Characterization and expression profile of Vitellogenin gene from Scylla paramamosain

被引:89
作者
Jia, Xiwei [1 ]
Chen, Yudong [1 ]
Zou, Zhihua [1 ]
Lin, Peng [1 ]
Wang, Yilei [1 ]
Zhang, Ziping [2 ]
机构
[1] Jimei Univ, Coll Fisheries, Minist Agr, Key Lab Hlth Mariculture East China Sea, Xiamen 361021, Peoples R China
[2] Seton Hall Univ, Dept Biol Sci, S Orange, NJ 07079 USA
关键词
Vitellogenin; Ovary; Hepatopancreas; Gene expression; Scylla paramamosain; CDNA-ENCODING VITELLOGENIN; MESSENGER-RNA EXPRESSION; FRESH-WATER PRAWN; MOLECULAR CHARACTERIZATION; KURUMA PRAWN; CALLINECTES-SAPIDUS; BANANA SHRIMP; BLUE-CRAB; IN-VITRO; BINDING;
D O I
10.1016/j.gene.2013.02.035
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
The full-length (7816 bp) cDNA of Vitellogenin (Vtg) encoding 2560 aa with an estimated molecular mass of 287.743 kDa was cloned from the green mud crab Scylla paramamosain. Semi-quantitative PCR (sq-PCR) revealed a specific expression pattern of Sp-vtg gene in ovaries and hepatopancreas. With the development of ovaries, the expression level of Sp-vtg gene showed an increasing trend both in ovaries and hepatopancreas, and the expression level of Sp-vtg gene in hepatopancreas and ovary was stable after stage IV. By in situ hybridization, the positive signals of Sp-vtg gene were detected in the cytoplasm of oocytes in stage I, in the follicle cell and the surrounding of the nucleus in stage III, and in the nucleus in stage V. Furthermore, the signals become stronger with the later development stages of ovary. Moreover, in situ hybridization analysis revealed that positive signals of Sp-vtg gene are present in the hepatopancreatic tubule, and the signals increase during the development, becoming the strongest in stage V. Our results indicate that both ovaries and hepatopancreas are sites of Vitellogenin gene synthesis in S. paramamosain. (c) 2013 Elsevier B.V. All rights reserved.
引用
收藏
页码:119 / 130
页数:12
相关论文
共 49 条
[1]   The vitellogenin cDNA of Cherax quadricarinatus encodes a lipoprotein with calcium binding ability, and its expression is induced following the removal of the androgenic gland in a sexually plastic system [J].
Abdu, U ;
Davis, C ;
Khalaila, I ;
Sagi, A .
GENERAL AND COMPARATIVE ENDOCRINOLOGY, 2002, 127 (03) :263-272
[2]   The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein [J].
Anderson, TA ;
Levitt, DG ;
Banaszak, LJ .
STRUCTURE WITH FOLDING & DESIGN, 1998, 6 (07) :895-909
[3]   DISTRIBUTION OF CAROTENOIDS IN THE EGGS FROM 4 SPECIES OF SALMONIDS [J].
ANDO, S ;
HATANO, M .
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 1991, 99 (02) :341-344
[4]  
AZUMA M, 1993, J EXP BIOL, V178, P89
[5]   BINDING OF THYROXINE AND 3,5,3'-TRIIODOTHYRONINE TO TROUT PLASMA-LIPOPROTEINS [J].
BABIN, PJ .
AMERICAN JOURNAL OF PHYSIOLOGY, 1992, 262 (05) :E712-E720
[6]   VITELLIN SYNTHESIS IN RELATION TO OOGENESIS IN INVITRO-INCUBATED OVARIES OF PENAEUS-SEMISULCATUS (CRUSTACEA, DECAPODA, PENAEIDAE) [J].
BROWDY, CL ;
FAINZILBER, M ;
TOM, M ;
LOYA, Y ;
LUBZENS, E .
JOURNAL OF EXPERIMENTAL ZOOLOGY, 1990, 255 (02) :205-215
[7]   THE EVOLUTION OF EGG-YOLK PROTEINS [J].
BYRNE, BM ;
GRUBER, M ;
AB, G .
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 1989, 53 (01) :33-69
[8]   Extensive sequence conservation among insect, nematode, and vertebrate vitellogenins reveals ancient common ancestry [J].
Chen, JS ;
Sappington, TW ;
Raikhel, AS .
JOURNAL OF MOLECULAR EVOLUTION, 1997, 44 (04) :440-451
[9]   Yolk protein expression in the green crab, Carcinus maenas [J].
Ding, X. ;
Nagaraju, G. P. C. ;
Novotney, D. ;
Lovett, D. L. ;
Borst, D. W. .
AQUACULTURE, 2010, 298 (3-4) :325-331
[10]   BINDING OF METALS TO RED DRUM VITELLOGENIN AND INCORPORATION INTO OOCYTES [J].
GHOSH, P ;
THOMAS, P .
MARINE ENVIRONMENTAL RESEARCH, 1995, 39 (1-4) :165-168