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Titolo:
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
Autore:
Matsubara, T; Ohkubo, N; Andoh, T; Sullivan, CV; Hara, A;
Indirizzi:
Hokkaido Natl Fisheries Res Inst, Kushiro, Hokkaido 085, Japan Hokkaido Natl Fisheries Res Inst Kushiro Hokkaido Japan 085 do 085, Japan N Carolina State Univ, Dept Zool, Raleigh, NC 27695 USA N Carolina State Univ Raleigh NC USA 27695 pt Zool, Raleigh, NC 27695 USA Hokkaido Univ, Fac Fisheries, Dept Biol, Hakodate, Hokkaido 0410821, JapanHokkaido Univ Hakodate Hokkaido Japan 0410821 te, Hokkaido 0410821, Japan
Titolo Testata:
DEVELOPMENTAL BIOLOGY
fascicolo: 1, volume: 213, anno: 1999,
pagine: 18 - 32
SICI:
0012-1606(19990901)213:1<18:TFOVYT>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
FREE AMINO-ACIDS; HALIBUT HIPPOGLOSSUS-HIPPOGLOSSUS; PRECURSOR-PRODUCT RELATIONSHIP; SALMON ONCORHYNCHUS-KISUTCH; TURBOT SCOPHTHALMUS-MAXIMUS; YOLK-SAC LARVAE; XENOPUS-LAEVIS; FUNDULUS OOCYTES; PROTEOLYTIC CLEAVAGE; OREOCHROMIS-AUREUS;
Keywords:
vitellogenin; yolk protein; lipovitellin; phosvitin; beta '-component; vitellogenesis; yolk proteolysis; oocyte maturation; teleost;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Matsubara, T Hokkaido Natl Fisheries Res Inst, 116 Katsurakoi, Kushiro, Hokkaido 085, Japan Hokkaido Natl Fisheries Res Inst 116 Katsurakoi Kushiro Hokkaido Japan 085
Citazione:
T. Matsubara et al., "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", DEVELOP BIO, 213(1), 1999, pp. 18-32

Abstract

Two forms of vitellogenin (Vg), Vg A and Vg B, were identified in serum from estrogen-treated barfin flounder (Verasper moseri). Structural changes of lipovitellins (Lvs) derived from the two Vgs were examined during vitellogenesis and oocyte maturation. Two Lvs, vLv A and vLv B, were identified electrophoretically and immunologically in postvitellogenic oocytes. Each appeared to be composed of distinct heavy chains (vLvH A, M-r 107,000, and vLvH B, M-r 94,000) and light chains (vLvL A, M-r 30,000, and vLvL B, M-r 28,000) when analyzed by SDS-PAGE. Results from N-terminal amino acid sequencing and Western blotting using antisera to vLvH A and vLvH B verified that there are two Vg polypeptides in serum from estrogen-treated fish, Vg A (M-r 168,000) and Vg B (M-r 175,000), which give rise to vLvH A-vLvL A and vLvH B-vLvL B, respectively. N-terminal sequencing revealed two sequences for both phosvitin and beta-component, supporting the concept of duality for all three classes of Vg-derived yolk proteins. During oocyte maturation, nativedimeric vLv B was dissociated into a native M, 170,000 monomer (oLv B). Meanwhile, vLv A was extensively cleaved including complete degradation of vLvH A into free amino acids. We propose that the quantitative ratio of vLv Ato vLv B in postvitellogenic. oocytes regulates the buoyancy of the spawned pelagic eggs by controlling availability of free amino acids which function as osmotic effecters during oocyte hydration. The vLv A/vLv B ratio likely also controls the proportional availability of different types of nutrients, free amino acids versus Lv, for use during embryonic development. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/08/20 alle ore 07:03:29