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

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

doi:10.1002/jez.a.53

Cited by 51 publications

(21 citation statements)

References 37 publications

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“…Additional sequences of LLTPs from arachnids may help define the context of the divergence of M-177. Importantly, the Vtg of decapodan Crustacea is not directly related to the Vtg genes of other taxons, as assumed by others (52)(53)(54)(55)(56)(57)(58)(59)(60), but is an apoB-like LLTP. This observation explains previous phylogenetic analyses on Vtgs only (57,62,69,70), in which decapodan Vtg failed to group with other invertebrate Vtgs.…”

Section: Three Families Of Lltpsmentioning

confidence: 87%

“…In another class of arthropods, the decapodan Crustacea (e.g., lobster, crayfish, crab, shrimp), two distinct LLTPs have been identified, a CP (7,8) and a yolk protein named Vtg (52)(53)(54)(55)(56)(57)(58)(59)(60). Although both LLTPs have been identified only in distinct species, the relatively close relationship among these species as well as the divergence of the identified proteins strongly suggest that the subset of LLTPs present in decapodan Crustacea con-sists at least of one CP and one Vtg.…”

Section: Lltp Family Membersmentioning

confidence: 99%

“…In view of the presence of other Vtg-like LLTPs in insects (e.g., Vtgs), MEP appears to originate from a duplicated Vtg gene that has been retained as a result of the acquisition of a novel function. CP, the single Vtg-like LLTP identified in decapodan Crustacea to date, may represent another example of neofunctionalization, as this protein functions as the major hemolymph coagulogen rather than as a yolk protein (7,8,50,52,53). In the same taxon, an apoB-like LLTP, named Vtg, constitutes the major yolk protein, rather than a Vtg-like LLTP as in most animals.…”

Section: A Role For Functional Dynamics In the Expansion Of Lltp Famimentioning

confidence: 99%

“…104). Putative cleavage sites are also present in the apoB-like Vtg of decapodan Crustacea at the same location (52)(53)(54)(55)(56)(57)(58)(59)(60), and also in some insect Vtgs at vary-ing locations in the LLT module (for review, see Ref. 4).…”

Section: Correlating Diversity In Structure and Functionmentioning

confidence: 99%

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Molecular diversity and evolution of the large lipid transfer protein superfamily

Smolenaars

Madsen

Rodenburg

et al. 2007

Journal of Lipid Research

153

160

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Circulatory lipid transport in animals is mediated to a substantial extent by members of the large lipid transfer (LLT) protein (LLTP) superfamily. These proteins, including apolipoprotein B (apoB), bind lipids and constitute the structural basis for the assembly of lipoproteins. The current analyses of sequence data indicate that LLTPs are unique to animals and that these lipid binding proteins evolved in the earliest multicellular animals. In addition, two novel LLTPs were recognized in insects. Structural and phylogenetic analyses reveal three major families of LLTPs: the apoB-like LLTPs, the vitellogenin-like LLTPs, and the microsomal triglyceride transfer protein (MTP)-like LLTPs, or MTPs. The latter are ubiquitous, whereas the two other families are distributed differentially between animal groups. Besides similarities, remarkable variations are also found among LLTPs in their major lipid-binding sites (i.e., the LLT module as well as the predicted clusters of amphipathic secondary structure): variations such as protein modification and number, size, or occurrence of the clusters. Strikingly, comparative research has also highlighted a multitude of functions for LLTPs in addition to circulatory lipid transport. The integration of LLTP structure, function, and evolution reveals multiple adaptations, which have come about in part upon neofunctionalization of duplicated genes. Moreover, the change, exchange, and expansion of functions illustrate the opportune application of lipid-binding proteins in nature.Accordingly, comparative research exposes the structural and functional adaptations in animal lipid carriers and brings up novel possibilities for the manipulation of lipid transport.

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Section: Three Families Of Lltpsmentioning

confidence: 87%

Section: Lltp Family Membersmentioning

confidence: 99%

Section: A Role For Functional Dynamics In the Expansion Of Lltp Famimentioning

confidence: 99%

Section: Correlating Diversity In Structure and Functionmentioning

confidence: 99%

See 2 more Smart Citations

Molecular diversity and evolution of the large lipid transfer protein superfamily

Smolenaars

Madsen

Rodenburg

et al. 2007

Journal of Lipid Research

153

160

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“…Most are from the commercially important penaeid shrimps in the suborder of Dendrobranchiata, including Marsupenaeus japonicus (Tsutsui et al, 2000), Penaeus monodon (Tiu et al, 2006), Litopenaeus vannamei (Raviv et al, 2006), Penaeus semisulcatus (Avarre et al, 2003), Fenneropenaeus chinensis (Xie et al, 2009), Fenneropenaeus merguiensis (Phiriyangkul and Utarabhand, 2006), and Pandalopsis japonica (Jeon et al, 2010). Others are from brachyuran and *Corresponding author: kimhw@pknu.ac.kr astacidean species in the suborder Pleocyemata, including Macrobrachium rosenbergii (Okuno et al, 2002), Pandalus hypsinotus (Tsutsui et al, 2004), Portunus trituberculatus (Yang et al, 2005), Cherax quadricarinatus (Abdu et al, 2002), Homarus americanus (Tiu et al, 2009), Upogebia major (Kang et al, 2008), Charybdis feriatus (Mak et al, 2005), Portunus trituberculatus (Yang et al, 2005), and Callinectes sapidus (Zmora et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Structural Similarity and Expression Differences of Two Pj-Vg Genes from the Pandalus Shrimp Pandalopsis japonica

Jeon¹,

Kim²,

Kim³

et al. 2011

Fisheries and aquatic sciences

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Vitellogenin (Vg) is the precursor of vitellin (Vn), which is the major yolk protein in nearly all oviparous species, including fish, amphibians, reptiles, and most invertebrates. It is one of the most important factors during reproduction, and numerous studies have shown that Vg genes are markers of the reproductive cycle and effecter genes induced by endocrine-disrupting chemicals (EDCs). Previously, we isolated two distinct cDNAs encoding vitellogenin homologs Pj-Vg1 and Pj-Vg2 from Pandalus shrimp Pandalopsis japonica. In this study, full-length genomic sequences of Pj-Vg1 and Pj-Vg2 were determined using a PCR-based genome walking strategy. Isolated Pj-Vg1 and Pj-Vg2 genes were 11,910 and 11,850 bp long, respectively. Both Pj-Vg genes had 15 exons and 14 introns, and the splicing sites were also the same, suggesting that they arose via gene duplication. The similar structural characteristics of decapod Vg genes suggest that they are all orthologs that evolved from the same ancestral gene. Analysis of Pj-Vg1 and Pj-Vg2 expression revealed that the relative copy numbers of Pj-Vg1 and Pj-Vg2 were similar in the hepatopancreas, whereas Pj-Vg2 transcripts were also detected in the ovary. Expression of both Pj-Vg genes was induced in hepatopancreas of mature individuals, whereas only Pj-Vg2 transcripts were upregulated in the ovaries from mature animals, suggesting that both Pj-Vgs are important for oocyte development. A strong positive correlation was found between Pj-Vg1 and Pj-Vg2 transcripts in the same individual, indicating they are under the same control mechanisms. Additionally, a positive correlation was found between ovarian and hepatopancreatic Pj-Vg2 transcripts, suggesting that its dual expression is regulated by similar physiological conditions. Knowledge of the similarities and differences between the two vitellogenin-like genes, Pj-Vg1 and Pj-Vg2, would help us to understand their roles in reproduction and other physiological effects.

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

Cited by 51 publications

References 37 publications

Molecular diversity and evolution of the large lipid transfer protein superfamily

Molecular diversity and evolution of the large lipid transfer protein superfamily

Structural Similarity and Expression Differences of Two Pj-Vg Genes from the Pandalus Shrimp Pandalopsis japonica

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

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