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Volumn 261, Issue 2, 2003, Pages 353-370

Selective transport and packaging of the major yolk protein in the sea urchin

Author keywords

Endocytosis; Major yolk protein (MYP); Oogenesis; Sea urchin; Vitellogenesis; Yolk platelet

Indexed keywords

YOLK PROTEIN;

EID: 0041384519     PISSN: 00121606     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0012-1606(03)00301-4     Document Type: Article
Times cited : (37)

References (52)
  • 1
    • 0033630506 scopus 로고    scopus 로고
    • Varied effects of 1-octanol on gap junctional communication between ovarian epithelial cells and oocytes of Oncopeltus fasciatus, Hyalophora cecropia, and Drosophila melanogaster
    • Adler E.L., Woodruff R.I. Varied effects of 1-octanol on gap junctional communication between ovarian epithelial cells and oocytes of Oncopeltus fasciatus, Hyalophora cecropia, and Drosophila melanogaster. Arch. Insect Biochem. Physiol. 43:2000;22-32.
    • (2000) Arch. Insect Biochem. Physiol. , vol.43 , pp. 22-32
    • Adler, E.L.1    Woodruff, R.I.2
  • 2
    • 0015060029 scopus 로고
    • Protein synthesis and uptake by isolated Cecropia oocytes
    • Anderson L.M. Protein synthesis and uptake by isolated Cecropia oocytes. J. Cell Sci. 8:1971;735-750.
    • (1971) J. Cell Sci. , vol.8 , pp. 735-750
    • Anderson, L.M.1
  • 3
    • 0026646617 scopus 로고
    • New perspectives on the structure and function of transferrins
    • Baker E.N., Lindley P.F. New perspectives on the structure and function of transferrins. J. Inorg. Biochem. 47:1992;147-160.
    • (1992) J. Inorg. Biochem. , vol.47 , pp. 147-160
    • Baker, E.N.1    Lindley, P.F.2
  • 4
    • 0034212198 scopus 로고    scopus 로고
    • Evidence for direct membrane retrieval following cortical granule exocytosis in Xenopus oocytes and eggs
    • Bement W.M., Benink H., Mandato C.A., Swelstad B.B. Evidence for direct membrane retrieval following cortical granule exocytosis in Xenopus oocytes and eggs. J. Exp. Zool. 286:2000;767-775.
    • (2000) J. Exp. Zool. , vol.286 , pp. 767-775
    • Bement, W.M.1    Benink, H.2    Mandato, C.A.3    Swelstad, B.B.4
  • 5
    • 0033512348 scopus 로고    scopus 로고
    • New perspectives on iron: An introduction
    • Boldt D.H. New perspectives on iron an introduction . Am. J. Med. Sci. 318:1999;207-212.
    • (1999) Am. J. Med. Sci. , vol.318 , pp. 207-212
    • Boldt, D.H.1
  • 6
    • 0026655197 scopus 로고
    • Why is there sequence similarity between insect yolk proteins and vertebrate lipases?
    • Bownes M. Why is there sequence similarity between insect yolk proteins and vertebrate lipases? J. Lipid Res. 33:1992;777-790.
    • (1992) J. Lipid Res. , vol.33 , pp. 777-790
    • Bownes, M.1
  • 8
    • 0036570143 scopus 로고    scopus 로고
    • The major yolk protein in sea urchins is a transferrin-like, iron binding protein
    • Brooks J.M., Wessel G.M. The major yolk protein in sea urchins is a transferrin-like, iron binding protein. Dev. Biol. 245:2002;1-12.
    • (2002) Dev. Biol. , vol.245 , pp. 1-12
    • Brooks, J.M.1    Wessel, G.M.2
  • 9
    • 0024443044 scopus 로고
    • Pathway and kinetics of vitellogenin-gold internalization in the Xenopus oocyte
    • Busson S., Ovtracht L., Gounon P. Pathway and kinetics of vitellogenin-gold internalization in the Xenopus oocyte. Biol. Cell. 67:1989;37-49.
    • (1989) Biol. Cell , vol.67 , pp. 37-49
    • Busson, S.1    Ovtracht, L.2    Gounon, P.3
  • 11
    • 0030934540 scopus 로고    scopus 로고
    • Extensive sequence conservation among insect, nematode, and vertebrate vitellogenins reveals ancient common ancestry
    • Chen J.S., Sappington T.W., Raikhel A.S. Extensive sequence conservation among insect, nematode, and vertebrate vitellogenins reveals ancient common ancestry. J. Mol. Evol. 44:1997;440-451.
    • (1997) J. Mol. Evol. , vol.44 , pp. 440-451
    • Chen, J.S.1    Sappington, T.W.2    Raikhel, A.S.3
  • 12
    • 0041722856 scopus 로고
    • The volumes occupied by the formed cytoplasmic components in marine eggs
    • Costello D.P. The volumes occupied by the formed cytoplasmic components in marine eggs. Physiol. Zool. 12:1939;13-20.
    • (1939) Physiol. Zool. , vol.12 , pp. 13-20
    • Costello, D.P.1
  • 13
    • 0023267213 scopus 로고
    • Differentiation of the animal-vegetal axis in Xenopus laevis oocytes. I. Polarized intracellular translocation of platelets establishes the yolk gradient
    • Danilchik M.V., Gerhart J.C. Differentiation of the animal-vegetal axis in Xenopus laevis oocytes. I. Polarized intracellular translocation of platelets establishes the yolk gradient. Dev. Biol. 122:1987;101-112.
    • (1987) Dev. Biol. , vol.122 , pp. 101-112
    • Danilchik, M.V.1    Gerhart, J.C.2
  • 14
    • 0001855190 scopus 로고
    • Studies on the biology of the sea urchin. I. Superficial and histological gonadal changes in the gametogenic process of two sea urchins, Strongylocentrotus nudus and Strongylocentrotus intermedius
    • Fuji A. Studies on the biology of the sea urchin. I. Superficial and histological gonadal changes in the gametogenic process of two sea urchins, Strongylocentrotus nudus and Strongylocentrotus intermedius. Bull. Fac. Fish. Hokkaido. Univ. 11:1969;1-14.
    • (1969) Bull. Fac. Fish. Hokkaido. Univ. , vol.11 , pp. 1-14
    • Fuji, A.1
  • 15
    • 85029464700 scopus 로고    scopus 로고
    • Geary, E.D., 1978. Oogenesis in the Pacific sand dollar Dendraster excentricus (Eschscholtz). MS Thesis, University of Alberta
    • Geary, E.D., 1978. Oogenesis in the Pacific sand dollar Dendraster excentricus (Eschscholtz). MS Thesis, University of Alberta.
  • 16
    • 0032734242 scopus 로고    scopus 로고
    • Receptor-mediated endocytosis in the Caenorhabditis elegans oocyte
    • Grant B., Hirsh D. Receptor-mediated endocytosis in the Caenorhabditis elegans oocyte. Mol. Biol. Cell. 10:1999;4311-4326.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4311-4326
    • Grant, B.1    Hirsh, D.2
  • 17
    • 0041722852 scopus 로고
    • Electron microscopy of the centrifuged sea urchin egg, with a note on the structure of the ground cytoplasm
    • Gross P.R., Philpott D.E., Nass S. Electron microscopy of the centrifuged sea urchin egg, with a note on the structure of the ground cytoplasm. J. Biophys. Biochem. Cytol. 7:1960;135-147.
    • (1960) J. Biophys. Biochem. Cytol. , vol.7 , pp. 135-147
    • Gross, P.R.1    Philpott, D.E.2    Nass, S.3
  • 18
    • 0020395052 scopus 로고
    • A putative precursor to the major yolk protein of the sea urchin
    • Harrington F.E., Easton D.P. A putative precursor to the major yolk protein of the sea urchin. Dev. Biol. 94:1982;505-508.
    • (1982) Dev. Biol. , vol.94 , pp. 505-508
    • Harrington, F.E.1    Easton, D.P.2
  • 19
    • 0022506149 scopus 로고
    • The major yolk glycoprotein precursor in echinoids is secreted by coelomocytes into the coelomic plasma
    • Harrington F.E., Ozaki H. The major yolk glycoprotein precursor in echinoids is secreted by coelomocytes into the coelomic plasma. Cell Differ. 19:1986;51-57.
    • (1986) Cell Differ. , vol.19 , pp. 51-57
    • Harrington, F.E.1    Ozaki, H.2
  • 21
    • 0042223225 scopus 로고
    • Physical and chemical constants of the egg of the sea urchin Arbacia punctulata
    • Harvey E.N. Physical and chemical constants of the egg of the sea urchin Arbacia punctulata. Biol. Bull. 62:1932;141-154.
    • (1932) Biol. Bull. , vol.62 , pp. 141-154
    • Harvey, E.N.1
  • 22
    • 0015007427 scopus 로고
    • The dependence of Cecropia yolk formation in vitro on specific blood proteins
    • Hausman S.J., Anderson L.M., Telfer W.H. The dependence of Cecropia yolk formation in vitro on specific blood proteins. J. Cell Biol. 48:1971;303-313.
    • (1971) J. Cell Biol. , vol.48 , pp. 303-313
    • Hausman, S.J.1    Anderson, L.M.2    Telfer, W.H.3
  • 23
    • 0018171483 scopus 로고
    • Water-soluble lipoproteins from yolk granules in sea urchin eggs. I. Isolation and general properties
    • Ichio I., Deguchi K., Kawashima S., Endo S., Ueta N. Water-soluble lipoproteins from yolk granules in sea urchin eggs. I. Isolation and general properties. J. Biochem. (Tokyo). 84:1978;737-749.
    • (1978) J. Biochem. (Tokyo) , vol.84 , pp. 737-749
    • Ichio, I.1    Deguchi, K.2    Kawashima, S.3    Endo, S.4    Ueta, N.5
  • 24
    • 0034850952 scopus 로고    scopus 로고
    • Plasma membrane resident "fusion complexes" mediate reconstituted exocytosis
    • Ikebuchi Y., Baibakov B., Smith R.M., Vogel S.S. Plasma membrane resident "fusion complexes" mediate reconstituted exocytosis. Traffic. 2:2001;654-667.
    • (2001) Traffic , vol.2 , pp. 654-667
    • Ikebuchi, Y.1    Baibakov, B.2    Smith, R.M.3    Vogel, S.S.4
  • 25
    • 4244205966 scopus 로고
    • Analysis of the yolk glycoproteins of the sea urchin embryo
    • Kari B.E., Rottman W.L. Analysis of the yolk glycoproteins of the sea urchin embryo. J. Cell Biol. 87:1980;144a.
    • (1980) J. Cell Biol. , vol.87
    • Kari, B.E.1    Rottman, W.L.2
  • 26
    • 0020724305 scopus 로고
    • Tissue-specific synthesis of yolk proteins in Caenorhabditis elegans
    • Kimble J., Sharrock W.J. Tissue-specific synthesis of yolk proteins in Caenorhabditis elegans. Dev. Biol. 96:1983;189-196.
    • (1983) Dev. Biol. , vol.96 , pp. 189-196
    • Kimble, J.1    Sharrock, W.J.2
  • 27
    • 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
  • 28
    • 0007400507 scopus 로고
    • Biochemical studies on the early development of the sea urchin
    • Monroy A.R., Maggio R. Biochemical studies on the early development of the sea urchin. Adv. Morphog. 3:1963;95-145.
    • (1963) Adv. Morphog. , vol.3 , pp. 95-145
    • Monroy, A.R.1    Maggio, R.2
  • 30
    • 0023664193 scopus 로고
    • Receptor-mediated endocytosis in Xenopus oocytes. I. Characterization of the vitellogenin receptor system
    • Opresko L.K., Wiley H.S. Receptor-mediated endocytosis in Xenopus oocytes. I. Characterization of the vitellogenin receptor system. J. Biol. Chem. 262:1987;4109-4115.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4109-4115
    • Opresko, L.K.1    Wiley, H.S.2
  • 31
    • 0019145244 scopus 로고
    • Yolk proteins of the sand dollar Dendraster excentricus
    • Ozaki H. Yolk proteins of the sand dollar Dendraster excentricus. Dev. Growth Differ. 22:1980;365-372.
    • (1980) Dev. Growth Differ. , vol.22 , pp. 365-372
    • Ozaki, H.1
  • 32
    • 34250121966 scopus 로고
    • A glycoprotein in the accessory cells of the echinoid ovary and its role in vitellogenesis
    • Ozaki H., Moriya O., Harrington F.E. A glycoprotein in the accessory cells of the echinoid ovary and its role in vitellogenesis. Roux's Arch. Dev. Biol. 195:1986;74-79.
    • (1986) Roux's Arch. Dev. Biol. , vol.195 , pp. 74-79
    • Ozaki, H.1    Moriya, O.2    Harrington, F.E.3
  • 33
    • 0034997557 scopus 로고    scopus 로고
    • Yolk protein endocytosis by oocytes in Drosophila melanogaster: Immunofluorescent localization of clathrin, adaptin and the yolk protein receptor
    • Richard D.S., Gilbert M., Crum B., Hollinshead D.M., Schelble S., Scheswohl D. Yolk protein endocytosis by oocytes in Drosophila melanogaster immunofluorescent localization of clathrin, adaptin and the yolk protein receptor . J. Insect Physiol. 47:2001;715-723.
    • (2001) J. Insect Physiol. , vol.47 , pp. 715-723
    • Richard, D.S.1    Gilbert, M.2    Crum, B.3    Hollinshead, D.M.4    Schelble, S.5    Scheswohl, D.6
  • 34
    • 0036145748 scopus 로고    scopus 로고
    • Structure and function of the egg cortex from oogenesis through fertilization
    • Sardet C., Prodon F., Dumollard R., Chang P., Chenevert J. Structure and function of the egg cortex from oogenesis through fertilization. Dev. Biol. 241:2002;1-23.
    • (2002) Dev. Biol. , vol.241 , pp. 1-23
    • Sardet, C.1    Prodon, F.2    Dumollard, R.3    Chang, P.4    Chenevert, J.5
  • 35
    • 0021763294 scopus 로고
    • Cleavage of two yolk proteins from a precursor in Caenorhabditis elegans
    • Sharrock W.J. Cleavage of two yolk proteins from a precursor in Caenorhabditis elegans. J. Mol. Biol. 174:1984;419-431.
    • (1984) J. Mol. Biol. , vol.174 , pp. 419-431
    • Sharrock, W.J.1
  • 36
    • 0023663203 scopus 로고
    • A single gene encoding vitellogenin in the sea urchin Strongylocentrotus purpuratus: Sequence at the 5′ end
    • Shyu A.B., Blumenthal T., Raff R.A. A single gene encoding vitellogenin in the sea urchin Strongylocentrotus purpuratus sequence at the 5′ end . Nucleic Acids Res. 15:1987;10405-10417.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 10405-10417
    • Shyu, A.B.1    Blumenthal, T.2    Raff, R.A.3
  • 37
    • 0022544506 scopus 로고
    • Expression of the vitellogenin gene in female and male sea urchin
    • Shyu A.B., Raff R.A., Blumenthal T. Expression of the vitellogenin gene in female and male sea urchin. Proc. Natl. Acad. Sci. USA. 83:1986;3865-3869.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3865-3869
    • Shyu, A.B.1    Raff, R.A.2    Blumenthal, T.3
  • 38
    • 0030829955 scopus 로고    scopus 로고
    • Internalization and recycling of vitellogenin receptor in the mosquito oocyte
    • Snigirevskaya E.S., Sappington T.W., Raikhel A.S. Internalization and recycling of vitellogenin receptor in the mosquito oocyte. Cell Tissue Res. 290:1997;175-183.
    • (1997) Cell Tissue Res. , vol.290 , pp. 175-183
    • Snigirevskaya, E.S.1    Sappington, T.W.2    Raikhel, A.S.3
  • 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
  • 40
    • 0013959661 scopus 로고
    • Electron microscope investigations of the modes of yolk and pigment formation in sea urchin oocytes
    • Takashima Y., Takashima R. Electron microscope investigations of the modes of yolk and pigment formation in sea urchin oocytes. Okajimas Folia Anat. Jpn. 42:1966;249-264.
    • (1966) Okajimas Folia Anat. Jpn. , vol.42 , pp. 249-264
    • Takashima, Y.1    Takashima, R.2
  • 41
    • 0015191846 scopus 로고
    • Electron microscopic studies on the behavior of glycogen particles during oogenesis in the sea urchin
    • Tsukahara J. Electron microscopic studies on the behavior of glycogen particles during oogenesis in the sea urchin. Dev. Growth Differ. 13:1971;367-378.
    • (1971) Dev. Growth Differ. , vol.13 , pp. 367-378
    • Tsukahara, J.1
  • 42
    • 84977249428 scopus 로고
    • Ultrastructural changes in the surface of the oocyte during oogenesis of the sea urchin, Hemicentrotus pulcherrimus
    • Tsukahara J., Sugiyama M. Ultrastructural changes in the surface of the oocyte during oogenesis of the sea urchin, Hemicentrotus pulcherrimus. Embryologia (Nagoya). 10:1969;343-355.
    • (1969) Embryologia (Nagoya) , vol.10 , pp. 343-355
    • Tsukahara, J.1    Sugiyama, M.2
  • 43
    • 0035593411 scopus 로고    scopus 로고
    • Cloning of cDNA encoding vitellogenin and its expression in the red sea urchin Pseudocentrotus depressus
    • Unuma T., Okamoto H., Konishi K., Ohta H., Mori K. Cloning of cDNA encoding vitellogenin and its expression in the red sea urchin Pseudocentrotus depressus. Zool. Sci. 18:2001;559-565.
    • (2001) Zool. Sci. , vol.18 , pp. 559-565
    • Unuma, T.1    Okamoto, H.2    Konishi, K.3    Ohta, H.4    Mori, K.5
  • 44
    • 0031939113 scopus 로고    scopus 로고
    • A protein identical to the yolk protein is stored in the testis in male red sea urchin, Pseudocentrotus depressus
    • Unuma T., Suzuki T., Kurokawa T., Yamamoto T., Akiyama T. A protein identical to the yolk protein is stored in the testis in male red sea urchin, Pseudocentrotus depressus. Biol. Bull. 194:1998;92-97.
    • (1998) Biol. Bull. , vol.194 , pp. 92-97
    • Unuma, T.1    Suzuki, T.2    Kurokawa, T.3    Yamamoto, T.4    Akiyama, T.5
  • 45
    • 84981864377 scopus 로고
    • Fine structural changes during sea urchin oogenesis
    • Verhey C.A., Moyer F.H. Fine structural changes during sea urchin oogenesis. J. Exp. Zool. 164:1967;95-132.
    • (1967) J. Exp. Zool. , vol.164 , pp. 95-132
    • Verhey, C.A.1    Moyer, F.H.2
  • 46
    • 0002208877 scopus 로고
    • Nutrition in gametes
    • M. Jangoux, & J.M. Lawrence. Rotterdam: Balkema Press
    • Walker C.W. Nutrition in gametes. Jangoux M., Lawrence J.M. Echinoderm Nutrition. 1982;449-468 Balkema Press, Rotterdam.
    • (1982) Echinoderm Nutrition , pp. 449-468
    • Walker, C.W.1
  • 47
    • 0023109345 scopus 로고
    • Multivesicular bodies play a key role in vitellogenin endocytosis by Xenopus oocytes
    • Wall D.A., Patel S. Multivesicular bodies play a key role in vitellogenin endocytosis by Xenopus oocytes. Dev. Biol. 119:1987;275-289.
    • (1987) Dev. Biol. , vol.119 , pp. 275-289
    • Wall, D.A.1    Patel, S.2
  • 48
    • 0018217561 scopus 로고
    • Long-term growth and differentiation of Xenopus oocytes in a defined medium
    • Wallace R.A., Misulovin Z. Long-term growth and differentiation of Xenopus oocytes in a defined medium. Proc. Natl. Acad. Sci. USA. 75:1978;5534-5538.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5534-5538
    • Wallace, R.A.1    Misulovin, Z.2
  • 50
    • 0036746622 scopus 로고    scopus 로고
    • Cortical granule translocation is microfilament mediated and linked to meiotic maturation in the sea urchin oocyte
    • Wessel G.M., Conner S.D., Berg L. Cortical granule translocation is microfilament mediated and linked to meiotic maturation in the sea urchin oocyte. Development. 129:2002;4315-4325.
    • (2002) Development , vol.129 , pp. 4315-4325
    • Wessel, G.M.1    Conner, S.D.2    Berg, L.3
  • 51
  • 52
    • 0028800961 scopus 로고
    • Direct membrane retrieval into large vesicles after exocytosis in sea urchin eggs
    • Whalley T., Terasaki M., Cho M.S., Vogel S.S. Direct membrane retrieval into large vesicles after exocytosis in sea urchin eggs. J. Cell Biol. 131:1995;1183-1192.
    • (1995) J. Cell Biol. , vol.131 , pp. 1183-1192
    • Whalley, T.1    Terasaki, M.2    Cho, M.S.3    Vogel, S.S.4


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