메뉴 건너뛰기




Volumn 135, Issue 1, 2003, Pages 71-81

Cleavage site of a major yolk protein (MYP) determined by cDNA isolation and amino acid sequencing in sea urchin, Hemicentrotus pulcherrimus

Author keywords

Development; Echinoferrin; Egg; Embryo; Hemicentrotus pulcherrimus; Ovary; Proteolysis; Sea urchin; Transferrin; Yolk protein

Indexed keywords

AMINO ACID; COMPLEMENTARY DNA; ECHINOFERRIN; MAJOR YOLK PROTEIN; NUCLEOTIDE; PROTEIN; TRANSFERRIN; UNCLASSIFIED DRUG; YOLK PROTEIN;

EID: 0038021500     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1096-4959(03)00084-8     Document Type: Article
Times cited : (44)

References (30)
  • 1
    • 0022538256 scopus 로고
    • Characterization of yolk platelets isolated from developing embroyos of Arbacia punctulata
    • Armant D.R., Carson D.D., Decker G.L., Welpy J.K., Lennarz W.J. Characterization of yolk platelets isolated from developing embroyos of Arbacia punctulata. Dev. Biol. 113:1986;342-355.
    • (1986) Dev. Biol. , vol.113 , pp. 342-355
    • Armant, D.R.1    Carson, D.D.2    Decker, G.L.3    Welpy, J.K.4    Lennarz, W.J.5
  • 2
    • 0036570143 scopus 로고    scopus 로고
    • The major yolk protein in sea urchin is a transferrin-like, iron-binding protein
    • Brooks J.M., Wessel G.M. The major yolk protein in sea urchin 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
  • 3
    • 0033045252 scopus 로고    scopus 로고
    • Maternal factors and the evolution of developmental mode: Evolution of oogenesis in Heliocidaris erythrogramma
    • Byrne M., Villinski J.T., Cisternas P., Siegel R.K., Popodi E., Raff R.A. Maternal factors and the evolution of developmental mode: evolution of oogenesis in Heliocidaris erythrogramma. Dev. Genes Evol. 209:1999;275-283.
    • (1999) Dev. Genes Evol. , vol.209 , pp. 275-283
    • Byrne, M.1    Villinski, J.T.2    Cisternas, P.3    Siegel, R.K.4    Popodi, E.5    Raff, R.A.6
  • 4
    • 0024587474 scopus 로고
    • Evidence of a precursor-product relationship between vitellogenin and toposome, a glycoprotein complex mediating cell adhesion
    • Cervello M., Matranga V. Evidence of a precursor-product relationship between vitellogenin and toposome, a glycoprotein complex mediating cell adhesion. Cell Differentiation. 26:1989;67-76.
    • (1989) Cell Differentiation , vol.26 , pp. 67-76
    • Cervello, M.1    Matranga, V.2
  • 5
    • 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;505-598.
    • (1982) Dev. Biol. , vol.94 , pp. 505-598
    • Harrington, F.E.1    Easton, D.P.2
  • 6
    • 0034185884 scopus 로고    scopus 로고
    • A juvenile hormone-repressible transferrin-like protein from the bean bag, Riptortus clavatus: CDNA sequence analysis and protein identification during diapause and vitellogenesis
    • Hirai M., Watanabe D., Chinzei Y. A juvenile hormone-repressible transferrin-like protein from the bean bag, Riptortus clavatus: cDNA sequence analysis and protein identification during diapause and vitellogenesis. Arch. Insect Biochem. Physiol. 33:2000;17-26.
    • (2000) Arch. Insect Biochem. Physiol. , vol.33 , pp. 17-26
    • Hirai, M.1    Watanabe, D.2    Chinzei, Y.3
  • 7
    • 0026325647 scopus 로고
    • An LRE (leucine-arginine-glutamate)-dependent mechanism for adhesion of neurons to S-laminin
    • Hunter D.D., Cashman N., Morris-Valero R., Bulock J.W., Adams S.P., Sanes J.R. An LRE (leucine-arginine-glutamate)-dependent mechanism for adhesion of neurons to S-laminin. J. Neurosci. 11:1991;3960-3971.
    • (1991) J. Neurosci. , vol.11 , pp. 3960-3971
    • Hunter, D.D.1    Cashman, N.2    Morris-Valero, R.3    Bulock, J.W.4    Adams, S.P.5    Sanes, J.R.6
  • 8
    • 0021996303 scopus 로고
    • Analysis of changes in a yolk glycoprotein complex in the developing sea urchin embryo
    • Kari B.E., Rottmann W.L. Analysis of changes in a yolk glycoprotein complex in the developing sea urchin embryo. Dev. Biol. 108:1985;18-25.
    • (1985) Dev. Biol. , vol.108 , pp. 18-25
    • Kari, B.E.1    Rottmann, W.L.2
  • 9
    • 0028954469 scopus 로고
    • Mouse complement regulatory protein Crry/p65 uses the specific mechanisms of both human decay accelerating facto and membrane cofactor protein
    • Kim Y.U., Kinoshita T., Molina H., et al. Mouse complement regulatory protein Crry/p65 uses the specific mechanisms of both human decay accelerating facto and membrane cofactor protein. J. Exp. Med. 181:1995;151-159.
    • (1995) J. Exp. Med. , vol.181 , pp. 151-159
    • Kim, Y.U.1    Kinoshita, T.2    Molina, H.3
  • 10
    • 0025255536 scopus 로고
    • The murine complement receptor gene family. IV. Alternative splicing of Cr2 gene transcripts predicts two distinct gene products that share homologous domains with both human Cr2 and Cr1
    • Kurtz C.B., O'toole E., Christensen S.M., Weis J.H. The murine complement receptor gene family. IV. Alternative splicing of Cr2 gene transcripts predicts two distinct gene products that share homologous domains with both human Cr2 and Cr1. J. Immunol. 144:1990;3581-3591.
    • (1990) J. Immunol. , vol.144 , pp. 3581-3591
    • Kurtz, C.B.1    O'toole, E.2    Christensen, S.M.3    Weis, J.H.4
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London). 227:1970;680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 0024510734 scopus 로고
    • Developmentally regulated processing of a yolk glycoprotein complex in embryos of the sea urchin, Strongylocentrotus purpuratus
    • Lee G.F., Fanning E.W., Small M.P., Hille M.B. Developmentally regulated processing of a yolk glycoprotein complex in embryos of the sea urchin, Strongylocentrotus purpuratus. Cell Differentiation Dev. 26:1989;5-18.
    • (1989) Cell Differentiation Dev. , vol.26 , pp. 5-18
    • Lee, G.F.1    Fanning, E.W.2    Small, M.P.3    Hille, M.B.4
  • 13
    • 0026654988 scopus 로고
    • Proteolysis of the major yolk glycoproteins is regulated by acidification of the yolk platelets in sea urchin embryos
    • Mallaya S.K., Partin J.S., Valdizan M.C., Lennarz W.J. Proteolysis of the major yolk glycoproteins is regulated by acidification of the yolk platelets in sea urchin embryos. J. Cell Biol. 117:1992;1211-1221.
    • (1992) J. Cell Biol. , vol.117 , pp. 1211-1221
    • Mallaya, S.K.1    Partin, J.S.2    Valdizan, M.C.3    Lennarz, W.J.4
  • 14
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262:1987;10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 15
    • 0030603225 scopus 로고    scopus 로고
    • Characterization of vitellogenin from rainbow trout (Oncorhynchus mykiss)
    • Mouchel N., Trichet V., Betz A., Le Pennec J.P., Wolff J. Characterization of vitellogenin from rainbow trout (Oncorhynchus mykiss). Gene. 174:1996;59-64.
    • (1996) Gene , vol.174 , pp. 59-64
    • Mouchel, N.1    Trichet, V.2    Betz, A.3    Le Pennec, J.P.4    Wolff, J.5
  • 16
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson W.R., Lipman D.J. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA. 85:1988;2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 17
  • 18
    • 0001511468 scopus 로고
    • Variants of the cell recognition site of fibronectin that retain attachment-promoting activity
    • Pierschbacher M.D., Ruoslahti E. Variants of the cell recognition site of fibronectin that retain attachment-promoting activity. Proc. Natl. Acad. Sci. USA. 81:1984;5985-5988.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 5985-5988
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 19
    • 0024513147 scopus 로고
    • Structure of a major yolk glycoprotein and its processing pathway by limited proteolysis are conserved in echinoids
    • Scott L.B., Lennarz W.J. Structure of a major yolk glycoprotein and its processing pathway by limited proteolysis are conserved in echinoids. Dev. Biol. 132:1989;91-102.
    • (1989) Dev. Biol. , vol.132 , pp. 91-102
    • Scott, L.B.1    Lennarz, W.J.2
  • 20
  • 21
    • 0023663203 scopus 로고
    • A single gene encoding Vg in the sea urchin Strongylocentrotus purpuratus
    • Shyu A.B., Blumenthal T., Raff R.A. A single gene encoding Vg in the sea urchin Strongylocentrotus purpuratus. 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
  • 23
    • 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
  • 24
    • 0035593411 scopus 로고    scopus 로고
    • Cloning of cDNA encoding vitellogenin and its expression in red sea urchin Pseudocentrotus depressus
    • Unuma T., Okamoto H., Konishi K., Ohta H., Mori K. Cloning of cDNA encoding vitellogenin and its expression in 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
  • 25
    • 0032033553 scopus 로고    scopus 로고
    • Putative vitellogenin in coelomic fluid of echinothurioid sea urchin Araeosoma owstoni and Asthenosoma ijimai
    • Yokota Y., Amemiya S. Putative vitellogenin in coelomic fluid of echinothurioid sea urchin Araeosoma owstoni and Asthenosoma ijimai. Comp. Biochem. Physiol. A. 119:1998;801-805.
    • (1998) Comp. Biochem. Physiol. A , vol.119 , pp. 801-805
    • Yokota, Y.1    Amemiya, S.2
  • 26
    • 0023880046 scopus 로고
    • Degradation of yolk proteins in sea urchin eggs and embryos
    • Yokota Y., Kato K.H. Degradation of yolk proteins in sea urchin eggs and embryos. Cell Differentiation. 23:1988;191-200.
    • (1988) Cell Differentiation , vol.23 , pp. 191-200
    • Yokota, Y.1    Kato, K.H.2
  • 28
    • 0001100261 scopus 로고
    • Morphological and biochemical studies on yolk degradation in the sea urchin, Hemicentrotus pulcherrimus
    • Yokota Y., Kato K.H., Mita M. Morphological and biochemical studies on yolk degradation in the sea urchin, Hemicentrotus pulcherrimus. Zool. Sci. 10:1993;661-670.
    • (1993) Zool. Sci. , vol.10 , pp. 661-670
    • Yokota, Y.1    Kato, K.H.2    Mita, M.3
  • 29
    • 0030817280 scopus 로고    scopus 로고
    • Mosquito transferrin, an acute-phase protein that is up-regulated upon infection
    • Yoshiga T., Hernandez V.P., Fallon A.M., Law J.H. Mosquito transferrin, an acute-phase protein that is up-regulated upon infection. Proc. Natl. Acad. Sci. USA. 94:1997;12337-12342.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12337-12342
    • Yoshiga, T.1    Hernandez, V.P.2    Fallon, A.M.3    Law, J.H.4
  • 30
    • 0033106306 scopus 로고    scopus 로고
    • Drosophila melanogaster transferrin. Cloning, deduced protein sequence, expression during the life cycle, gene localization and up-regulation on bacterial infection
    • Yoshiga T., Gerogieva T., Dunklov B.C., Harizanova N., Ralchev K., Law J.H. Drosophila melanogaster transferrin. Cloning, deduced protein sequence, expression during the life cycle, gene localization and up-regulation on bacterial infection. Eur. J. Biochem. 260:1999;414-420.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 414-420
    • Yoshiga, T.1    Gerogieva, T.2    Dunklov, B.C.3    Harizanova, N.4    Ralchev, K.5    Law, J.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.