Identification of the yolk receptor protein in oocytes of Nereis virens (Annelida, Polychaeta) and comparison with the locust vitellogenin receptor

Hafer, Johannes; Fischer, A.; Ferenz, Hans‐Jörg

doi:10.1007/bf00398340

Cited by 33 publications

(27 citation statements)

References 20 publications

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“…1a, lanes 1-3). In accordance with previous observations (18,19,23), we were unable to visualize the receptor under reducing conditions (Fig. 1b, lanes 1-3).…”

Section: Resultssupporting

confidence: 93%

“…Solubilized membrane preparations of queen ovaries, worker rectums, and worker HPGs were then made as described in ref. 18. Subsequent immunoblotting did not reveal any signs of 180-kDa vitellogenin in the preparations.…”

Section: Methodsmentioning

confidence: 88%

“…The queen ovary membrane contains a receptor protein of the same size, whereas the worker rectum does not (Fig. 1a, (18). No binding of vitellogenin was observed in the presence of 15 mM EDTA, which is known to block binding to the receptor (19) (Fig.…”

Section: Resultsmentioning

confidence: 99%

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Social exploitation of vitellogenin

Amdam¹,

Norberg²,

Hagen³

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

352

295

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Vitellogenin is a female-specific glucolipoprotein yolk precursor produced by all oviparous animals. Vitellogenin expression is under hormonal control, and the protein is generally synthesized directly before yolk deposition. In the honeybee (Apis mellifera), vitellogenin is not only synthesized by the reproductive queen, but also by the functionally sterile workers. In summer, the worker population consists of a hive bee group performing a multitude of tasks including nursing inside the nest, and a forager group specialized in collecting nectar, pollen, water, and propolis. Vitellogenin is synthesized in large quantities by hive bees. When hive bees develop into foragers, their juvenile hormone titers increase, and this causes cessation of their vitellogenin production. This inverse relationship between vitellogenin synthesis and juvenile hormone is opposite to the norm in insects, and the underlying proximate processes and life-history reasons are still not understood. Here we document an alternative use of vitellogenin by showing that it is a source for the proteinaceous royal jelly that is produced by the hive bees. Hive bees use the jelly to feed larvae, queen, workers, and drones. This finding suggests that the evolution of a brood-rearing worker class and a specialized forager class in an advanced eusocial insect society has been directed by an alternative utilization of yolk protein.

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“…1a, lanes 1-3). In accordance with previous observations (18,19,23), we were unable to visualize the receptor under reducing conditions (Fig. 1b, lanes 1-3).…”

Section: Resultssupporting

confidence: 93%

Section: Methodsmentioning

confidence: 88%

See 1 more Smart Citation

Social exploitation of vitellogenin

Amdam¹,

Norberg²,

Hagen³

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

352

295

View full text Add to dashboard Cite

show abstract

“…The immunohistochemical localization of mucin-D in ovary cells [16] suggests that, along with the locust vitellogenin receptor [11], it can be considered as a members of the family of insect mucin-type glycoproteins which play some role in egg maturation. An interesting parallel can be drawn with vertebrate mucins which are present in the extracellular coat (the zona pellucida) of mouse oocyte and account for its sperm receptor activities [33].…”

Section: Discussionmentioning

confidence: 99%

“…The data available at present mainly concern glycoproteins having N-linked oligomannose chains [3][4][5][6][7][8], and show some similarity between the mechanism of N-glycosylation of proteins in insects and vertebrates. Insect O-glycoproteins are much less characterized, their oligosaccharide structure being described only for a couple of objects [9][10][11] while a growing body of evidence for important roles played by vertebrate O-glycoproteins, particularly of the mucin family, in cellular communication, differentiation and carcinogenesis, has recently been accumulated (for review see [12,13]), However, mucin-type glycoproteins have not been previously found in invertebrates and biochemical and cellular characterization of O-glycosylation and its possible biological functions in insect cells remain to be elucidated.…”

Section: Introductionmentioning

confidence: 99%

Mucin‐type glycoprotein from Drosophila melanogaster embryonic cells: characterization of carbohydrate component

et al. 1996

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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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Identification of the yolk receptor protein in oocytes of Nereis virens (Annelida, Polychaeta) and comparison with the locust vitellogenin receptor

Cited by 33 publications

References 20 publications

Social exploitation of vitellogenin

Social exploitation of vitellogenin

Mucin‐type glycoprotein from Drosophila melanogaster embryonic cells: characterization of carbohydrate component

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

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