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Identification and characterization of the vitellogenin receptor in Macrobrachium rosenbergii and its expression during vitellogenesis
Author(s) -
Roth Ziv,
Khalaila Isam
Publication year - 2012
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.22055
Subject(s) - vitellogenin , vitellogenesis , biology , vitellogenins , macrobrachium rosenbergii , oocyte , yolk , oviparity , microbiology and biotechnology , transmembrane domain , receptor , biochemistry , gene , zoology , prawn , embryo , fishery
In oviparous organisms, oocyte maturation depends on massive production of the egg yolk‐precursor protein, vitellogenin (Vg). Vg is taken up by the developing oocytes through receptor‐mediated endocytosis (RME), a process essential to successful reproduction. The aims of this study were to identify and characterize the yet‐unknown vitellogenin receptor (VgR) from the pleocyamate crustacean Macrobrachium rosenbergii , and to investigate its expression levels during vitellogenesis and its interaction with Vg. The VgR gene was cloned, and its translated protein was specifically located at the oocyte membrane. Moreover, for the first time, a VgR protein was identified and sequenced by mass spectrometry. The putative MrVgR displayed high sequence similarity to VgRs from crustaceans, insects, and vertebrates, and its structure includes typical elements, such as an extracellular, lipoprotein‐binding domain (LBD), EGF‐like, and O ‐glycosylation domains, a transmembrane domain, and a short, C‐terminal, cytosolic tail. In this article, we identify the first crustacean VgR protein, and present data demonstrating its high affinity for a Vg column followed by elution with suramin and EDTA. Additionally we demonstrate that VgR expression in the oocyte is elevated during vitellogenesis. Our results contribute to the fundamental understanding of oocyte maturation in crustaceans, and particularly elucidate Vg uptake through RME via the VgR. Mol. Reprod. Dev. 79:478–487, 2012. © Wiley Periodicals, Inc.