메뉴 건너뛰기




Volumn 76, Issue 6, 2007, Pages 936-948

The maturational disassembly and differential proteolysis of paralogous vitellogenins in a marine pelagophil teleost: A conserved mechanism of oocyte hydration

Author keywords

Gamete biology; Gametogenesis; Meiosis; Oocyte development; Ovulation

Indexed keywords

AMINO ACID; COMPLEMENTARY DNA; LIPOVITELLIN; VITELLOGENIN;

EID: 34249725019     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod.106.055772     Document Type: Article
Times cited : (69)

References (76)
  • 1
    • 0036321923 scopus 로고    scopus 로고
    • In vivo oocyte hydration in Atlantic halibut (Hippoglossus hippoglossus): Proteolytic liberation of free amino acids, and ion transport, are driving forces for osmotic water influx
    • Finn RN, Østby GC, Norberg B, Fyhn HJ. In vivo oocyte hydration in Atlantic halibut (Hippoglossus hippoglossus): proteolytic liberation of free amino acids, and ion transport, are driving forces for osmotic water influx. J Exp Biol 2002; 205:211-224.
    • (2002) J Exp Biol , vol.205 , pp. 211-224
    • Finn, R.N.1    Østby, G.C.2    Norberg, B.3    Fyhn, H.J.4
  • 2
    • 0037130152 scopus 로고    scopus 로고
    • Differential processing of yolk proteins during oocyte hydration in fishes (Labridae) that spawn benthic and pelagic eggs
    • Finn RN, Wamboldt M, Fyhn HJ. Differential processing of yolk proteins during oocyte hydration in fishes (Labridae) that spawn benthic and pelagic eggs. Mar Ecol Prog Ser 2002; 237:217-226.
    • (2002) Mar Ecol Prog Ser , vol.237 , pp. 217-226
    • Finn, R.N.1    Wamboldt, M.2    Fyhn, H.J.3
  • 3
    • 34249733664 scopus 로고    scopus 로고
    • Finn RN, Kristoffersen BA. Vertebrate vitellogenin gene duplication in relation to the 3R hypothesis. Correlation to the pelagic egg and the oceanic radiation of teleosts. PLoS ONE 2007; 2:e169.
    • Finn RN, Kristoffersen BA. Vertebrate vitellogenin gene duplication in relation to the "3R hypothesis". Correlation to the pelagic egg and the oceanic radiation of teleosts. PLoS ONE 2007; 2:e169.
  • 5
    • 33746008840 scopus 로고    scopus 로고
    • Yolk proteolysis and aquaporin-lo play essential roles to regulate fish oocyte hydration during meiosis resumption
    • Fabra M, Raldúa D, Bozzo MG, Deen PM, Lubzens E, Cerdà J. Yolk proteolysis and aquaporin-lo play essential roles to regulate fish oocyte hydration during meiosis resumption. Dev Biol 2006; 295:250-262.
    • (2006) Dev Biol , vol.295 , pp. 250-262
    • Fabra, M.1    Raldúa, D.2    Bozzo, M.G.3    Deen, P.M.4    Lubzens, E.5    Cerdà, J.6
  • 7
    • 0032078463 scopus 로고    scopus 로고
    • Molecular characteristics of insect vitellogenins and vitellogenin receptors
    • Sappington TW, Raikhel AS. Molecular characteristics of insect vitellogenins and vitellogenin receptors. Insect Biochem Mol Biol 1998; 28:277-300.
    • (1998) Insect Biochem Mol Biol , vol.28 , pp. 277-300
    • Sappington, T.W.1    Raikhel, A.S.2
  • 9
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner SD, Schmid SL. Regulated portals of entry into the cell. Nature 2003; 422:37-44.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 10
    • 0021185179 scopus 로고
    • Endosomes transfer yolk proteins to lysosomes in the vitellogenic oocyte of the trout
    • Busson-Mabillot S. Endosomes transfer yolk proteins to lysosomes in the vitellogenic oocyte of the trout. Biol Cell 1984; 51:53-66.
    • (1984) Biol Cell , vol.51 , pp. 53-66
    • Busson-Mabillot, S.1
  • 11
    • 0025015440 scopus 로고
    • Ultrastructural aspects of oogenesis and oocyte growth in fish and amphibians
    • Wallace RA, Selman K. Ultrastructural aspects of oogenesis and oocyte growth in fish and amphibians. J Electron Microsc Tech 1990; 16:175-201.
    • (1990) J Electron Microsc Tech , vol.16 , pp. 175-201
    • Wallace, R.A.1    Selman, K.2
  • 12
    • 0030829955 scopus 로고    scopus 로고
    • Internalization and recycling of vitellogenin receptor in the mosquito oocyte
    • Snigirevskaya ES, Sappington TW, Raikhel AS. Internalization and recycling of vitellogenin receptor in the mosquito oocyte. Cell Tissue Res 1997; 290:175-183.
    • (1997) Cell Tissue Res , vol.290 , pp. 175-183
    • Snigirevskaya, E.S.1    Sappington, T.W.2    Raikhel, A.S.3
  • 14
    • 0024063518 scopus 로고
    • Evolution and expression of vitellogenin genes
    • Wahli W. Evolution and expression of vitellogenin genes. Trends Genet 1988; 4:227-232.
    • (1988) Trends Genet , vol.4 , pp. 227-232
    • Wahli, W.1
  • 15
    • 0033199056 scopus 로고    scopus 로고
    • Two forms of vitellogenin, yielding two distinct lipovitellins, play different roles during oocyte maturation and early development of barfin flounder, Verasper moseri, a marine teleost that spawns pelagic eggs
    • Matsubara T, Ohkubo N, Andoh T, Sullivan CV, Hara A. Two forms of vitellogenin, yielding two distinct lipovitellins, play different roles during oocyte maturation and early development of barfin flounder, Verasper moseri, a marine teleost that spawns pelagic eggs. Dev Biol 1999; 213:18-32.
    • (1999) Dev Biol , vol.213 , pp. 18-32
    • Matsubara, T.1    Ohkubo, N.2    Andoh, T.3    Sullivan, C.V.4    Hara, A.5
  • 17
    • 0035870296 scopus 로고    scopus 로고
    • Lipovitellins derived from two forms of vitellogenin are differentially processed during oocyte maturation in haddock (Melanogrammus aeglefinus)
    • Reith M, Munholland J, Kelly J, Finn RN, Fyhn HJ. Lipovitellins derived from two forms of vitellogenin are differentially processed during oocyte maturation in haddock (Melanogrammus aeglefinus). J Exp Zool 2001; 291:58-67.
    • (2001) J Exp Zool , vol.291 , pp. 58-67
    • Reith, M.1    Munholland, J.2    Kelly, J.3    Finn, R.N.4    Fyhn, H.J.5
  • 18
    • 0036006819 scopus 로고    scopus 로고
    • Identification and characterization of proteases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids
    • Hiramatsu N, Ichikawa N, Fukada H, Fujita T, Sullivan CV, Hara A. Identification and characterization of proteases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids. J Exp Zool 2002; 292:11-25.
    • (2002) J Exp Zool , vol.292 , pp. 11-25
    • Hiramatsu, N.1    Ichikawa, N.2    Fukada, H.3    Fujita, T.4    Sullivan, C.V.5    Hara, A.6
  • 19
    • 1942535909 scopus 로고    scopus 로고
    • Deduced primary structure of two forms of vitellogenin in Japanese common goby (Acanthogobius flavimanus)
    • Ohkubo N, Andoh T, Mochida K, Adachi S, Hara A, Matsubara T. Deduced primary structure of two forms of vitellogenin in Japanese common goby (Acanthogobius flavimanus). Gen Comp Endocrinol 2004; 137:19-28.
    • (2004) Gen Comp Endocrinol , vol.137 , pp. 19-28
    • Ohkubo, N.1    Andoh, T.2    Mochida, K.3    Adachi, S.4    Hara, A.5    Matsubara, T.6
  • 20
    • 15544368550 scopus 로고    scopus 로고
    • Multiple vitellogenins (Vgs) in mosquitofish (Gambusia affinis): Identification and characterization of three functional Vg genes and their circulating and yolk protein products
    • Sawaguchi S, Koya Y, Yoshizaki N, Ohkubo N, Andoh T, Hiramatsu N, Sullivan CV, Hara A, Matsubara T. Multiple vitellogenins (Vgs) in mosquitofish (Gambusia affinis): identification and characterization of three functional Vg genes and their circulating and yolk protein products. Biol Reprod 2005; 72:1045-1060.
    • (2005) Biol Reprod , vol.72 , pp. 1045-1060
    • Sawaguchi, S.1    Koya, Y.2    Yoshizaki, N.3    Ohkubo, N.4    Andoh, T.5    Hiramatsu, N.6    Sullivan, C.V.7    Hara, A.8    Matsubara, T.9
  • 21
    • 33646441137 scopus 로고    scopus 로고
    • Molecular characterization of three forms of vitellogenin and their yolk protein products during oocyte growth and maturation in red seabream (Pagrus major), a marine teleost spawning pelagic eggs
    • Sawaguchi S, Kagawa H, Ohkubo N, Hiramatsu N, Sullivan CV, Matsubara T. Molecular characterization of three forms of vitellogenin and their yolk protein products during oocyte growth and maturation in red seabream (Pagrus major), a marine teleost spawning pelagic eggs. Mol Reprod Dev 2006; 73:719-736.
    • (2006) Mol Reprod Dev , vol.73 , pp. 719-736
    • Sawaguchi, S.1    Kagawa, H.2    Ohkubo, N.3    Hiramatsu, N.4    Sullivan, C.V.5    Matsubara, T.6
  • 22
    • 0022416087 scopus 로고
    • Major protein changes during vitellogenesis and maturation of Fundulus oocytes
    • Wallace RA, Selman K. Major protein changes during vitellogenesis and maturation of Fundulus oocytes. Dev Biol 1985; 110:492-498.
    • (1985) Dev Biol , vol.110 , pp. 492-498
    • Wallace, R.A.1    Selman, K.2
  • 23
    • 25144498370 scopus 로고    scopus 로고
    • Derivation of major yolk proteins from parental vitellogenins and alternative processing during oocyte maturation in Fundulus heteroclitus
    • LaFleur GJ Jr, Raldúa D, Fabra M, Carnevali O, Denslow N, Wallace RA, Cerdà J. Derivation of major yolk proteins from parental vitellogenins and alternative processing during oocyte maturation in Fundulus heteroclitus. Biol Reprod 2005; 73:815-824.
    • (2005) Biol Reprod , vol.73 , pp. 815-824
    • LaFleur Jr, G.J.1    Raldúa, D.2    Fabra, M.3    Carnevali, O.4    Denslow, N.5    Wallace, R.A.6    Cerdà, J.7
  • 24
    • 0032527992 scopus 로고    scopus 로고
    • The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein
    • Anderson TA, Levitt DG, Banaszak LJ. The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein. Structure 1998; 6:895-909.
    • (1998) Structure , vol.6 , pp. 895-909
    • Anderson, T.A.1    Levitt, D.G.2    Banaszak, L.J.3
  • 26
    • 0037018919 scopus 로고    scopus 로고
    • The N-terminal 1000 residues of apolipoprotein B associate with microsomal triglyceride transfer protein to create a lipid transfer pocket required for lipoprotein assembly
    • Dashti N, Gandhi M, Liu X, Lin X, Segrest JP. The N-terminal 1000 residues of apolipoprotein B associate with microsomal triglyceride transfer protein to create a lipid transfer pocket required for lipoprotein assembly. Biochemistry 2002; 41:6978-6987.
    • (2002) Biochemistry , vol.41 , pp. 6978-6987
    • Dashti, N.1    Gandhi, M.2    Liu, X.3    Lin, X.4    Segrest, J.P.5
  • 27
    • 0037199420 scopus 로고    scopus 로고
    • Lipid-protein interactions in lipovitellin
    • Thompson JR, Banaszak LJ. Lipid-protein interactions in lipovitellin. Biochemistry 2002; 41:9398-9409.
    • (2002) Biochemistry , vol.41 , pp. 9398-9409
    • Thompson, J.R.1    Banaszak, L.J.2
  • 28
    • 13444281988 scopus 로고    scopus 로고
    • Limited proteolysis and biophysical characterization of the lipovitellin homology region in apolipoprotein B
    • Jiang ZG, Carraway M, McKnight CJ. Limited proteolysis and biophysical characterization of the lipovitellin homology region in apolipoprotein B. Biochemistry 2005; 44:1163-1173.
    • (2005) Biochemistry , vol.44 , pp. 1163-1173
    • Jiang, Z.G.1    Carraway, M.2    McKnight, C.J.3
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 1987; 166:368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 33
    • 0021881554 scopus 로고
    • The primary structure of avian phosvitins. Contributions through the Edman degradation of methylmercaptovitins prepared from the constituent phosphoproteins
    • Clark RC. The primary structure of avian phosvitins. Contributions through the Edman degradation of methylmercaptovitins prepared from the constituent phosphoproteins. Int J Biochem 1985; 17:983-988.
    • (1985) Int J Biochem , vol.17 , pp. 983-988
    • Clark, R.C.1
  • 34
    • 0018908112 scopus 로고
    • Identification, purification, and characterization of two distinct avian vitellogenins
    • Wang SY, Williams DL. Identification, purification, and characterization of two distinct avian vitellogenins. Biochemistry 1980; 19:1557-1563.
    • (1980) Biochemistry , vol.19 , pp. 1557-1563
    • Wang, S.Y.1    Williams, D.L.2
  • 35
    • 0000985335 scopus 로고
    • Purification of avian vitellogenin III: Comparison with vitellogenins I and II
    • Wang SY, Smith DE, Williams DL. Purification of avian vitellogenin III: comparison with vitellogenins I and II. Biochemistry 1983; 22:6206-6212.
    • (1983) Biochemistry , vol.22 , pp. 6206-6212
    • Wang, S.Y.1    Smith, D.E.2    Williams, D.L.3
  • 36
    • 0021760617 scopus 로고    scopus 로고
    • Byrne BM, van het Schip AD, van de Klundert JA, Arnberg AC, Gruber M, Ab G. Amino acid sequence of phosvitin derived from the nucleotide sequence of part of the chicken vitellogenin gene. Biochemistry 1984; 23: 4275-4279.
    • Byrne BM, van het Schip AD, van de Klundert JA, Arnberg AC, Gruber M, Ab G. Amino acid sequence of phosvitin derived from the nucleotide sequence of part of the chicken vitellogenin gene. Biochemistry 1984; 23: 4275-4279.
  • 37
    • 0022868429 scopus 로고
    • Chromatographic resolution of chicken phosvitin. Multiple macromolecular species in a classic vitellogenin-derived phosphoprotein
    • Wallace RA, Morgan JP. Chromatographic resolution of chicken phosvitin. Multiple macromolecular species in a classic vitellogenin-derived phosphoprotein. Biochem J 1986; 240:871-878.
    • (1986) Biochem J , vol.240 , pp. 871-878
    • Wallace, R.A.1    Morgan, J.P.2
  • 38
    • 0022549434 scopus 로고
    • Isolation of phosvitin: Retention of small molecular weight species and staining characteristics on electrophoretic gels
    • Wallace RA, Morgan JP. Isolation of phosvitin: retention of small molecular weight species and staining characteristics on electrophoretic gels. Anal Biochem 1986; 157:256-261.
    • (1986) Anal Biochem , vol.157 , pp. 256-261
    • Wallace, R.A.1    Morgan, J.P.2
  • 39
    • 0023660763 scopus 로고    scopus 로고
    • van het Schip FD, Samallo J, Broos J, Ophuis J, Mojet M, Gruber M, Ab G. Nucleotide sequence of a chicken vitellogenin gene and derived amino acid sequence of the encoded yolk precursor protein. J Mol Biol 1987; 196:245-260.
    • van het Schip FD, Samallo J, Broos J, Ophuis J, Mojet M, Gruber M, Ab G. Nucleotide sequence of a chicken vitellogenin gene and derived amino acid sequence of the encoded yolk precursor protein. J Mol Biol 1987; 196:245-260.
  • 40
    • 0024345781 scopus 로고
    • The major and minor chicken vitellogenin genes are each adjacent to partially deleted pseudogene copies of the other
    • Silva R, Fischer AH, Burch JB. The major and minor chicken vitellogenin genes are each adjacent to partially deleted pseudogene copies of the other. Mol Cell Biol 1989; 9:3557-3562.
    • (1989) Mol Cell Biol , vol.9 , pp. 3557-3562
    • Silva, R.1    Fischer, A.H.2    Burch, J.B.3
  • 41
    • 34249689094 scopus 로고    scopus 로고
    • Vertebrate yolk complexes and the functional implications of phosvitins and other sub-domains in vitellogenins
    • Finn RN. Vertebrate yolk complexes and the functional implications of phosvitins and other sub-domains in vitellogenins. Biol Reprod 2007; 76:926-935.
    • (2007) Biol Reprod , vol.76 , pp. 926-935
    • Finn, R.N.1
  • 42
    • 0942265428 scopus 로고    scopus 로고
    • Ovarian cysteine proteinases in the teleost Fundulus heteroclitus: Molecular cloning and gene expression during vitellogenesis and oocyte maturation
    • Fabra M, Cerdà J. Ovarian cysteine proteinases in the teleost Fundulus heteroclitus: molecular cloning and gene expression during vitellogenesis and oocyte maturation. Mol Reprod Dev 2004; 67:282-294.
    • (2004) Mol Reprod Dev , vol.67 , pp. 282-294
    • Fabra, M.1    Cerdà, J.2
  • 44
    • 33644764063 scopus 로고    scopus 로고
    • Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes
    • Lakadamyali M, Rust MJ, Zhuang X. Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes. Cell 2006; 124:997-1009.
    • (2006) Cell , vol.124 , pp. 997-1009
    • Lakadamyali, M.1    Rust, M.J.2    Zhuang, X.3
  • 45
    • 0032918875 scopus 로고    scopus 로고
    • Yolk formation and degradation during oocyte maturation in seabream Sparus aurata: Involvement of two lysosomal proteinases
    • Carnevali O, Carletta R, Cambi A, Vita A, Bromage N. Yolk formation and degradation during oocyte maturation in seabream Sparus aurata: involvement of two lysosomal proteinases. Biol Reprod 1999; 60:140-146.
    • (1999) Biol Reprod , vol.60 , pp. 140-146
    • Carnevali, O.1    Carletta, R.2    Cambi, A.3    Vita, A.4    Bromage, N.5
  • 46
    • 0020956821 scopus 로고
    • Lipovitellin-phosvitin crystals with orthorhombic features: Thin-section electron microscopy, gel electrophoresis, and microanalysis in teleost and amphibian yolk platelets and a comparison with other vertebrates
    • Lange RH, Richter HP, Riehl R, Zierold K, Trandaburu T, Magdowski G. Lipovitellin-phosvitin crystals with orthorhombic features: thin-section electron microscopy, gel electrophoresis, and microanalysis in teleost and amphibian yolk platelets and a comparison with other vertebrates. J Ultrastruct Res 1983; 83:122-140.
    • (1983) J Ultrastruct Res , vol.83 , pp. 122-140
    • Lange, R.H.1    Richter, H.P.2    Riehl, R.3    Zierold, K.4    Trandaburu, T.5    Magdowski, G.6
  • 47
    • 0022356686 scopus 로고
    • The vertebrate yolk platelet crystal: Comparative analysis of an in vivo crystalline aggregate
    • Lange RH. The vertebrate yolk platelet crystal: comparative analysis of an in vivo crystalline aggregate. Int Rev Cytol 1984; 97:133-181.
    • (1984) Int Rev Cytol , vol.97 , pp. 133-181
    • Lange, R.H.1
  • 48
    • 0032794641 scopus 로고    scopus 로고
    • Molecular cloning and expression of ovarian cathepsin D in seabream, Sparus aurata
    • Carnevali O, Centonze F, Brooks S, Marota I, Sumpter JP. Molecular cloning and expression of ovarian cathepsin D in seabream, Sparus aurata. Biol Reprod 1999; 61:785-791.
    • (1999) Biol Reprod , vol.61 , pp. 785-791
    • Carnevali, O.1    Centonze, F.2    Brooks, S.3    Marota, I.4    Sumpter, J.P.5
  • 49
    • 0035184222 scopus 로고    scopus 로고
    • Molecular characterization of putative yolk processing enzymes and their expression during oogenesis and embryogenesis in rainbow trout (Oncorhynchus mykiss)
    • Kwon JY, Prat F, Randall C, Tyler CR. Molecular characterization of putative yolk processing enzymes and their expression during oogenesis and embryogenesis in rainbow trout (Oncorhynchus mykiss). Biol Reprod 2001; 65:1701-1709.
    • (2001) Biol Reprod , vol.65 , pp. 1701-1709
    • Kwon, J.Y.1    Prat, F.2    Randall, C.3    Tyler, C.R.4
  • 50
    • 0029123767 scopus 로고
    • Fundulus heteroclitus vitellogenin: The deduced primary structure of a piscine precursor to noncrystalline, liquid-phase yolk protein
    • LaFleur GJ Jr, Byrne BM, Kanungo J, Nelson LD, Greenberg RM, Wallace RA. Fundulus heteroclitus vitellogenin: the deduced primary structure of a piscine precursor to noncrystalline, liquid-phase yolk protein. J Mol Evol 1995; 41:505-521.
    • (1995) J Mol Evol , vol.41 , pp. 505-521
    • LaFleur Jr, G.J.1    Byrne, B.M.2    Kanungo, J.3    Nelson, L.D.4    Greenberg, R.M.5    Wallace, R.A.6
  • 51
    • 0035904464 scopus 로고    scopus 로고
    • Sequence analysis of a fish vitellogenin cDNA with a large phosvitin domain
    • Lim EH, Teo BY, Lam TJ, Ding JL. Sequence analysis of a fish vitellogenin cDNA with a large phosvitin domain. Gene 2001; 277:175-186.
    • (2001) Gene , vol.277 , pp. 175-186
    • Lim, E.H.1    Teo, B.Y.2    Lam, T.J.3    Ding, J.L.4
  • 52
    • 0037474268 scopus 로고    scopus 로고
    • Receptor-ligand interaction between vitellogenin receptor (VtgR) and vitellogenin (Vtg), implications on low density lipoprotein receptor and apolipoprotein B/E. The first three ligand-binding repeats of VtgR interact with the amino-terminal region of Vtg
    • Li A, Sadasivam M, Ding JL. Receptor-ligand interaction between vitellogenin receptor (VtgR) and vitellogenin (Vtg), implications on low density lipoprotein receptor and apolipoprotein B/E. The first three ligand-binding repeats of VtgR interact with the amino-terminal region of Vtg. J Biol Chem 2003; 278:2799-2806.
    • (2003) J Biol Chem , vol.278 , pp. 2799-2806
    • Li, A.1    Sadasivam, M.2    Ding, J.L.3
  • 53
    • 0031977582 scopus 로고    scopus 로고
    • Molecular characterization and expression of two ovarian lipoprotein receptors in the rainbow trout, Oncorhynchus mykiss
    • Prat F, Coward K, Sumpter JP, Tyler CR. Molecular characterization and expression of two ovarian lipoprotein receptors in the rainbow trout, Oncorhynchus mykiss. Biol Reprod 1998; 58:1146-1153.
    • (1998) Biol Reprod , vol.58 , pp. 1146-1153
    • Prat, F.1    Coward, K.2    Sumpter, J.P.3    Tyler, C.R.4
  • 54
    • 0025971504 scopus 로고
    • Vitellogenin purification and development of assay for vitellogenin receptor in oocyte membranes of the tilapia (Oreochromis niloticus, Linnaeus 1766)
    • Chan SL, Tan CH, Pang MK, Lam TJ. Vitellogenin purification and development of assay for vitellogenin receptor in oocyte membranes of the tilapia (Oreochromis niloticus, Linnaeus 1766). J Exp Zool 1991; 274:96-109.
    • (1991) J Exp Zool , vol.274 , pp. 96-109
    • Chan, S.L.1    Tan, C.H.2    Pang, M.K.3    Lam, T.J.4
  • 55
    • 0030270960 scopus 로고    scopus 로고
    • The sequence of catabolic substrate oxidation and enthalpy balance of developing embryos and yolk-sac larvae of turbot (Scophthalmus maximus L.)
    • Finn RN, Fyhn HJ, Henderson RJ, Evjen MS. The sequence of catabolic substrate oxidation and enthalpy balance of developing embryos and yolk-sac larvae of turbot (Scophthalmus maximus L.). Comp Biochem Physiol 1996; 115A:133-151.
    • (1996) Comp Biochem Physiol , vol.115 A , pp. 133-151
    • Finn, R.N.1    Fyhn, H.J.2    Henderson, R.J.3    Evjen, M.S.4
  • 56
    • 85008137625 scopus 로고
    • Changes in the electrophoretic patterns of lipovitellin during oocyte development in the Japanese eel Anguilla japonica
    • Okumura H, Kayaba T, Kazeto Y, Hara A, Adachi S, Yamauchi K. Changes in the electrophoretic patterns of lipovitellin during oocyte development in the Japanese eel Anguilla japonica. Fish Sci 1995; 61: 529-530.
    • (1995) Fish Sci , vol.61 , pp. 529-530
    • Okumura, H.1    Kayaba, T.2    Kazeto, Y.3    Hara, A.4    Adachi, S.5    Yamauchi, K.6
  • 57
    • 0037429178 scopus 로고    scopus 로고
    • Differences in the biochemical content of buoyant and non-buoyant eggs of the Japanese eel. Anguilla japonica
    • Seoka M, Yamada S, Iwata Y, Yanagisawa T, Nakagawa T, Kumai H. Differences in the biochemical content of buoyant and non-buoyant eggs of the Japanese eel. Anguilla japonica. Aquaculture 2003; 216:355-362.
    • (2003) Aquaculture , vol.216 , pp. 355-362
    • Seoka, M.1    Yamada, S.2    Iwata, Y.3    Yanagisawa, T.4    Nakagawa, T.5    Kumai, H.6
  • 58
    • 4143144453 scopus 로고    scopus 로고
    • Free amino acids in Japanese eel eggs obtained by hormonal inducement
    • Seoka M, Yamada S, Kumai H. Free amino acids in Japanese eel eggs obtained by hormonal inducement. J Fish Biol 2004; 65:595-596.
    • (2004) J Fish Biol , vol.65 , pp. 595-596
    • Seoka, M.1    Yamada, S.2    Kumai, H.3
  • 59
    • 0028095918 scopus 로고
    • Involvement of the lysosomal system in yolk protein deposit and degradation during vitellogenesis and embryonic development in trout
    • Sire MF, Babin PJ, Vernier JM. Involvement of the lysosomal system in yolk protein deposit and degradation during vitellogenesis and embryonic development in trout. J Exp Zool 1994; 269:69-83.
    • (1994) J Exp Zool , vol.269 , pp. 69-83
    • Sire, M.F.1    Babin, P.J.2    Vernier, J.M.3
  • 61
    • 0031761930 scopus 로고    scopus 로고
    • Cysteine proteinase plays a key role for the initiation of yolk digestion during development of Xenopus laevis
    • Yoshizaki N, Yonezawa S. Cysteine proteinase plays a key role for the initiation of yolk digestion during development of Xenopus laevis. Dev Growth Differ 1998; 40:659-667.
    • (1998) Dev Growth Differ , vol.40 , pp. 659-667
    • Yoshizaki, N.1    Yonezawa, S.2
  • 62
    • 0035421972 scopus 로고    scopus 로고
    • Bafilomycin A1 inhibits proteolytic cleavage and hydration but not yolk crystal disassembly or meiosis during maturation of sea bass oocytes
    • Selman K, Wallace RA, Cerdà J. Bafilomycin A1 inhibits proteolytic cleavage and hydration but not yolk crystal disassembly or meiosis during maturation of sea bass oocytes. J Exp Zool 2001; 290:265-278.
    • (2001) J Exp Zool , vol.290 , pp. 265-278
    • Selman, K.1    Wallace, R.A.2    Cerdà, J.3
  • 63
    • 0001565058 scopus 로고
    • Ionic strength and pH effects on composition and microstructure of yolk granules
    • Causeret D, Matringe E, Lorient D. Ionic strength and pH effects on composition and microstructure of yolk granules. J Food Sci 1991; 56: 1532-1536.
    • (1991) J Food Sci , vol.56 , pp. 1532-1536
    • Causeret, D.1    Matringe, E.2    Lorient, D.3
  • 64
    • 0032496158 scopus 로고    scopus 로고
    • pH-induced conformational transitions of the propeptide of human cathepsin L. A role for a molten globule state in zymogen activation
    • Jerala R, Zerovnik E, Kidric J, Turk V. pH-induced conformational transitions of the propeptide of human cathepsin L. A role for a molten globule state in zymogen activation. J Biol Chem 1998; 273:11498-11504.
    • (1998) J Biol Chem , vol.273 , pp. 11498-11504
    • Jerala, R.1    Zerovnik, E.2    Kidric, J.3    Turk, V.4
  • 66
    • 84985091499 scopus 로고
    • Water and ion balance in hydrating oocytes of the grey mullet, Mugil cephalus (L.), during hormonal induced final maturation
    • Watanabe WO, Kuo CM. Water and ion balance in hydrating oocytes of the grey mullet, Mugil cephalus (L.), during hormonal induced final maturation. J Fish Biol 1986; 28:425-437.
    • (1986) J Fish Biol , vol.28 , pp. 425-437
    • Watanabe, W.O.1    Kuo, C.M.2
  • 67
    • 0028587431 scopus 로고
    • Changes in yolk platelet pH during Xenopus laevis development correlate with yolk utilization. A quantitative confocal microscopy study
    • Fagotto F, Maxfield FR. Changes in yolk platelet pH during Xenopus laevis development correlate with yolk utilization. A quantitative confocal microscopy study. J Cell Sci 1994; 107:3325-3337.
    • (1994) J Cell Sci , vol.107 , pp. 3325-3337
    • Fagotto, F.1    Maxfield, F.R.2
  • 69
    • 0026148892 scopus 로고
    • +-ATPase in the hydration of Atlantic croaker and spotted seatrout oocytes during final maturation
    • +-ATPase in the hydration of Atlantic croaker and spotted seatrout oocytes during final maturation. J Exp Zool 1991; 258:126-136.
    • (1991) J Exp Zool , vol.258 , pp. 126-136
    • LaFleur Jr, G.J.1    Thomas, P.2
  • 70
    • 0026481575 scopus 로고
    • +, and water uptake during volume increases associated with Fundulus oocyte maturation in vitro
    • +, and water uptake during volume increases associated with Fundulus oocyte maturation in vitro. J Comp Physiol B 1992; 162:241-248.
    • (1992) J Comp Physiol B , vol.162 , pp. 241-248
    • Wallace, R.A.1    Greeley Jr, M.S.2    McPherson, R.3
  • 71
    • 0029583839 scopus 로고
    • Regulation of yolk degradation, or how to make sleepy lysosomes
    • Fagotto F. Regulation of yolk degradation, or how to make sleepy lysosomes. J Cell Sci 1995; 108:3645-3647.
    • (1995) J Cell Sci , vol.108 , pp. 3645-3647
    • Fagotto, F.1
  • 72
    • 4544328500 scopus 로고    scopus 로고
    • Apolipoprotein B-containing lipoprotein particle assembly: Lipid capacity of the nascent lipoprotein particle
    • Manchekar M, Richardson PE, Forte TM, Datta G, Segrest JP, Dashti N. Apolipoprotein B-containing lipoprotein particle assembly: lipid capacity of the nascent lipoprotein particle. J Biol Chem 2004; 279:39757-39766.
    • (2004) J Biol Chem , vol.279 , pp. 39757-39766
    • Manchekar, M.1    Richardson, P.E.2    Forte, T.M.3    Datta, G.4    Segrest, J.P.5    Dashti, N.6
  • 75
    • 0028128428 scopus 로고
    • Microsomal triglyceride transfer protein, the abetalipoproteinemia gene product, mediates the secretion of apolipoprotein B-containing lipoproteins from heterologous cells
    • Leiper JM, Bayliss JD, Pease RJ, Brett DJ, Scott J, Shoulders CC. Microsomal triglyceride transfer protein, the abetalipoproteinemia gene product, mediates the secretion of apolipoprotein B-containing lipoproteins from heterologous cells. J Biol Chem 1994; 269:21951-21954.
    • (1994) J Biol Chem , vol.269 , pp. 21951-21954
    • Leiper, J.M.1    Bayliss, J.D.2    Pease, R.J.3    Brett, D.J.4    Scott, J.5    Shoulders, C.C.6
  • 76
    • 0033230418 scopus 로고    scopus 로고
    • Developmental fate of the yolk protein lipovitellin in embryos and larvae of winter flounder, Pleuronectes americanus
    • Hartling RC, Kunkel JG. Developmental fate of the yolk protein lipovitellin in embryos and larvae of winter flounder, Pleuronectes americanus. J Exp Zool 1999; 284:686-695.
    • (1999) J Exp Zool , vol.284 , pp. 686-695
    • Hartling, R.C.1    Kunkel, J.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.