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Volumn 120, Issue 8, 2003, Pages 937-948

A homologue of cysteine-rich secretory proteins induces premature degradation of vitelline envelopes and hatching of Xenopus laevis embryos

Author keywords

Cysteine rich secretory proteins; Hatching gland; Xenopus laevis CRISP

Indexed keywords

CYSTEINE; CYSTEINE RICH SECRETORY PROTEIN; MUTANT PROTEIN; NOGGIN; PHOSPHATIDYLCHOLINE; SECRETORY PROTEIN; UNCLASSIFIED DRUG; WNT PROTEIN;

EID: 0041328572     PISSN: 09254773     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0925-4773(03)00162-X     Document Type: Article
Times cited : (20)

References (42)
  • 1
    • 0020613589 scopus 로고
    • Localization of epididymal secretory proteins on rat spermatozoa
    • Brooks D.E., Tiver K. Localization of epididymal secretory proteins on rat spermatozoa. J. Reprod. Fertil. 69:1983;651-657.
    • (1983) J. Reprod. Fertil. , vol.69 , pp. 651-657
    • Brooks, D.E.1    Tiver, K.2
  • 2
    • 0022918330 scopus 로고
    • Molecular cloning of the cDNA for androgen-dependent sperm-coating glycoproteins secreted by the rat epididymis
    • Brooks D.E., Means A.R., Wright E.J., Singh S.P., Tiver K.K. Molecular cloning of the cDNA for androgen-dependent sperm-coating glycoproteins secreted by the rat epididymis. Eur. J. Biochem. 161:1986;13-18.
    • (1986) Eur. J. Biochem. , vol.161 , pp. 13-18
    • Brooks, D.E.1    Means, A.R.2    Wright, E.J.3    Singh, S.P.4    Tiver, K.K.5
  • 3
    • 0017067054 scopus 로고
    • Androgen-controlled specific proteins in rat epididymis
    • Cameo M.S., Blaquier J.A. Androgen-controlled specific proteins in rat epididymis. J. Endocrinol. 69:1976;47-55.
    • (1976) J. Endocrinol. , vol.69 , pp. 47-55
    • Cameo, M.S.1    Blaquier, J.A.2
  • 5
    • 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 D.J., Munuce M.J., Cuasnicu P.S. Mammalian sperm-egg fusion: the development of rat oolemma fusibility during oogenesis involves the appearance of binding sites for sperm protein 'DE'. Biol. Reprod. 55:1996;200-206.
    • (1996) Biol. Reprod. , vol.55 , pp. 200-206
    • Cohen, D.J.1    Munuce, M.J.2    Cuasnicu, P.S.3
  • 6
    • 0026026474 scopus 로고
    • Development of the Xenopus laevis hatching gland and its relationship to surface ectoderm patterning
    • Drysdale T.A., Elinson R.P. Development of the Xenopus laevis hatching gland and its relationship to surface ectoderm patterning. Development. 111:1991;469-478.
    • (1991) Development , vol.111 , pp. 469-478
    • Drysdale, T.A.1    Elinson, R.P.2
  • 8
    • 0034795758 scopus 로고    scopus 로고
    • Properties of the hatching enzyme from Xenopus laevis
    • Fan T.J., Katagiri C. Properties of the hatching enzyme from Xenopus laevis. Eur. J. Biochem. 268:2001;4892-4898.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4892-4898
    • Fan, T.J.1    Katagiri, C.2
  • 9
    • 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 J.A., Gerton G.L. 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. 44:1996;221-229.
    • (1996) Mol. Reprod. Dev. , vol.44 , pp. 221-229
    • Foster, J.A.1    Gerton, G.L.2
  • 10
    • 0031883963 scopus 로고    scopus 로고
    • Expression of the Armadillo family member p120cas1B in Xenopus embryos affects head differentiation but not axis formation
    • Geis K., Aberle H., Kuhl M., Kemler R., Wedlich D. Expression of the Armadillo family member p120cas1B in Xenopus embryos affects head differentiation but not axis formation. Dev. Genes Evol. 207:1998;471-481.
    • (1998) Dev. Genes Evol. , vol.207 , pp. 471-481
    • Geis, K.1    Aberle, H.2    Kuhl, M.3    Kemler, R.4    Wedlich, D.5
  • 12
    • 0037121051 scopus 로고    scopus 로고
    • Molecular characterization of the equine testis-specific protein 1 (TPX1) and acidic epididymal glycoprotein 2 (AEG2) genes encoding members of the cysteine-rich secretory protein (CRISP) family
    • Giese A., Jude R., Kuiper H., Raudsepp T., Piumi F., Schambony A., Guerin G., Chowdhary B.P., Distl O., Topfer-Petersen E., Leeb T. Molecular characterization of the equine testis-specific protein 1 (TPX1) and acidic epididymal glycoprotein 2 (AEG2) genes encoding members of the cysteine-rich secretory protein (CRISP) family. Gene. 299:2002;101-109.
    • (2002) Gene , vol.299 , pp. 101-109
    • Giese, A.1    Jude, R.2    Kuiper, H.3    Raudsepp, T.4    Piumi, F.5    Schambony, A.6    Guerin, G.7    Chowdhary, B.P.8    Distl, O.9    Topfer-Petersen, E.10    Leeb, T.11
  • 13
    • 0027321118 scopus 로고
    • Transcripts for cysteine-rich secretory protein-1 (CRISP-1; DE/AEG) and the novel related CRISP-3 are expressed under androgen control in the mouse salivary gland
    • Haendler B., Kratzschmar J., Theuring F., Schleuning W.D. Transcripts for cysteine-rich secretory protein-1 (CRISP-1; DE/AEG) and the novel related CRISP-3 are expressed under androgen control in the mouse salivary gland. Endocrinology. 133:1993;192-198.
    • (1993) Endocrinology , vol.133 , pp. 192-198
    • Haendler, B.1    Kratzschmar, J.2    Theuring, F.3    Schleuning, W.D.4
  • 15
    • 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 M.C., 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. 32:1996;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
  • 16
    • 85031083285 scopus 로고    scopus 로고
    • Hollemann, T., Panitz, F., Pieler, T., 1999. In situ hybridization techniques with Xenopus embryos. In: Richter, J.D. (Ed.), A Comparative Methods Approach to the Study of Oocytes and Embryos. Oxford University Press, Oxford, pp. 279-290.
    • Hollemann, T., Panitz, F., Pieler, T., 1999. In situ hybridization techniques with Xenopus embryos. In: Richter, J.D. (Ed.), A Comparative Methods Approach to the Study of Oocytes and Embryos. Oxford University Press, Oxford, pp. 279-290.
  • 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 P.N. Cloning and mapping of a testis-specific gene with sequence similarity to a sperm-coating glycoprotein gene. Genomics. 5:1989;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
    • 0031029642 scopus 로고    scopus 로고
    • Molecular cloning of Xenopus hatching enzyme and its specific expression in hatching gland cells
    • Katagiri C., Maeda R., Yamasika R., Mita K., Sargent T., Yasumasu Y. Molecular cloning of Xenopus hatching enzyme and its specific expression in hatching gland cells. Int. J. Dev. Biol. 41:1997;19-25.
    • (1997) Int. J. Dev. Biol. , vol.41 , pp. 19-25
    • Katagiri, C.1    Maeda, R.2    Yamasika, R.3    Mita, K.4    Sargent, T.5    Yasumasu, Y.6
  • 19
    • 0030020880 scopus 로고    scopus 로고
    • SGP28, a novel matrix glycoprotein in specific granules of human neutrophils with similarity to a human testis-specific gene product and a rodent sperm-coating glycoprotein
    • Kjeldsen L., Cowland J.B., Johnsen A.H., Borregaard N. SGP28, a novel matrix glycoprotein in specific granules of human neutrophils with similarity to a human testis-specific gene product and a rodent sperm-coating glycoprotein. FEBS Lett. 380:1996;246-250.
    • (1996) FEBS Lett. , vol.380 , pp. 246-250
    • Kjeldsen, L.1    Cowland, J.B.2    Johnsen, A.H.3    Borregaard, N.4
  • 20
    • 0029925313 scopus 로고    scopus 로고
    • The human cysteine-rich secretory protein (CRISP) family. Primary structure and tissue distribution of CRISP-1, CRISP-2 and CRISP-3
    • Kratzschmar J., Haendler B., Eberspaecher U., Roosterman D., Donner P., Schleuning W.D. The human cysteine-rich secretory protein (CRISP) family. Primary structure and tissue distribution of CRISP-1, CRISP-2 and CRISP-3. Eur. J. Biochem. 236:1996;827-836.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 827-836
    • Kratzschmar, J.1    Haendler, B.2    Eberspaecher, U.3    Roosterman, D.4    Donner, P.5    Schleuning, W.D.6
  • 21
    • 0033843245 scopus 로고    scopus 로고
    • Expression of connexin 30 in Xenopus embryos and its involvement in hatching gland function
    • Levin M., Mercola M. Expression of connexin 30 in Xenopus embryos and its involvement in hatching gland function. Dev. Dyn. 219:2000;96-101.
    • (2000) Dev. Dyn. , vol.219 , pp. 96-101
    • Levin, M.1    Mercola, M.2
  • 22
    • 0035726506 scopus 로고    scopus 로고
    • A hatching enzyme substrate in the Xenopus laevis egg envelope is a high molecular weight ZPA homolog
    • Lindsay L.L., Wallace M.A., Hedrick J.L. A hatching enzyme substrate in the Xenopus laevis egg envelope is a high molecular weight ZPA homolog. Dev. Growth Differ. 43:2001;305-313.
    • (2001) Dev. Growth Differ. , vol.43 , pp. 305-313
    • Lindsay, L.L.1    Wallace, M.A.2    Hedrick, J.L.3
  • 23
    • 0032867869 scopus 로고    scopus 로고
    • Direct regulation of the Xenopus engrailed-2 promoter by the Wnt signaling pathway, and a molecular screen for Wnt-responsive genes, confirm a role for Wnt signaling during neural patterning in Xenopus
    • McGrew L.L., Takemaru K.-I., Bates R., Moon R.T. Direct regulation of the Xenopus engrailed-2 promoter by the Wnt signaling pathway, and a molecular screen for Wnt-responsive genes, confirm a role for Wnt signaling during neural patterning in Xenopus. Mech. Dev. 87:1999;21-32.
    • (1999) Mech. Dev. , vol.87 , pp. 21-32
    • McGrew, L.L.1    Takemaru, K.-I.2    Bates, R.3    Moon, R.T.4
  • 24
    • 0026444953 scopus 로고
    • The mouse male germ cell-specific gene Tpx-1: Molecular structure, mode of expression in spermatogenesis, and sequence similarity to two non-mammalian genes
    • Mizuki N., Sarapata D.E., Garcia-Sanz J.A., Kasahara M. The mouse male germ cell-specific gene Tpx-1: molecular structure, mode of expression in spermatogenesis, and sequence similarity to two non-mammalian genes. Mamm. Genome. 3:1992;274-280.
    • (1992) Mamm. Genome. , vol.3 , pp. 274-280
    • Mizuki, N.1    Sarapata, D.E.2    Garcia-Sanz, J.A.3    Kasahara, M.4
  • 26
    • 0029057894 scopus 로고
    • The human glioma pathogenesis-related protein is structurally related to plant pathogenesis-related proteins and its gene is expressed specifically in brain tumors
    • Murphy E.V., Zhang Y., Zhu W., Biggs J. The human glioma pathogenesis-related protein is structurally related to plant pathogenesis-related proteins and its gene is expressed specifically in brain tumors. Gene. 159:1995;131-135.
    • (1995) Gene , vol.159 , pp. 131-135
    • Murphy, E.V.1    Zhang, Y.2    Zhu, W.3    Biggs, J.4
  • 27
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Engng. 10:1997;1-6.
    • (1997) Protein Engng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 30
    • 0029848759 scopus 로고    scopus 로고
    • CRISP-3, a protein with homology to plant defense proteins, is expressed in mouse B cells under the control of Oct2
    • Pfisterer P., Konig H., Hess J., Lipowsky G., Haendler B., Schleuning W.D., Wirth T. CRISP-3, a protein with homology to plant defense proteins, is expressed in mouse B cells under the control of Oct2. Mol. Cell Biol. 16:1996;6160-6168.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 6160-6168
    • Pfisterer, P.1    Konig, H.2    Hess, J.3    Lipowsky, G.4    Haendler, B.5    Schleuning, W.D.6    Wirth, T.7
  • 31
    • 0026521538 scopus 로고
    • Redistribution of a rat sperm epididymal glycoprotein after in vitro and in vivo capacitation
    • Rochwerger L., Cuasnicu P.S. Redistribution of a rat sperm epididymal glycoprotein after in vitro and in vivo capacitation. Mol. Reprod. Dev. 31:1992;34-41.
    • (1992) Mol. Reprod. Dev. , vol.31 , pp. 34-41
    • Rochwerger, L.1    Cuasnicu, P.S.2
  • 32
    • 0026670417 scopus 로고
    • Mammalian sperm-egg fusion: The rat egg has complementary sites for a sperm protein that mediates gamete fusion
    • Rochwerger L., Cohen D.J., Cuasnicu P.S. Mammalian sperm-egg fusion: the rat egg has complementary sites for a sperm protein that mediates gamete fusion. Dev. Biol. 153:1992;83-90.
    • (1992) Dev. Biol. , vol.153 , pp. 83-90
    • Rochwerger, L.1    Cohen, D.J.2    Cuasnicu, P.S.3
  • 34
    • 0029081819 scopus 로고
    • Isolation and characterization of the androgen-dependent mouse cysteine-rich secretory protein-3 (CRISP-3) gene
    • Schwidetzky U., Haendler B., Schleuning W.D. Isolation and characterization of the androgen-dependent mouse cysteine-rich secretory protein-3 (CRISP-3) gene. Biochem. J. 309:1995;831-836.
    • (1995) Biochem. J. , vol.309 , pp. 831-836
    • Schwidetzky, U.1    Haendler, B.2    Schleuning, W.D.3
  • 35
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68:1996;850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 36
    • 0030960366 scopus 로고    scopus 로고
    • Rapid 'de novo' peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer
    • Shevchenko A., Chernushevich I., Ens W., Standing K.G., Thomson B., Wilm M., Mann M. Rapid 'de novo' peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer. Rapid Commun. Mass Spectrom. 11:1997;1015-1024.
    • (1997) Rapid Commun. Mass Spectrom. , vol.11 , pp. 1015-1024
    • Shevchenko, A.1    Chernushevich, I.2    Ens, W.3    Standing, K.G.4    Thomson, B.5    Wilm, M.6    Mann, M.7
  • 37
    • 0029978849 scopus 로고    scopus 로고
    • A sticky problem: The Xenopus cement gland as a paradigm for anteriopsterior patterning
    • Sive H.L., Bradley L.C. A sticky problem: the Xenopus cement gland as a paradigm for anteriopsterior patterning. Dev. Dyn. 205:1996;265.
    • (1996) Dev. Dyn. , vol.205 , pp. 265
    • Sive, H.L.1    Bradley, L.C.2
  • 38
    • 0024337818 scopus 로고
    • Progressive determination during formation of the anterioposterior axis in Xenopus laevis
    • Sive H.L., Hatton K., Weintraub H. Progressive determination during formation of the anterioposterior axis in Xenopus laevis. Cell. 1989;58.
    • (1989) Cell , pp. 58
    • Sive, H.L.1    Hatton, K.2    Weintraub, H.3
  • 39
    • 0032478175 scopus 로고    scopus 로고
    • Structure comparison of human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein P14a indicates a functional link between the human immune system and a plant defense system
    • Szyperski T., Fernandez C., Mumenthaler C., Wuthrich K. Structure comparison of human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein P14a indicates a functional link between the human immune system and a plant defense system. Proc. Natl Acad. Sci. USA. 95:1998;2262-2266.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 2262-2266
    • Szyperski, T.1    Fernandez, C.2    Mumenthaler, C.3    Wuthrich, K.4
  • 40
    • 0019797705 scopus 로고
    • The hatching enzyme from Xenopus laevis: Limited proteolysis of the fertilization envelope
    • Urch U.A., Hedrick J.L. The hatching enzyme from Xenopus laevis: limited proteolysis of the fertilization envelope. J. Supramol. Struct. Cell Biochem. 15:1981;111-117.
    • (1981) J. Supramol. Struct. Cell Biochem. , vol.15 , pp. 111-117
    • Urch, U.A.1    Hedrick, J.L.2
  • 41
    • 0037167616 scopus 로고    scopus 로고
    • Purification and cloning of toxins from elapid venoms that target cyclic nucleotide-gated ion channels
    • Yamazaki Y., Brown R.L., Morita T. Purification and cloning of toxins from elapid venoms that target cyclic nucleotide-gated ion channels. Biochemistry. 41:2002;11331-11337.
    • (2002) Biochemistry , vol.41 , pp. 11331-11337
    • Yamazaki, Y.1    Brown, R.L.2    Morita, T.3


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