메뉴 건너뛰기




Volumn 272, Issue 1, 2004, Pages 191-202

Proteolytic cleavage of the cell surface protein p160 is required for detachment of the fertilization envelope in the sea urchin

Author keywords

artificial sea water; ASW; Block to polyspermy; CGSP1; cortical granule serine protease; dithiothreitol; DTT; Egg; FE; Fertilization; fertilization envelope; Protease; SBTI; Sea urchin; soybean trypsin inhibitor; Strongylocentrotus purpuratus; Vitelline layer

Indexed keywords

AMINO ACID; CELL SURFACE PROTEIN; COMPLEMENTARY DNA; MEMBRANE PROTEIN; PROTEIN P160; SERINE PROTEINASE;

EID: 3042740984     PISSN: 00121606     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ydbio.2004.03.043     Document Type: Article
Times cited : (22)

References (45)
  • 1
    • 0022397028 scopus 로고
    • Characterization of soybean trypsin inhibitor sensitive protease from unfertilized sea urchin eggs
    • Alliegro M.C., Schuel H. Characterization of soybean trypsin inhibitor sensitive protease from unfertilized sea urchin eggs. Biochemistry. 24:1985;3926-3931
    • (1985) Biochemistry , vol.24 , pp. 3926-3931
    • Alliegro, M.C.1    Schuel, H.2
  • 2
    • 0023901540 scopus 로고
    • Immunocytochemical localization of the 35-kDa sea urchin egg trypsin-like protease and its effects upon the egg surface
    • Alliegro M.C., Schuel H. Immunocytochemical localization of the 35-kDa sea urchin egg trypsin-like protease and its effects upon the egg surface. Dev. Biol. 125:1988;168-180
    • (1988) Dev. Biol. , vol.125 , pp. 168-180
    • Alliegro, M.C.1    Schuel, H.2
  • 5
    • 0027190974 scopus 로고
    • The CUB domain. a widespread module in developmentally regulated proteins
    • Bork P., Beckmann G. The CUB domain. A widespread module in developmentally regulated proteins. J. Mol. Biol. 231:1993;539-545
    • (1993) J. Mol. Biol. , vol.231 , pp. 539-545
    • Bork, P.1    Beckmann, G.2
  • 6
    • 0031780826 scopus 로고    scopus 로고
    • The apical lamina and its role in cell adhesion in sea urchin embryos
    • Burke R.D., Lail M., Nakajima Y. The apical lamina and its role in cell adhesion in sea urchin embryos. Cell Adhes. Commun. 5:1998;97-108
    • (1998) Cell Adhes. Commun. , vol.5 , pp. 97-108
    • Burke, R.D.1    Lail, M.2    Nakajima, Y.3
  • 7
    • 0346362278 scopus 로고    scopus 로고
    • Integrins on eggs: The βc subunit is essential for formation of the cortical actin cytoskeleton in sea urchin eggs
    • Burke R.D., Murray G., Rise M., Wang D. Integrins on eggs: the βC subunit is essential for formation of the cortical actin cytoskeleton in sea urchin eggs. Dev. Biol. 265:2004;53-60
    • (2004) Dev. Biol. , vol.265 , pp. 53-60
    • Burke, R.D.1    Murray, G.2    Rise, M.3    Wang, D.4
  • 8
    • 0016759504 scopus 로고
    • Isolation and biological activity of the proteases released by sea urchin eggs following fertilization
    • Carroll E.J. Jr., Epel D. Isolation and biological activity of the proteases released by sea urchin eggs following fertilization. Dev. Biol. 44:1975;22-32
    • (1975) Dev. Biol. , vol.44 , pp. 22-32
    • Carroll Jr., E.J.1    Epel, D.2
  • 9
    • 0019817763 scopus 로고
    • Reevaluation of cell surface protein release at fertilization and its role in regulation of sea urchin egg protein synthesis
    • Carroll E.J., Epel D. Reevaluation of cell surface protein release at fertilization and its role in regulation of sea urchin egg protein synthesis. Dev. Biol. 87:1981;374-378
    • (1981) Dev. Biol. , vol.87 , pp. 374-378
    • Carroll, E.J.1    Epel, D.2
  • 10
    • 0029123214 scopus 로고
    • Proteases stimulate fertilization-like responses in starfish eggs
    • Carroll D.J., Jaffe L.A. Proteases stimulate fertilization-like responses in starfish eggs. Dev. Biol. 170:1995;690-700
    • (1995) Dev. Biol. , vol.170 , pp. 690-700
    • Carroll, D.J.1    Jaffe, L.A.2
  • 12
    • 0022343703 scopus 로고
    • In vitro reconstitution of exocytosis from plasma membrane and isolated secretory vesicles
    • Crabb J.H., Jackson R.C. In vitro reconstitution of exocytosis from plasma membrane and isolated secretory vesicles. J. Cell Biol. 101:1985;2263-2273
    • (1985) J. Cell Biol. , vol.101 , pp. 2263-2273
    • Crabb, J.H.1    Jackson, R.C.2
  • 13
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:1984;387-395
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 14
    • 0014819058 scopus 로고
    • Methods for removal of the vitelline membrane of sea urchin eggs: I. Use of dithiothreitol (Cleland Reagent)
    • Epel D., Weaver A.M., Mazia D. Methods for removal of the vitelline membrane of sea urchin eggs: I. Use of dithiothreitol (Cleland Reagent). Exp. Cell Res. 61:1970;64-68
    • (1970) Exp. Cell Res. , vol.61 , pp. 64-68
    • Epel, D.1    Weaver, A.M.2    Mazia, D.3
  • 15
    • 0028929353 scopus 로고
    • Identification and localization of integrin subunits in oocytes and eggs of the mouse
    • Evans J.P., Schultz R.M., Kopf G.S. Identification and localization of integrin subunits in oocytes and eggs of the mouse. Mol. Reprod. Dev. 40:1995;211-220
    • (1995) Mol. Reprod. Dev. , vol.40 , pp. 211-220
    • Evans, J.P.1    Schultz, R.M.2    Kopf, G.S.3
  • 16
    • 0016843022 scopus 로고
    • Isolation of a protease from sea urchin eggs before and after fertilization
    • Fodor E.J., Ako H., Walsh K.A. Isolation of a protease from sea urchin eggs before and after fertilization. Biochemistry. 14:1975;4923-4927
    • (1975) Biochemistry , vol.14 , pp. 4923-4927
    • Fodor, E.J.1    Ako, H.2    Walsh, K.A.3
  • 17
    • 0344705266 scopus 로고
    • Studies on polyspermy in sea urchins
    • Hagström B.E. Studies on polyspermy in sea urchins. Ark. Zool. 10:1956;307-315
    • (1956) Ark. Zool. , vol.10 , pp. 307-315
    • Hagström, B.E.1
  • 18
    • 0033168970 scopus 로고    scopus 로고
    • The cortical granule serine protease CGSP1 of the sea urchin, Strongylocentrotus purpuratus, is autocatalytic and contains a low-density lipoprotein receptor-like domain
    • Haley S.A., Wessel G.M. The cortical granule serine protease CGSP1 of the sea urchin, Strongylocentrotus purpuratus, is autocatalytic and contains a low-density lipoprotein receptor-like domain. Dev. Biol. 211:1999;1-10
    • (1999) Dev. Biol. , vol.211 , pp. 1-10
    • Haley, S.A.1    Wessel, G.M.2
  • 20
    • 0037442567 scopus 로고    scopus 로고
    • None of the integrins known to be present on the mouse egg or to be ADAM receptors are essential for sperm-egg binding and fusion
    • He Z.Y., Brakebusch C., Fassler R., Kreidberg J.A., Primakoff P., Myles D.G. None of the integrins known to be present on the mouse egg or to be ADAM receptors are essential for sperm-egg binding and fusion. Dev. Biol. 254:2003;226-237
    • (2003) Dev. Biol. , vol.254 , pp. 226-237
    • He, Z.Y.1    Brakebusch, C.2    Fassler, R.3    Kreidberg, J.A.4    Primakoff, P.5    Myles, D.G.6
  • 21
    • 0032387736 scopus 로고    scopus 로고
    • The 350-kDa sea urchin egg receptor for sperm is localized in the vitelline layer
    • Hirohashi N., Lennarz W.J. The 350-kDa sea urchin egg receptor for sperm is localized in the vitelline layer. Dev. Biol. 204:1998;305-315
    • (1998) Dev. Biol. , vol.204 , pp. 305-315
    • Hirohashi, N.1    Lennarz, W.J.2
  • 22
    • 0016825870 scopus 로고
    • Relationship between release of surface proteins and metabolic activation of sea urchin eggs at fertilization
    • Johnson J.D., Epel D. Relationship between release of surface proteins and metabolic activation of sea urchin eggs at fertilization. Proc. Natl. Acad. Sci. U. S. A. 72:1975;4474-4478
    • (1975) Proc. Natl. Acad. Sci. U. S. A. , vol.72 , pp. 4474-4478
    • Johnson, J.D.1    Epel, D.2
  • 23
    • 0022921590 scopus 로고
    • Cloning and sequencing of full-length cDNA encoding the precursor of human complement component C1r
    • Journet A., Tosi M. Cloning and sequencing of full-length cDNA encoding the precursor of human complement component C1r. Biochem. J. 240:1986;783-787
    • (1986) Biochem. J. , vol.240 , pp. 783-787
    • Journet, A.1    Tosi, M.2
  • 24
    • 0022609883 scopus 로고
    • Purification and properties of the egg plasma membrane
    • Kinsey W.H. Purification and properties of the egg plasma membrane. Methods Cell Biol. 27:1986;139-152
    • (1986) Methods Cell Biol. , vol.27 , pp. 139-152
    • Kinsey, W.H.1
  • 25
    • 0028351952 scopus 로고
    • Cortical granule biogenesis is active throughout oogenesis in sea urchins
    • Laidlaw M., Wessel G.M. Cortical granule biogenesis is active throughout oogenesis in sea urchins. Development. 120:1994;1325-1333
    • (1994) Development , vol.120 , pp. 1325-1333
    • Laidlaw, M.1    Wessel, G.M.2
  • 26
    • 0026019881 scopus 로고
    • Fertilization-induced changes in the vitelline envelope of echinoderm and amphibian eggs: Self-assembly of an extracellular matrix
    • Larabell C., Chandler D.E. Fertilization-induced changes in the vitelline envelope of echinoderm and amphibian eggs: self-assembly of an extracellular matrix. J. Electron Microsc. Tech. 17:1991;294-318
    • (1991) J. Electron Microsc. Tech. , vol.17 , pp. 294-318
    • Larabell, C.1    Chandler, D.E.2
  • 28
    • 0022480853 scopus 로고
    • On the role of calcium in the adhesion of embryonic sea urchin cells
    • McClay D.R., Matranga V. On the role of calcium in the adhesion of embryonic sea urchin cells. Exp. Cell Res. 165:1986;152-164
    • (1986) Exp. Cell Res. , vol.165 , pp. 152-164
    • McClay, D.R.1    Matranga, V.2
  • 29
    • 0025797507 scopus 로고
    • Evidence for the existence of two assembly domains within the sea urchin fertilization envelope
    • Mozingo N.M., Chandler D.E. Evidence for the existence of two assembly domains within the sea urchin fertilization envelope. Dev. Biol. 146:1991;148-157
    • (1991) Dev. Biol. , vol.146 , pp. 148-157
    • Mozingo, N.M.1    Chandler, D.E.2
  • 30
    • 0034668390 scopus 로고    scopus 로고
    • The αbβC integrin is expressed on the surface of the sea urchin egg and removed at fertilization
    • Murray G., Reed C., Marsden M., Rise M., Wang D., Burke R.D. The αBβC integrin is expressed on the surface of the sea urchin egg and removed at fertilization. Dev. Biol. 227:2000;633-647
    • (2000) Dev. Biol. , vol.227 , pp. 633-647
    • Murray, G.1    Reed, C.2    Marsden, M.3    Rise, M.4    Wang, D.5    Burke, R.D.6
  • 33
    • 0028024865 scopus 로고
    • Developmental expression of the sea urchin egg receptor for sperm
    • Ohlendieck K., Partin J.S., Stears R.L., Lennarz W.J. Developmental expression of the sea urchin egg receptor for sperm. Dev. Biol. 165:1994;53-62
    • (1994) Dev. Biol. , vol.165 , pp. 53-62
    • Ohlendieck, K.1    Partin, J.S.2    Stears, R.L.3    Lennarz, W.J.4
  • 35
    • 0015812265 scopus 로고
    • A trypsin-like proteinase localized in cortical granules isolated from unfertilized sea urchin eggs by zonal centrifugation. Role of the enzyme in fertilization
    • Schuel H., Wilson W.L., Chen K., Lorand L. A trypsin-like proteinase localized in cortical granules isolated from unfertilized sea urchin eggs by zonal centrifugation. Role of the enzyme in fertilization. Dev. Biol. 34:1973;175-186
    • (1973) Dev. Biol. , vol.34 , pp. 175-186
    • Schuel, H.1    Wilson, W.L.2    Chen, K.3    Lorand, L.4
  • 36
    • 0016829916 scopus 로고
    • Limited proteolysis of some egg surface components is an early event following fertilization of the sea urchin, Strongylocentrotus purpuratus
    • Shapiro B.M. Limited proteolysis of some egg surface components is an early event following fertilization of the sea urchin, Strongylocentrotus purpuratus. Dev. Biol. 46:1975;88-102
    • (1975) Dev. Biol. , vol.46 , pp. 88-102
    • Shapiro, B.M.1
  • 37
    • 0002412281 scopus 로고
    • Extracellular remodeling during fertilization
    • H. Schatten, & G. Schatten. San Diego: Academic Press
    • Shapiro B.M., Somers C., Weidman P.J. Extracellular remodeling during fertilization. Schatten H., Schatten G. Cell Biology of Fertilization. 1989;251-276 Academic Press, San Diego
    • (1989) Cell Biology of Fertilization , pp. 251-276
    • Shapiro, B.M.1    Somers, C.2    Weidman, P.J.3
  • 38
    • 0025986820 scopus 로고
    • The Drosophila dorsal-ventral patterning gene tolloid is related to human bone morphogenetic protein 1
    • Shimell M.J., Ferguson E.L., Childs S.R., O'Connor M.B. The Drosophila dorsal-ventral patterning gene tolloid is related to human bone morphogenetic protein 1. Cell. 67:1991;469-481
    • (1991) Cell , vol.67 , pp. 469-481
    • Shimell, M.J.1    Ferguson, E.L.2    Childs, S.R.3    O'Connor, M.B.4
  • 39
    • 0014444144 scopus 로고
    • A low viscosity epoxy resin embedding medium for electron microscopy
    • Spurr A. A low viscosity epoxy resin embedding medium for electron microscopy. J. Ultrastruct. Res. 26:1969;31-43
    • (1969) J. Ultrastruct. Res. , vol.26 , pp. 31-43
    • Spurr, A.1
  • 42
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76:1979;4350-4354
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 43
    • 0015494806 scopus 로고
    • Sea urchin eggs release protease activity at fertilization
    • Vacquier V.D., Epel D., Douglas L.A. Sea urchin eggs release protease activity at fertilization. Nature. 237:1972;34-36
    • (1972) Nature , vol.237 , pp. 34-36
    • Vacquier, V.D.1    Epel, D.2    Douglas, L.A.3
  • 44
    • 0015498753 scopus 로고
    • Protease activity establishes the block against polyspermy in sea urchin eggs
    • Vacquier V.D., Tegner M.J., Epel D. Protease activity establishes the block against polyspermy in sea urchin eggs. Nature. 240:1972;352-353
    • (1972) Nature , vol.240 , pp. 352-353
    • Vacquier, V.D.1    Tegner, M.J.2    Epel, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.