Molecular characterization of a cDNA encoding vitellogenin in the coonstriped shrimp, Pandalus hypsinotus and site of vitellogenin mRNA expression

Naoaki Tsutsui, Hisako Saido-Sakanaka, Wei J. Yang, Vidya Jayasankar, Safiah Jasmani, Atsuro Okuno, Tsuyoshi Ohira, Takuji Okumura, Katsumi Aida, Marcy N. Wilder

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

In order to determine the primary structure of vitellogenin in a protandric species, the coonstriped shrimp Pandalus hypsinotus, we previously purified four vitellin components (designated as VnA, VnB, VnC, and VnD, respectively), and chemically analyzed their partial amino acid sequences. In this study, we subsequently cloned a cDNA encoding vitellogenin in this species based on the N-terminal and internal amino acid sequences of VnA, as well as the N-terminal sequence of VnC. The open reading frame of this cDNA encoded a pro-vitellogenin in which vitellins were arranged as follows: NH2-VnA-VnB-VnC/D-COOH. The deduced amino acid sequence possessed a single consensus cleavage sequence, R-X-K/R-R, along the lines of vitellogenins reported in other crustaceans and insects, and the N-terminal sequence of VnB was immediately preceded by this sequence. The comparison of primary structures revealed the existence of a basic and characteristic structure for the vitellogenin molecule in decapod crustacean species, and phylogenetic analysis reflected the current taxonomic classifications of Crustacea. An approximately 8 kb-long transcript of the vitellogenin gene was detected in the hepatopancreas of female shrimps having a gonadosomatic index higher than 1.0 by Northern blot analysis, but was not observed in the hepatopancreas and gonads of male shrimps and the hepatopancreas of female shrimps having a gonadosomatic index lower than 1.0. These results indicate that the hepatopancreas is responsible for vitellogenin synthesis.

Original languageEnglish
Pages (from-to)802-814
Number of pages13
JournalJournal of Experimental Zoology Part A: Comparative Experimental Biology
Volume301
Issue number10
DOIs
Publication statusPublished - Oct 1 2004
Externally publishedYes

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Pandalus
vitellogenin
shrimp
hepatopancreas
vitellin
amino acid sequences
Crustacea
gonadosomatic index
Northern blotting
Decapoda
open reading frames
gonads
insects
synthesis
phylogeny

ASJC Scopus subject areas

  • Animal Science and Zoology

Cite this

Molecular characterization of a cDNA encoding vitellogenin in the coonstriped shrimp, Pandalus hypsinotus and site of vitellogenin mRNA expression. / Tsutsui, Naoaki; Saido-Sakanaka, Hisako; Yang, Wei J.; Jayasankar, Vidya; Jasmani, Safiah; Okuno, Atsuro; Ohira, Tsuyoshi; Okumura, Takuji; Aida, Katsumi; Wilder, Marcy N.

In: Journal of Experimental Zoology Part A: Comparative Experimental Biology, Vol. 301, No. 10, 01.10.2004, p. 802-814.

Research output: Contribution to journalArticle

Tsutsui, Naoaki ; Saido-Sakanaka, Hisako ; Yang, Wei J. ; Jayasankar, Vidya ; Jasmani, Safiah ; Okuno, Atsuro ; Ohira, Tsuyoshi ; Okumura, Takuji ; Aida, Katsumi ; Wilder, Marcy N. / Molecular characterization of a cDNA encoding vitellogenin in the coonstriped shrimp, Pandalus hypsinotus and site of vitellogenin mRNA expression. In: Journal of Experimental Zoology Part A: Comparative Experimental Biology. 2004 ; Vol. 301, No. 10. pp. 802-814.
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T1 - Molecular characterization of a cDNA encoding vitellogenin in the coonstriped shrimp, Pandalus hypsinotus and site of vitellogenin mRNA expression

AU - Tsutsui, Naoaki

AU - Saido-Sakanaka, Hisako

AU - Yang, Wei J.

AU - Jayasankar, Vidya

AU - Jasmani, Safiah

AU - Okuno, Atsuro

AU - Ohira, Tsuyoshi

AU - Okumura, Takuji

AU - Aida, Katsumi

AU - Wilder, Marcy N.

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AB - In order to determine the primary structure of vitellogenin in a protandric species, the coonstriped shrimp Pandalus hypsinotus, we previously purified four vitellin components (designated as VnA, VnB, VnC, and VnD, respectively), and chemically analyzed their partial amino acid sequences. In this study, we subsequently cloned a cDNA encoding vitellogenin in this species based on the N-terminal and internal amino acid sequences of VnA, as well as the N-terminal sequence of VnC. The open reading frame of this cDNA encoded a pro-vitellogenin in which vitellins were arranged as follows: NH2-VnA-VnB-VnC/D-COOH. The deduced amino acid sequence possessed a single consensus cleavage sequence, R-X-K/R-R, along the lines of vitellogenins reported in other crustaceans and insects, and the N-terminal sequence of VnB was immediately preceded by this sequence. The comparison of primary structures revealed the existence of a basic and characteristic structure for the vitellogenin molecule in decapod crustacean species, and phylogenetic analysis reflected the current taxonomic classifications of Crustacea. An approximately 8 kb-long transcript of the vitellogenin gene was detected in the hepatopancreas of female shrimps having a gonadosomatic index higher than 1.0 by Northern blot analysis, but was not observed in the hepatopancreas and gonads of male shrimps and the hepatopancreas of female shrimps having a gonadosomatic index lower than 1.0. These results indicate that the hepatopancreas is responsible for vitellogenin synthesis.

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