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Volumn 139, Issue 2, 2004, Pages 157-162

Effects of proteinase inhibitors on fertilization in sea lamprey (Petromyzon marinus)

Author keywords

Chymotrypsin; Fertilization; Fish eggs; Inhibitors; Proteinase; Sea lamprey; Spermatozoa; Sterilization

Indexed keywords

BENZOIC ACID DERIVATIVE; CHYMOSTATIN; PROTEINASE INHIBITOR; SERINE PROTEINASE; TOSYLLYSYL CHLOROMETHYL KETONE; TOSYLPHENYLALANYL CHLOROMETHYL KETONE;

EID: 4644230511     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2004.06.010     Document Type: Article
Times cited : (4)

References (33)
  • 2
    • 0028119151 scopus 로고
    • Identification of trypsin-like activity in sturgeon spermatozoa
    • A. Ciereszko, K. Dabrowski, F. Lin, and S.I. Doroshov Identification of trypsin-like activity in sturgeon spermatozoa J. Exp. Zool. 268 1994 486 491
    • (1994) J. Exp. Zool. , vol.268 , pp. 486-491
    • Ciereszko, A.1    Dabrowski, K.2    Lin, F.3    Doroshov, S.I.4
  • 3
    • 0029763097 scopus 로고    scopus 로고
    • Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa
    • A. Ciereszko, K. Dabrowski, and S.I. Ochkur Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa Mol. Reprod. Dev. 45 1996 72 77
    • (1996) Mol. Reprod. Dev. , vol.45 , pp. 72-77
    • Ciereszko, A.1    Dabrowski, K.2    Ochkur, S.I.3
  • 4
    • 0034020202 scopus 로고    scopus 로고
    • Characteristics of sperm acrosin-like activity of paddlefish (Polyodon spathula Walbaum)
    • A. Ciereszko, K. Dabrowski, S.D. Mims, and J. Glogowski Characteristics of sperm acrosin-like activity of paddlefish (Polyodon spathula Walbaum) Comp. Biochem. Physiol., B 125 2000 197 203
    • (2000) Comp. Biochem. Physiol., B , vol.125 , pp. 197-203
    • Ciereszko, A.1    Dabrowski, K.2    Mims, S.D.3    Glogowski, J.4
  • 5
    • 0033864289 scopus 로고    scopus 로고
    • Fertilization in landlocked sea lamprey: Storage of gametes, optimal sperm:egg ratio, and methods for assessing fertilization success
    • A. Ciereszko, J. Glogowski, and K. Dabrowski Fertilization in landlocked sea lamprey: storage of gametes, optimal sperm:egg ratio, and methods for assessing fertilization success J. Fish Biol. 56 2000 495 505
    • (2000) J. Fish Biol. , vol.56 , pp. 495-505
    • Ciereszko, A.1    Glogowski, J.2    Dabrowski, K.3
  • 7
    • 0024383340 scopus 로고
    • Inhibition of the human sperm acrosome reaction by proteinase inhibitors
    • C.J. De Jonge, S.R. Mack, and L.J.D. Zaneveld Inhibition of the human sperm acrosome reaction by proteinase inhibitors Gamete Res. 23 1989 387 397
    • (1989) Gamete Res. , vol.23 , pp. 387-397
    • De Jonge, C.J.1    MacK, S.R.2    Zaneveld, L.J.D.3
  • 9
    • 0000015423 scopus 로고
    • The general biology of adult lampreys
    • M.W. Hardisty I.C. Potter Academic Press New York
    • M.W. Hardisty, and I.C. Potter The general biology of adult lampreys M.W. Hardisty I.C. Potter The Biology of Lampreys 1971 Academic Press New York 1 66
    • (1971) The Biology of Lampreys , pp. 1-66
    • Hardisty, M.W.1    Potter, I.C.2
  • 10
    • 0036267547 scopus 로고    scopus 로고
    • Interactions between zona pellucida glycoproteins and sperm proacrosin/acrosin during fertilization
    • L. Howes, and R. Jones Interactions between zona pellucida glycoproteins and sperm proacrosin/acrosin during fertilization J. Reprod. Immunol. 53 2002 181 192
    • (2002) J. Reprod. Immunol. , vol.53 , pp. 181-192
    • Howes, L.1    Jones, R.2
  • 11
    • 0002954811 scopus 로고
    • The ultrastructure of spermatozoa with a note on the formation of the acrosomal filaments in the lamprey
    • H. Jaana, and T.S. Yamamoto The ultrastructure of spermatozoa with a note on the formation of the acrosomal filaments in the lamprey Jpn. J. Ichthyol. 28 1981 135 147
    • (1981) Jpn. J. Ichthyol. , vol.28 , pp. 135-147
    • Jaana, H.1    Yamamoto, T.S.2
  • 15
    • 0028042794 scopus 로고
    • Fertilization in the lamprey (Lampetra japonica) eggs: Implication of the presence of fast and permanent blocks against polyspermy
    • W. Kobayashi, and T.S. Yamamoto Fertilization in the lamprey (Lampetra japonica) eggs: implication of the presence of fast and permanent blocks against polyspermy J. Exp. Zool. 269 1994 166 176
    • (1994) J. Exp. Zool. , vol.269 , pp. 166-176
    • Kobayashi, W.1    Yamamoto, T.S.2
  • 16
    • 0028349681 scopus 로고
    • Sperm-surface chymotrypsin-like protease activity required for fertilization in ascidians
    • R.A. Koch, M.L. Norton, H. Vázquez, and C.C. Lambert Sperm-surface chymotrypsin-like protease activity required for fertilization in ascidians Dev. Biol. 162 1994 438 450
    • (1994) Dev. Biol. , vol.162 , pp. 438-450
    • Koch, R.A.1    Norton, M.L.2    Vázquez, H.3    Lambert, C.C.4
  • 17
    • 0002534245 scopus 로고
    • Fertilization of sea lamprey eggs
    • R.A. Kille Fertilization of sea lamprey eggs Exp. Cell Res. 20 1960 12 27
    • (1960) Exp. Cell Res. , vol.20 , pp. 12-27
    • Kille, R.A.1
  • 18
    • 0028927831 scopus 로고
    • Isolation and characterization of ovochymase, a chymotrypsin-like protease released during Xenopus laevis egg activation
    • L.L. Lindsay, and J.L. Hedrick Isolation and characterization of ovochymase, a chymotrypsin-like protease released during Xenopus laevis egg activation Dev. Biol. 167 1995 513 516
    • (1995) Dev. Biol. , vol.167 , pp. 513-516
    • Lindsay, L.L.1    Hedrick, J.L.2
  • 19
    • 0026484831 scopus 로고
    • Localization of a chymotrypsin-like protease to the perivitelline space of Xenopus laevis eggs
    • L.L. Lindsay, C.A. Larabell, and J.L. Hedrick Localization of a chymotrypsin-like protease to the perivitelline space of Xenopus laevis eggs Dev. Biol. 154 1992 433 436
    • (1992) Dev. Biol. , vol.154 , pp. 433-436
    • Lindsay, L.L.1    Larabell, C.A.2    Hedrick, J.L.3
  • 20
    • 0033613248 scopus 로고    scopus 로고
    • Ovochymase, a Xenopus laevis egg extracellular protease, is translated as part of an unusual polyprotease
    • L.L. Lindsay, J.C. Yang, and J.L. Hedrick Ovochymase, a Xenopus laevis egg extracellular protease, is translated as part of an unusual polyprotease Proc. Natl. Acad. Sci. U. S. A. 96 1999 11253 11258
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 11253-11258
    • Lindsay, L.L.1    Yang, J.C.2    Hedrick, J.L.3
  • 21
    • 0032981826 scopus 로고    scopus 로고
    • Oviduction, the Xenopus laevis oviductal protease that processes egg envelope glycoprotein gp43, increases sperm binding to envelopes, and is translated as part of an unusual mosaic protein composed of two proteases and several CUB domains
    • L.L. Lindsay, M.J. Wieduwilt, and J.L. Hedrick Oviduction, the Xenopus laevis oviductal protease that processes egg envelope glycoprotein gp43, increases sperm binding to envelopes, and is translated as part of an unusual mosaic protein composed of two proteases and several CUB domains Biol. Reprod. 60 1999 989 995
    • (1999) Biol. Reprod. , vol.60 , pp. 989-995
    • Lindsay, L.L.1    Wieduwilt, M.J.2    Hedrick, J.L.3
  • 22
    • 0024695433 scopus 로고
    • 2+ channels during the acrosome reaction of sea urchin sperm is inhibited by inhibitors of chymotrypsin-like proteases
    • 2+ channels during the acrosome reaction of sea urchin sperm is inhibited by inhibitors of chymotrypsin-like proteases Gamete Res. 23 1989 255 266
    • (1989) Gamete Res. , vol.23 , pp. 255-266
    • Matsumara, K.1    Aketa, K.2
  • 23
    • 0025764331 scopus 로고
    • Proteasome (multicatalytic proteinase) of sea urchin sperm and its possible participation in the acrosome reaction
    • K. Matsumara, and K. Aketa Proteasome (multicatalytic proteinase) of sea urchin sperm and its possible participation in the acrosome reaction Mol. Reprod. Dev. 29 1991 189 199
    • (1991) Mol. Reprod. Dev. , vol.29 , pp. 189-199
    • Matsumara, K.1    Aketa, K.2
  • 24
    • 0028276054 scopus 로고
    • Evidences for the presence of chymotrypsin-like activity in human spermatozoa with a role on the acrosome reaction
    • P. Morales, T. Socias, J. Cortez, and M.N. Llanos Evidences for the presence of chymotrypsin-like activity in human spermatozoa with a role on the acrosome reaction Mol. Reprod. Dev. 38 1994 222 230
    • (1994) Mol. Reprod. Dev. , vol.38 , pp. 222-230
    • Morales, P.1    Socias, T.2    Cortez, J.3    Llanos, M.N.4
  • 25
    • 0000054905 scopus 로고
    • An electron microscopical study of the acrosomal complex and its role in fertilization in the river lamprey, Lampetra fluviatilis
    • L. Nicander, and I. Sjödén An electron microscopical study of the acrosomal complex and its role in fertilization in the river lamprey, Lampetra fluviatilis J. Submicrosc. Cytol. 3 1971 309 317
    • (1971) J. Submicrosc. Cytol. , vol.3 , pp. 309-317
    • Nicander, L.1    Sjödén, I.2
  • 26
    • 0025143682 scopus 로고
    • Chymotrypsin-like enzymes are involved in sperm penetration through the vitelline coat of Ciona intestinalis eggs
    • M.R. Pinto, M. Hoshi, R. Marino, A. Amoroso, and R. De Santis Chymotrypsin-like enzymes are involved in sperm penetration through the vitelline coat of Ciona intestinalis eggs Mol. Reprod. Dev. 26 1990 319 323
    • (1990) Mol. Reprod. Dev. , vol.26 , pp. 319-323
    • Pinto, M.R.1    Hoshi, M.2    Marino, R.3    Amoroso, A.4    De Santis, R.5
  • 27
    • 0036348395 scopus 로고    scopus 로고
    • Ascidian sperm lysine system
    • H. Sawada Ascidian sperm lysine system Zool. Sci. 19 2002 139 151
    • (2002) Zool. Sci. , vol.19 , pp. 139-151
    • Sawada, H.1
  • 28
    • 0026831439 scopus 로고
    • Presence of trypsin-like protease in starfish sperm acrosome
    • M. Sousa, P. Morades-Ferreira, and C. Azevedo Presence of trypsin-like protease in starfish sperm acrosome J. Exp. Zool. 261 1992 349 354
    • (1992) J. Exp. Zool. , vol.261 , pp. 349-354
    • Sousa, M.1    Morades-Ferreira, P.2    Azevedo, C.3
  • 29
    • 0027917966 scopus 로고
    • Effect of protease inhibitors on binding of sperm to the vitelline coat of ascidian eggs: Implications for participation of proteasome (multicatalytic proteinases complex)
    • S. Takizawa, H. Sawada, T. Someno, Y. Saitoh, H. Yokosawa, and M. Hoshi Effect of protease inhibitors on binding of sperm to the vitelline coat of ascidian eggs: implications for participation of proteasome (multicatalytic proteinases complex) J. Exp. Zool. 267 1993 86 91
    • (1993) J. Exp. Zool. , vol.267 , pp. 86-91
    • Takizawa, S.1    Sawada, H.2    Someno, T.3    Saitoh, Y.4    Yokosawa, H.5    Hoshi, M.6
  • 30
    • 0001826169 scopus 로고
    • Mammalian sperm acrosome enzymes and the acrosome reaction
    • B.S. Dunbar M.G. O'Rand Plenum New York
    • L.J.D. Zaneveld, and C.J. De Jonge Mammalian sperm acrosome enzymes and the acrosome reaction B.S. Dunbar M.G. O'Rand A Comparative Overview of Mammalian Fertilization 1991 Plenum New York 63 79
    • (1991) A Comparative Overview of Mammalian Fertilization , pp. 63-79
    • Zaneveld, L.J.D.1    De Jonge, C.J.2
  • 31
    • 0020092339 scopus 로고
    • Purification and characterization of chymotrypsin-like enzyme from sperm of the sea urchin, Hemicentrotus pulcherrimus
    • Y. Yamada, T. Matsui, and K. Aketa Purification and characterization of chymotrypsin-like enzyme from sperm of the sea urchin, Hemicentrotus pulcherrimus Eur. J. Biochem. 122 1982 57 62
    • (1982) Eur. J. Biochem. , vol.122 , pp. 57-62
    • Yamada, Y.1    Matsui, T.2    Aketa, K.3
  • 32
    • 0032197525 scopus 로고    scopus 로고
    • Aminobenzamidine-sensitive acrosomal protease(s) other than acrosin serve the sperm penetration of the egg zona pellucida in mouse
    • K. Yamagata, K. Murayama, N. Kohono, S. Kashiwabara, and T. Baba Aminobenzamidine-sensitive acrosomal protease(s) other than acrosin serve the sperm penetration of the egg zona pellucida in mouse Zygote 6 1998 311 319
    • (1998) Zygote , vol.6 , pp. 311-319
    • Yamagata, K.1    Murayama, K.2    Kohono, N.3    Kashiwabara, S.4    Baba, T.5
  • 33
    • 0023655745 scopus 로고
    • Sperm chymotrypsin-like enzymes of different inhibitor-susceptibility as lysins in ascidians
    • H. Yokosawa, T. Numakunai, S. Murao, and S. Ishii Sperm chymotrypsin-like enzymes of different inhibitor-susceptibility as lysins in ascidians Experientia 43 1987 925 927
    • (1987) Experientia , vol.43 , pp. 925-927
    • Yokosawa, H.1    Numakunai, T.2    Murao, S.3    Ishii, S.4


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