Characterization of vitellin from the ovaries of the banana shrimp Litopenaeus merguiensis

Auttarat, Jongruk; Phiriyangkul, Pharima; Utarabhand, Prapaporn

doi:10.1016/j.cbpb.2005.09.009

Cited by 32 publications

(21 citation statements)

References 53 publications

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“…Results from RT-PCR analysis showed that Vg mRNA expression occurred in both the ovary and the hepatopancreas of vitellogenic females and both of them are possible sites for Vg synthesis in P. merguiensis . Quantification of Vg in the hemolymph and ovarian Vt by ELISA during various stages of vitellogenesis confirmed that the contribution of Vg synthesized by the hepatopancreas alone might be insufficient to adequately account for the development of the oocytes in this shrimp species (Auttarat et al, 2006). In the present study we clearly identify Vg as the extraovarian protein present in the hemolymph and hepatopancreas while Vt is the major intraovarian protein.…”

Section: Introductionsupporting

confidence: 71%

“…Sodium dodecyl sulphatepolyacrylamide gel electrophoresis (SDS-PAGE) of purified Vt showed that it was composed of two major subunits that appeared to be arranged in doublets of 87 and 78 kDa and one minor 104-kDa subunit. The Nterminal amino acid sequence of the 78-kDa subunit of P. merguiensis Vt was very similar to the corresponding Vt sequences of some penaeid shrimps (Auttarat et al, 2006), but was less similar to the Vg of the freshwater prawn M. rosenbergii . In addition, cDNA encoding Vg has been cloned based on the Nterminal amino acid sequence of the 78-kDa subunit of purified Vt and conserved sequences of Vg/Vt from other crustacean species.…”

Section: Introductionmentioning

confidence: 63%

“…This site corresponds to a consensus motif (R-X-X-R) recognized by the subtilisin endoprotease family or other endoprotease enzymes (Barr, 1991;Chen et al, 1997). Moreover, purified P. merguiensis Vt is a lipoglycocaroteno-protein (Auttarat et al, 2006). As the N-terminal amino acid sequences of the 78-and 87-kDa subunits are identical, this suggests there is post-translational modification by Molecular Reproduction and Development.…”

Section: Discussionmentioning

confidence: 96%

“…In previous studies, we have purified and characterized Vt from the ovaries of vitellogenic females of the banana shrimp Penaeus merguiensis, as this is one of the most important species for aquaculture in Thailand (Auttarat et al, 2006). Sodium dodecyl sulphatepolyacrylamide gel electrophoresis (SDS-PAGE) of purified Vt showed that it was composed of two major subunits that appeared to be arranged in doublets of 87 and 78 kDa and one minor 104-kDa subunit.…”

Section: Introductionmentioning

confidence: 99%

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Dynamics of vitellogenin mRNA expression during vitellogenesis in the banana shrimp Penaeus (Fenneropenaeus) merguiensis using real‐time PCR

Phiriyangkul

Puengyam

Jakobsen

et al. 2007

Molecular Reproduction Devel

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An open reading frame (ORF) of vitellogenin (Vg) cDNA was amplified from the ovaries of the banana shrimp, Penaeus merguiensis. An examination of Vg-deduced amino acid sequence revealed the presence of cleavage sites at a consensus motif for subtilisin-like endoproteases prior to the N-terminal sequences of purified vitellin (Vt) subunits. A comparison of the primary structures of Vg molecules in decapod crustacean species revealed the existence of a common characteristic structure, and phylogenetic analysis reflected the current taxonomic classifications of crustaceans. A PCR product of 1.1 kb encoding the 3'-end of Vg cDNA was cloned from the hepatopancreas. Although its sequence was almost identical to that of the same region of the ovarian Vg, with only 18 nucleotide differences, analysis suggests that they have been subjected to natural selection, indicating that there may be two different, tissue-specific Vg genes in P. merguiensis. This is consistent with the different expression patterns of Vg mRNA, as determined by real-time PCR. Vg mRNA levels were maintained at low levels during the previtellogenic stage and they increased as vitellogenesis progressed to reach a peak at the early vitellogenic stage in the ovary or at the vitellogenic stage in the hepatopancreas, and thereafter, levels decreased. Expression of Vg mRNA was much higher in the ovary compared to the hepatopancreas at all stages of ovarian development, implying that the ovary is mainly responsible for Vt synthesis. These indicate that penaeids constitute a unique model for vitellogenesis, showing intraovarian gene expression and synthesis of yolk protein.

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Section: Introductionsupporting

confidence: 71%

Section: Introductionmentioning

confidence: 63%

Section: Discussionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

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Dynamics of vitellogenin mRNA expression during vitellogenesis in the banana shrimp Penaeus (Fenneropenaeus) merguiensis using real‐time PCR

Phiriyangkul

Puengyam

Jakobsen

et al. 2007

Molecular Reproduction Devel

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“…The rapidly increasing list of characterized crustacean VTG genes includes those from penaeids [15,23,[33][34][35], crayfish [36], prawns [19,37], and two brachyuran species [38,39]. From these reports, data have emerged indicating that VTG expression takes place in the hepatopancreas of Pleocyamata (including brachyurans), while in the Dendrobranchiata, both the hepatopancreas and the ovary express VTG [15,[33][34][35]. However, the relative contribution of each tissue during vitellogenesis, either at the mRNA or protein level, remains unclear.…”

Section: Introductionmentioning

confidence: 94%

Vitellogenin and Its Messenger RNA During Ovarian Development in the Female Blue Crab, Callinectes sapidus: Gene Expression, Synthesis, Transport, and Cleavage1

Zmora

Trant

Chan

et al. 2007

Biology of Reproduction

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Blue crab vitellogenin (VTG) cDNA encodes a precursor that, together with two other Brachyuran VTGs, forms a distinctive cluster within a phylogenetic tree of crustacean VTGs. Using quantitative RT-PCR, we found that VTG was primarily expressed in the hepatopancreas of a vitellogenic female, with minor expression in the ovary. VTG expression in the hepatopancreas correlated with ovarian growth, with a remarkable 8000-fold increase in expression from stage 3 to 4 of ovarian development. In contrast, the VTG levels in the hepatopancreas and hemolymph decreased in stage 4. Western blot analysis and N-terminal sequencing revealed that vitellin is composed of three subunits of approximately 78.5 kDa, 119.42 kDa, and 87.9 kDa. The processing pathway for VTG includes an initial hepatopancreatic cleavage of the primary precursor into approximately 78.5-kDa and 207.3-kDa subunits, both of which are found in the hemolymph. A second cleavage in the ovary splits the approximately 207.3-kDa subunit into approximately 119.4-kDa and approximately 87.9-kDa subunits. The hemolymph VTG profiles of mated and unmated females during ovarian development indicate that early vitellogenesis and ovarian development do not require mating, which may be essential for later stages, as VTG decreased to the basal level at stage 4 in the unmated group but remained high in the mated females. Our results encompass comprehensive overall temporal and spatial aspects of vitellogenesis, which may reflect the reproductive physiology of the female blue crab, e.g., single mating and anecdysis in adulthood.

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Molecular characterization of a cDNA encoding vitellogenin in the banana shrimp, Penaeus (Litopenaeus) merguiensis and sites of vitellogenin mRNA expression

Phiriyangkul¹,

Utarabhand²

2006

Molecular Reproduction Devel

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In order to determine the primary structure of banana shrimp, Penaeus merguiensis, vitellogenin (Vg), we previously purified vitellin (Vt) from the ovaries of vitellogenic females, and chemically analyzed the N-terminal amino acid sequence of its 78 kDa subunit. In this study, a cDNA from this species encoding Vg was cloned based on the N-terminal amino acid sequence of the major 78 kDa subunit of Vt and conserved sequences of Vg/Vt from other crustacean species. The complete nucleotide sequence of Vg cDNA was achieved by RT-PCR and 5' and 3' rapid amplification of cDNA ends (RACE) approaches. The full-length Vg cDNA consisted of 7,961 nucleotides. The open reading frame of this cDNA encoding a precursor peptide was comprised of 2,586 amino acid residues, with a putative processing site, R-X-K/R-R, recognized by subtilisin-like endoproteases. The deduced amino acid sequence was obtained from the Vg cDNA and its amino acid composition showed a high similarity to that of purified Vt. The deduced primary structure, of P. merguiensis Vg was 91.4% identical to the Vg of Penaeus semisulcatus and was also related to the Vg sequences of six other crustacean species with identities that ranged from 86.9% to 36.6%. In addition, the amino acid sequences corresponding to the signal peptide, N-terminal region and C-terminal region of P. merguiensis Vg were almost identical to the same sequences of the seven other reported crustacean species. Results from RT-PCR analysis showed that Vg mRNA expression was present in both the ovary and hepatopancreas of vitellogenic females but was not detected in other tissues including muscle, heart, and intestine of females or in the hepatopancreas of mature males. These results indicate that the Vg gene may be expressed only by mature P. merguiensis females and that both the ovary and hepatopancreas are possible sites for Vg synthesis in this species of shrimp.

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Characterization of vitellin from the ovaries of the banana shrimp Litopenaeus merguiensis

Cited by 32 publications

References 53 publications

Dynamics of vitellogenin mRNA expression during vitellogenesis in the banana shrimp Penaeus (Fenneropenaeus) merguiensis using real‐time PCR

Dynamics of vitellogenin mRNA expression during vitellogenesis in the banana shrimp Penaeus (Fenneropenaeus) merguiensis using real‐time PCR

Vitellogenin and Its Messenger RNA During Ovarian Development in the Female Blue Crab, Callinectes sapidus: Gene Expression, Synthesis, Transport, and Cleavage1

Molecular characterization of a cDNA encoding vitellogenin in the banana shrimp, Penaeus (Litopenaeus) merguiensis and sites of vitellogenin mRNA expression

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