Role of the lysine and arginine residues of vitellogenin in high affinity binding to vitellogenin receptors in locust oocyte membranes

Roehrkasten, Axel; Ferenz, Hans‐Jörg

doi:10.1016/0167-4889(92)90064-i

Cited by 16 publications

(5 citation statements)

References 25 publications

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“…The VgR belongs to a superfamily of lipoprotein receptors that include the very low density lipoprotein receptor and low density lipoprotein receptor (LDLR). Functional models of these types of lipoprotein receptors involve binding of lysine and arginine residues in the ligand to clusters of acidic residues in the seven or eight ligand-binding repeat domains of the receptor [59]. A recent study using the yeast two-hybrid system to study interactions of tilapia Vg with its receptor demonstrated that an 85-amino acid fragment (referred to as VtgSE) located in the LvH domain of Vg mediates receptor binding [48].…”

Section: Discussionmentioning

confidence: 99%

Multiple Vitellogenins (Vgs) in Mosquitofish (Gambusia affinis): Identification and Characterization of Three Functional Vg Genes and Their Circulating and Yolk Protein Products1

Sawaguchi

Koya

Yoshizaki

et al. 2005

Biology of Reproduction

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The objectives of this study were to characterize multiple forms of vitellogenin (Vg) in mosquitofish (Gambusia affinis) and to discover the fate of each Vg during its processing into product yolk proteins. Two Vg preparations, with apparent masses of 600 kDa (600 Vg) and 400 kDa (400 Vg), were isolated from the plasma of fish treated with estradiol-17beta (E(2)) by various chromatographic procedures. Immunological analyses verified the presence of two different Vg proteins (600 VgA and 600 VgB) in the 600 Vg preparation and of a single protein in the 400 Vg preparation. Three major yolk proteins (Yps) with apparent masses of 560, 400, and 28 kDa were observed in extracts of ovarian follicles from vitellogenic females. Immunological analyses demonstrated that the 400 Vg underwent no change in native mass after being incorporated into oocytes. The 600 Vgs gave rise to a 28 kDa beta'-component and a native 560 kDa Yp, which was heterodimeric in structure, consisting of two types of complexes between phosvitin (Pv) and lipovitellin (Lv) heavy- and light-chains. Full-length cDNAs encoding the 600 VgA, 600 VgB, and 400 Vg were isolated from a liver cDNA library of E(2) treated fish. Similar to the zebrafish vg3 gene, the 400 Vg cDNA lacked a Pv domain and was classified as an incomplete or phosvitinless (C-type) Vg. The deduced primary structures of 600 VgA and 600 VgB were complete, and these were categorized as type A and type B Vgs, respectively, according to our recent classification scheme. This is the first report on the characterization of three functional Vg genes and their circulating and yolk protein products in any vertebrate species.

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Section: Discussionmentioning

confidence: 99%

Multiple Vitellogenins (Vgs) in Mosquitofish (Gambusia affinis): Identification and Characterization of Three Functional Vg Genes and Their Circulating and Yolk Protein Products1

Sawaguchi

Koya

Yoshizaki

et al. 2005

Biology of Reproduction

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“…Roughly a quarter of the amino acids in the multiple sequence alignment are charged, in line with previous studies that described the Vg–VgR interaction as electrostatic 11. 31, 32…”

Section: Discussionmentioning

confidence: 99%

Identification of Receptor‐Interacting Regions of Vitellogenin within Evolutionarily Conserved β‐Sheet Structures by Using a Peptide Array

et al. 2013

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Vitellogenesis, a key process in oviparous animals, is characterized by enhanced synthesis of the lipoprotein vitellogenin, which serves as the major yolk-protein precursor. In most oviparous animals, and specifically in crustaceans, vitellogenin is mainly synthesized in the hepatopancreas, secreted to the hemolymph, and taken up into the ovary by receptor-mediated endocytosis. In the present study, localization of the vitellogenin receptor and its interaction with vitellogenin were investigated in the freshwater prawn Macrobrachium rosenbergii. The receptor was immuno-histochemically localized to the cell periphery and around yolk vesicles. A receptor blot assay revealed that the vitellogenin receptor interacts with most known vitellogenin subunits, the most prominent being the 79 kDa subunit. The receptor was, moreover, able to interact with trypsin-digested vitellogenin peptides. By combining a novel peptide-array approach with tandem mass spectrometry, eleven vitellogenin-derived peptides that interacted with the receptor were identified. A 3D model of vitellogenin indicated that four of the identified peptides are N-terminally localized. One of the peptides is homologous to the receptor-recognized site of vertebrate vitellogenin, and assumes a conserved β-sheet structure. These findings suggest that this specific β-sheet region in the vitellogenin N-terminal lipoprotein domain is the receptor-interacting site, with the rest of the protein serving to enhance affinity for the receptor. The conservation of the receptor recognition site in invertebrate and vertebrate vitellogenin might have vast implications for oviparous species reproduction, development, immunity, and pest management.

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“…Gerber-Huber et al (1987) suggested that these sequences allowed for hydrophobic interactions between vitellogenin monomers, while leaving charged residues and the phosvitin domain exposed as hydrophilic loops to maintain the solubility of the protein in the serum. Chemical modification of lysine and arginine residues of locust, Locusta migratoria, viteUogenin reduces binding to the oocyte receptor (Roehrkasten and Ferenz 1992). As described in Results, the third subdomain of lipovitellin I contained a conserved sequence found in all four species and had the greatest number of positively charged residues.…”

Section: Discussionmentioning

confidence: 99%

Characterization of vitellogenin from white sturgeon, Acipenser transmontanus

Bidwell

Carlson

1995

J Mol Evol

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Sturgeon are an ancient family (Acipenseridae) of fishes that lie close to the divergence of fish that eventually evolved into terrestrial animals and those that evolved into modern teleost species. Therefore, white sturgeon vitellogenin sequences fill a gap in the current understanding of the functional domains of this protein family. Vitellogenin cDNA was sequenced and used to investigate gene expression in white sturgeon, Acipenser transmontanus. Estrogen-induced vitellogenin mRNA was detected in the livers of both males and females and was also detected in undifferentiated gonads of estrogen-treated fish. Low levels of vitellogenin mRNA were also detected in the testis of both control and estrogen-treated males. The cDNA encoded a 186-kDa protein that was missing only six to seven of the amino-terminal amino acids. Comparisons to silver lamprey, Xenopus, and chicken vitellogenin sequences indicate that the overall structure of the yolk protein domains were highly conserved. There was considerable homology in three regions of the lipovitellin I domain. These conserved sequences are likely to be involved in vitellogenin receptor binding. The phosvitin domain of white sturgeon vitellogenin contained fewer and shorter serine repeats as predicted from yolk protein phosphate content of fish compared to Xenopus and chicken. However, the vitellogenin of white sturgeon had a lower serine content as compared with silver lamprey, indicating that an increased serine content is not strictly a function of evolutionary age.

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Role of the lysine and arginine residues of vitellogenin in high affinity binding to vitellogenin receptors in locust oocyte membranes

Cited by 16 publications

References 25 publications

Multiple Vitellogenins (Vgs) in Mosquitofish (Gambusia affinis): Identification and Characterization of Three Functional Vg Genes and Their Circulating and Yolk Protein Products1

Multiple Vitellogenins (Vgs) in Mosquitofish (Gambusia affinis): Identification and Characterization of Three Functional Vg Genes and Their Circulating and Yolk Protein Products1

Identification of Receptor‐Interacting Regions of Vitellogenin within Evolutionarily Conserved β‐Sheet Structures by Using a Peptide Array

Characterization of vitellogenin from white sturgeon, Acipenser transmontanus

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