Solubilization of the locust vitellogenin receptor

Röhrkasten, Axel; Ferenz, Hans‐Jörg

doi:10.1016/0005-2736(86)90556-0

Cited by 31 publications

(17 citation statements)

References 13 publications

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“…This finding supports the concept that VTG is taken up into teleost oocytes via receptor-mediated endocytosis, as it is in insects, amphibians, and birds [5][6][7][8][9][10]. Detailed studies of the latter species and more limited information on fishes indicate that the VTG receptor has an affinity (Kd) from the nanomolar to low micromolar range.…”

Section: Discussionsupporting

confidence: 79%

“…Vertical brackets indicate the range of values for the incubations. The specific activity of '21-wVTG was calculated by dividing the amount of '2 5 1-wVTG necessary to achieve 5 0% of maximum binding by the quantity of unlabeled VTG needed to obtain a 50% reduction in inhibitable ' 25 1-wVTG tracer binding. Bo, the quantity of ' 2 lI-wVTG tracer bound in the absence of unlabeled VTG.…”

Section: Binding Of 3 H-wvtg To Ovarian Membranesmentioning

confidence: 99%

“…In birds, amphibians, and insects, VTG is sequestered by the oocytes through the process of receptor-mediated endocytosis [5][6][7][8][9][10]. Recent evidence suggests that this is also true of teleosts.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of a Vitellogenin Receptor in White Perch (Morone Americana)1

Tao

Berlinsky

Sullivan

1996

Biology of Reproduction

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Receptors for white perch vitellogenin (wVTG) were characterized using wVTG, labeled in vivo with [3H]leucine or in vitro with 125I, and semipurified ovarian membranes. Specific binding of wVTG to the membranes was temperature-dependent, proportional to the amount of membrane, and saturable. Scatchard analyses revealed a single class of binding sites of low maximum binding capacity (MBC; approximately 35 pmol VTG/mg membrane protein) and high affinity (Kd approximately 400 nM), consistent with wVTG levels (540-2700 nM) circulating in maturing females. Ligand blotting revealed a receptor protein of M(r) approximately 157000 and a smaller protein, possibly its degradation product. Striped bass vitellogenin, chicken egg yolk very low density lipoprotein, and suramin displaced wVTG from its receptor, but BSA did not. No change in Kd was noted over the course of vitellogenesis in maturing perch, and MBC increased only slightly very late in the gametogenic cycle. The wVTG bound specifically to membranes prepared from liver, muscle, and mesenteric fat, but not to erythrocyte membranes. The Kd for ovary (394 nM) and liver (345 nM) were similar, but the Kd for muscle (1440 nM) was much higher.

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Section: Discussionsupporting

confidence: 79%

Section: Binding Of 3 H-wvtg To Ovarian Membranesmentioning

confidence: 99%

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Characterization of a Vitellogenin Receptor in White Perch (Morone Americana)1

Tao

Berlinsky

Sullivan

1996

Biology of Reproduction

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“…Figure 2 illustrates the purity of the obtained receptor protein. This material was analyzed for its ability to bind ' *?-VTG in a filtration assay [17]. Scatchard analysis of the binding data gave a linear plot, indicating a single binding site on the receptor protein for VTG (Fig.…”

Section: Purification Of the Locusta Vtg Receptor By Immunoaffinity Cmentioning

confidence: 99%

Yolk formation in Locusta migratoria and Schistocerca gregaria: Related ligands and oocyte receptors

Hafer

Ferenz

1994

Arch Insect Biochem Physiol

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During vitellogenesis the transport of yolk precursor proteins, the vitellogenins (VTG), from the hemolymph into the oocyte is achieved by receptor-mediated endocytosis. Recently the receptor for the VTG of Locusfa migratoria has been isolated. Now a new protocol has been developed for the purification of the VTC receptor of this locust from ovarian membranes. By CHAPS solubilization of the membranes followed by ion exchange and immunoaffinity chromatography, a 1 00-fold purification of the VTG receptor was achieved. The amino acid composition of the receptor protein has been determined. However, first attempts to sequence the receptor failed due to the N-terminal blocking of the molecule. With the same methods the VTG receptor of another locust, Schistocerca gregaria, has been isolated, purified, and characterized. This receptor has an apparent M, of 186 kDa under nonreducing conditions. It recognizes L. migratoria VTG and vice versa. However, in cross-competition experiments in which the Schistocerca VTG competed with Locusfa VTC for binding to the Locusfa VTG receptor, the Schistocerca VTG was less efficient.Furthermore, the VTG receptor proteins of S. gregaria and L. migraforia are immunologically related as revealed by Western blotting with anti-Locusta VTG receptor antibodies. It appears that important structural elements required for efficient and specific endocytosis of VTG have been conserved.

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“…During yolk formation, insect oocytes endocytose vitellogenin from the intercellular spaces of the ovary by a mechanism that has been shown to be saturable [l-41 and to entail membrane binding [5][6][7]. Early experiments with moth ovaries indicated that smaller amounts of several other blood proteins accompany vitellogenin into the yolk [8,9].…”

Section: Introductionmentioning

confidence: 99%

Adsorptive endocytosis of vitellogenin, lipophorin, and microvitellogenin during yolk formation in Hyalophora

Telfer

Pan

1988

Arch Insect Biochem Physiol

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Yolk in Hyalophora cecropia is a mixture of proteins that are derived from the extracellular medium. We have measured for five of these proteins the number of moles deposited in each egg, the molarity of their precursors in the hemolymph at a midpoint in vitellogenesis (day 18 of adult development), and the degree to which they are concentrated by the oocyte, relative to inulin. The proteins were isolated by gel permeation and ion exchange chromatography and used to generate antibodies in rabbits. Preliminary studies established that yolk proteins are essentially quantitatively extractable in media suitable for measuring antigen concentrations by precipitation with antibodies and that yolk and hemolymph forms of the five proteins have, effectively, the same antibody-binding specificities as the isolated standards. Content per egg was about 900 pmol for vitellogenin, 600 pmol for microvitellogenin, and 300 pmol for lipophorin. By contrast, two hemolymph storage hexamers, arylphorin and a flavoprotein, occurred at less than 3 pmol per egg. In principle, yolk precursors are taken in both as solutes in the fluid phase of the endocytotic vesicles and as ligands adsorbed to vesicle membranes. Measurements of inulin uptake indicated that fluid phase endocytosis could account for only 4% of vitellogenin, 1% of microvitellogenin, and 15% of lipophorin in the yolk, when hemolymph precursors are at their day 18 concentrations. By the same comparison, arylphorin and flavoprotein appear to be excluded from the yolk, relative to inulin.

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Solubilization of the locust vitellogenin receptor

Cited by 31 publications

References 13 publications

Characterization of a Vitellogenin Receptor in White Perch (Morone Americana)1

Characterization of a Vitellogenin Receptor in White Perch (Morone Americana)1

Yolk formation in Locusta migratoria and Schistocerca gregaria: Related ligands and oocyte receptors

Adsorptive endocytosis of vitellogenin, lipophorin, and microvitellogenin during yolk formation in Hyalophora

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