 1225-1231
    • Ellerman, D.A.1    Da Ros, V.G.2    Cohen, D.J.3    Busso, D.4    Morgenfeld, M.M.5    Cuasnicu, P.S.6
  • 35
    • 0029906927 scopus 로고    scopus 로고
    • Characterization of high-affinity protein D binding sites on the surface of rat epididymal spermatozoa
    • Hall JC, Tubbs CE, Li Y, Ashraf S. Characterization of high-affinity protein D binding sites on the surface of rat epididymal spermatozoa. Biochem Mol Biol Int 1996; 40:1003-1010.
    • (1996) Biochem Mol Biol Int , vol.40 , pp. 1003-1010
    • Hall, J.C.1    Tubbs, C.E.2    Li, Y.3    Ashraf, S.4
  • 36
    • 0020357527 scopus 로고
    • Studies on the binding of a 32K rat epididymal protein to rat epididymal spermatozoa
    • Wong PY, Tsang AY. Studies on the binding of a 32K rat epididymal protein to rat epididymal spermatozoa. Biol Reprod 1982; 27:1239-1246.
    • (1982) Biol Reprod , vol.27 , pp. 1239-1246
    • Wong, P.Y.1    Tsang, A.Y.2
  • 38
    • 1942508906 scopus 로고    scopus 로고
    • Bicarbonate is required for migration of sperm epididymal protein DE (CRISP-1) to the equatorial segment and expression of rat sperm fusion ability
    • Da Ros VG, Munuce MJ, Cohen DJ, Marin-Briggiler CI, Busso D, Visconti PE, Cuasnicu PS. Bicarbonate is required for migration of sperm epididymal protein DE (CRISP-1) to the equatorial segment and expression of rat sperm fusion ability. Biol Reprod 2004; 70:1325-1332.
    • (2004) Biol Reprod , vol.70 , pp. 1325-1332
    • Da Ros, V.G.1    Munuce, M.J.2    Cohen, D.J.3    Marin-Briggiler, C.I.4    Busso, D.5    Visconti, P.E.6    Cuasnicu, P.S.7
  • 39
    • 26944457328 scopus 로고    scopus 로고
    • A mouse sperm decapacitation factor receptor is phosphatidylethanolamine-binding protein 1
    • Gibbons R, Adeoya-Osiguwa SA, Fraser LR. A mouse sperm decapacitation factor receptor is phosphatidylethanolamine-binding protein 1. Reproduction 2005; 130:497-508.
    • (2005) Reproduction , vol.130 , pp. 497-508
    • Gibbons, R.1    Adeoya-Osiguwa, S.A.2    Fraser, L.R.3
  • 40
    • 31044442157 scopus 로고    scopus 로고
    • The identification of mouse sperm-surface-associated proteins and characterization of their ability to act as decapacitation factors
    • Nixon B, MacIntyre DA, Mitchell LA, Gibbs GM, O'Bryan M, Aitken RJ. The identification of mouse sperm-surface-associated proteins and characterization of their ability to act as decapacitation factors. Biol Reprod 2006; 74:275-287.
    • (2006) Biol Reprod , vol.74 , pp. 275-287
    • Nixon, B.1    MacIntyre, D.A.2    Mitchell, L.A.3    Gibbs, G.M.4    O'Bryan, M.5    Aitken, R.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.