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Volumn 110, Issue 3, 2010, Pages 620-629

Exclusive expression of a membrane-bound spink3-interacting serine protease-like protein TESPL in mouse testis

Author keywords

Acrosome; Prss2; Sperm; Spink3; Testicular serine protease

Indexed keywords

CHYMOTRYPSIN; COMPLEMENTARY DNA; CYSTEINE; PROLINE; PRSS 2 PROTEIN; SERINE PROTEINASE; SPINK 3 PROTEIN; TESTIS SPECIFIC PROTEASE LIKE PROTEIN; TRYPSIN; TRYPSIN INHIBITOR; TRYPSINOGEN; UNCLASSIFIED DRUG;

EID: 77952681714     PISSN: 07302312     EISSN: 10974644     Source Type: Journal    
DOI: 10.1002/jcb.22571     Document Type: Article
Times cited : (11)

References (30)
  • 1
    • 0020491487 scopus 로고
    • Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 a resolution. Structure solution, crystallographic refinement and preliminary structural interpretation
    • Bolognesi M, Gatti G, Menagatti E, Guarneri M, Marquart M, Papamokos E, Huber R. 1982. Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 A resolution. Structure solution, crystallographic refinement and preliminary structural interpretation. J Mol Biol 162:839-868.
    • (1982) J Mol Biol , vol.162 , pp. 839-868
    • Bolognesi, M.1    Gatti, G.2    Menagatti, E.3    Guarneri, M.4    Marquart, M.5    Papamokos, E.6    Huber, R.7
  • 2
    • 0018188613 scopus 로고
    • The activation of proacrosin in spermatozoa from ram bull and boar
    • Brown CR, Harrison RA. 1978. The activation of proacrosin in spermatozoa from ram bull and boar. Biochem Biophys Acta 526:202-217.
    • (1978) Biochem Biophys Acta , vol.526 , pp. 202-217
    • Brown, C.R.1    Harrison, R.A.2
  • 3
    • 77957022252 scopus 로고
    • Bull seminal plasma proteinase inhibitors
    • Cechová D, Jonáková V. 1981. Bull seminal plasma proteinase inhibitors. Methods Enzymol 80:792-803.
    • (1981) Methods Enzymol , vol.80 , pp. 792-803
    • Cechová, D.1    Jonáková, V.2
  • 4
    • 0031794477 scopus 로고    scopus 로고
    • Developmental profile of a caltrin-like protease inhibitor, P12, in mouse seminal vesicle and characterization of its binding sites on sperm surface
    • Chen LY, Lin YH, Lai ML, Chen YH. 1998. Developmental profile of a caltrin-like protease inhibitor, P12, in mouse seminal vesicle and characterization of its binding sites on sperm surface. Biol Reprod 59:1498-1505.
    • (1998) Biol Reprod , vol.59 , pp. 1498-1505
    • Chen, L.Y.1    Lin, Y.H.2    Lai, M.L.3    Chen, Y.H.4
  • 6
    • 0017221864 scopus 로고
    • Proteinase inhibitors from guinea pig seminal vesicles
    • Fink E, Fritz H. 1976. Proteinase inhibitors from guinea pig seminal vesicles. Methods Enzymol 45:825-833.
    • (1976) Methods Enzymol , vol.45 , pp. 825-833
    • Fink, E.1    Fritz, H.2
  • 7
    • 0025040329 scopus 로고
    • Amino acid sequence elucidation of human acrosin-trypsin inhibitor (HUSI-II) reveals that Kazal-type proteinase inhibitors are structurally related to beta-subunits of glycoprotein hormones
    • DOI 10.1016/0014-5793(90)81273-Q
    • Fink E, Hehlein-Fink C, Eulitz M. 1990. Amino acid sequence elucidation of human acrosin-trypsin inhibitor (HUSI-II) reveals that Kazal-type proteinase inhibitors are structurally related to beta-subunits of glycoprotein hormones. FEBS Lett 270:222-224. (Pubitemid 20288607)
    • (1990) FEBS Letters , vol.270 , Issue.1-2 , pp. 222-224
    • Fink, E.1    Hehlein-Fink, C.2    Eulitz, M.3
  • 8
    • 0014432941 scopus 로고
    • Chemistry and biochemistry of proteinase inhibitors from mammalian tissues
    • Fritz H, Trautschold I, Haendle H, Werle E. 1968. Chemistry and biochemistry of proteinase inhibitors from mammalian tissues. Ann NY Acad Sci 146:400-413.
    • (1968) Ann NY Acad Sci , vol.146 , pp. 400-413
    • Fritz, H.1    Trautschold, I.2    Haendle, H.3    Werle, E.4
  • 9
    • 0017242086 scopus 로고
    • Proteinase inhibitors from boar seminal plasma
    • Fritz H, Tschesche H, Fink E. 1976. Proteinase inhibitors from boar seminal plasma. Methods Enzymol 45:834-847.
    • (1976) Methods Enzymol , vol.45 , pp. 834-847
    • Fritz, H.1    Tschesche, H.2    Fink, E.3
  • 10
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Gavel Y, von Heijne G. 1990. Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering. Protein Eng 3:433-442. (Pubitemid 20201068)
    • (1990) Protein Engineering , vol.3 , Issue.5 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 11
    • 0013841509 scopus 로고
    • On a hormone dependent inhibitor of proteolytic enzymes in male accessory sex glands and in sperm
    • Haendle H, Fritz H, Trautschold I, Werle E. 1965. On a hormone dependent inhibitor of proteolytic enzymes in male accessory sex glands and in sperm. Hoppe Seylers Z Physiol Chem 343:185-188.
    • (1965) Hoppe Seylers Z Physiol Chem , vol.343 , pp. 185-188
    • Haendle, H.1    Fritz, H.2    Trautschold, I.3    Werle, E.4
  • 12
    • 0020401889 scopus 로고
    • The location of acrosin and proacrosin in ram spermatozoa
    • Harrison RA, Flechon JE, Brown CR. 1982. The location of acrosin and proacrosin in ram spermatozoa. J Reprod Fertil 66:349-358.
    • (1982) J Reprod Fertil , vol.66 , pp. 349-358
    • Harrison, R.A.1    Flechon, J.E.2    Brown, C.R.3
  • 13
    • 0037053319 scopus 로고    scopus 로고
    • A mouse serine protease TESP5 is selectively included into lipid rafts of sperm membrane presumably as a glycosylphosphatidylinositol-anchored protein
    • DOI 10.1074/jbc.M112470200
    • Honda A, Yamagata K, Sugiura S, Watanabe K, Baba T. 2002. A mouse serine protease TESP5 is selectively included into lipid rafts of sperm membrane presumably as a glycosylphosphatidylinositol-anchored protein. J Biol Chem 277:16976-16984. (Pubitemid 34967726)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.19 , pp. 16976-16984
    • Honda, A.1    Yamagata, K.2    Sugiura, S.3    Watanabe, K.4    Baba, T.5
  • 14
    • 0021166026 scopus 로고
    • Demonstration of a new acrosin inhibitor in human seminal plasma
    • Huhtala ML. 1984. Demonstration of a new acrosin inhibitor in human seminal plasma. Hoppe Seylers Z Physiol Chem 365:819-825.
    • (1984) Hoppe Seylers Z Physiol Chem , vol.365 , pp. 819-825
    • Huhtala, M.L.1
  • 16
    • 0025950239 scopus 로고
    • Purification and characterization of a trypsin inhibitor from mouse seminal vesicle secretion
    • Lai ML, Chen SW, Chen YH. 1991. Purification and characterization of a trypsin inhibitor from mouse seminal vesicle secretion. Arch Biochem Biophys 290:265-271.
    • (1991) Arch Biochem Biophys , vol.290 , pp. 265-271
    • Lai, M.L.1    Chen, S.W.2    Chen, Y.H.3
  • 17
    • 0035831547 scopus 로고    scopus 로고
    • A Novel Heat-labile Phospholipid-binding Protein, SVS VII, in Mouse Seminal Vesicle as a Sperm Motility Enhancer
    • DOI 10.1074/jbc.M006954200
    • Luo CW, Lin HJ, Chen YH. 2001. A novel heat-labile phospholipid-binding protein, SVS VII, in mouse seminal vesicle as a sperm motility enhancer. J Biol Chem 276:6913-6921. (Pubitemid 37391984)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.10 , pp. 6913-6921
    • Luo, C.-W.1    Lin, H.-J.2    Chen, Y.-H.3
  • 18
    • 1642273611 scopus 로고    scopus 로고
    • Distinction of sperm-binding site and reactive site for trypsin inhibition on p12 secreted from the accessory sex glands of male mice
    • Luo CW, Lin HJ, Gopinath SC, Chen YH. 2004. Distinction of sperm-binding site and reactive site for trypsin inhibition on p12 secreted from the accessory sex glands of male mice. Biol Reprod 70:965-971.
    • (2004) Biol Reprod , vol.70 , pp. 965-971
    • Luo, C.W.1    Lin, H.J.2    Gopinath, S.C.3    Chen, Y.H.4
  • 20
    • 0021018557 scopus 로고
    • Homologies in the structures of bull seminal plasma acrosin inhibitors and comparison with other homologous proteinase inhibitors of the Kazal type
    • Meloun B, Cechová D, Jonáková V. 1983. Homologies in the structures of bull seminal plasma acrosin inhibitors and comparison with other homologous proteinase inhibitors of the Kazal type. Hoppe Seylers Z Physiol Chem 364: 1665-1670.
    • (1983) Hoppe Seylers Z Physiol Chem , vol.364 , pp. 1665-1670
    • Meloun, B.1    Cechová, D.2    Jonáková, V.3
  • 21
    • 0023484841 scopus 로고
    • A secretory protease inhibitor requires androgens for its expression in male sex accessory tissues but is expressed constitutively in pancreas
    • Mills JS, Needham M, Parker MG. 1987. A secretory protease inhibitor requires androgens for its expression in male sex accessory tissues but is expressed constitutively in pancreas. EMBO J 6:3711-3717.
    • (1987) EMBO J , vol.6 , pp. 3711-3717
    • Mills, J.S.1    Needham, M.2    Parker, M.G.3
  • 22
    • 0032883785 scopus 로고    scopus 로고
    • A homologue of pancreatic trypsin is localized in the acrosome of mammalian sperm and is released during acrosome reaction
    • DOI 10.1074/jbc.274.41.29426
    • Ohmura K, Kohno N, Kobayashi Y, Yamagata K, Sato S, Kashiwabara S, Baba T. 1999. A homologue of pancreatic trypsin is localized in the acrosome of mammalian sperm and is released during acrosome reaction. J Biol Chem 274:29426-29432. (Pubitemid 29477114)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.41 , pp. 29426-29432
    • Ohmura, K.1    Kohno, N.2    Kobayashi, Y.3    Yamagata, K.4    Sato, S.5    Kashiwabara, S.-I.6    Baba, T.7
  • 23
    • 0019722350 scopus 로고
    • Isolation and characterization of two proteinase inhibitors from the male reproductive tract of mice
    • DOI 10.1002/mrd.1120040609
    • Poirier GR, Jackson J. 1981. Isolation and characterization of two proteinase inhibitors from the male reproductive tract of mice. Gamete Res 4:555-569. (Pubitemid 12056421)
    • (1981) Gamete Research , vol.4 , Issue.6 , pp. 555-569
    • Poirier, G.R.1    Jackson, J.2
  • 24
    • 1642464622 scopus 로고    scopus 로고
    • Evolutionary families of peptidase inhibitors
    • Rawlings ND, Tolle DP, Barrett AJ. 2004. Evolutionary families of peptidase inhibitors. Biochem J 378:705-716.
    • (2004) Biochem J , vol.378 , pp. 705-716
    • Rawlings, N.D.1    Tolle, D.P.2    Barrett, A.J.3
  • 25
    • 0021915292 scopus 로고
    • Evaluation of the human sperm proacrosinacrosin system using gelatin-sodium dodecyl sulfate-polyacrylamide gel electrophesis
    • Siegel MS, Polakoski KL. 1985. Evaluation of the human sperm proacrosinacrosin system using gelatin-sodium dodecyl sulfate-polyacrylamide gel electrophesis. Biol Reprod 32:713-720.
    • (1985) Biol Reprod , vol.32 , pp. 713-720
    • Siegel, M.S.1    Polakoski, K.L.2
  • 26
    • 0029836135 scopus 로고    scopus 로고
    • The initial molecular interaction between mouse sperm and the zona pellucida is a complex binding event
    • Thaler CD, Cardullo RA. 1996. The initial molecular interaction between mouse sperm and the zona pellucida is a complex binding event. J Biol Chem 271:23289-23297.
    • (1996) J Biol Chem , vol.271 , pp. 23289-23297
    • Thaler, C.D.1    Cardullo, R.A.2
  • 27
    • 0020429613 scopus 로고
    • A new acrosin inhibitor from boar spermatozoa
    • DOI 10.1111/j.1432-1033.1982.tb06752.x
    • Tschesche H, Wittig B, Decker G, Muller-Esterl W, Fritz H. 1982. A new acrosin inhibitor from boar spermatozoa. Eur J Biochem 126:99-104. (Pubitemid 13231144)
    • (1982) European Journal of Biochemistry , vol.126 , Issue.1 , pp. 99-104
    • Tschesche, H.1    Wittig, B.2    Decker, G.3
  • 28
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne G. 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res 14:4683-4690.
    • (1986) Nucleic Acids Res , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 29
    • 0034848170 scopus 로고    scopus 로고
    • DAMBE: Software package for data analysis in molecular biology and evolution
    • Xia X, Xie Z. 2001. DAMBE: Software package for data analysis in molecular biology and evolution. J Hered 92:371-373. (Pubitemid 32848767)
    • (2001) Journal of Heredity , vol.92 , Issue.4 , pp. 371-373
    • Xia, X.1    Xie, Z.2
  • 30
    • 0015071907 scopus 로고
    • Inhibition of fertilization in vivo by pancreatic and seminal plasma trypsin inhibitors
    • Zaneveld LJ, Robertson RT, Kessler M, Williams WL. 1971. Inhibition of fertilization in vivo by pancreatic and seminal plasma trypsin inhibitors. J Reprod Fertil 25:387-392.
    • (1971) J Reprod Fertil , vol.25 , pp. 387-392
    • Zaneveld, L.J.1    Robertson, R.T.2    Kessler, M.3    Williams, W.L.4


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