Journal
MOLECULAR REPRODUCTION AND DEVELOPMENT
Volume 61, Issue 4, Pages 536-548Publisher
WILEY
DOI: 10.1002/mrd.10106
Keywords
vitellogenin; vitellogenin receptor; low density lipoprotein; very low density lipoprotein; receptor-mediated endocytosis; ultrastructural immunolocalization
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The receptor-mediated uptake of major yolk protein precursor, vitellogenin (Vg) is crucial for oocyte growth in egg laying animals. In the present study plasma membrane receptor for Vg was isolated from the oocyte of the red mud crab, Scylla serrata. Vitellogenin receptor (VgR) protein was visualized by ligand blotting using labeled crab V (I-125-Vg) as well as labeled low density lipoprotein (I-125-LDL) and very low density lipoprotein (I-125-VLDL) isolated from rat. The endocytosis of Vg was visualized in the crab oocyte by ultrastructural immunolocalization of Vg. The Vg receptor was purified by gel filtration high performance liquid chromatography (HPLC) and its molecular weight was estimated to be 230 kDa. In direct binding studies, the receptor exhibited high affinity (dissociation constant K-d 0.8 X 10(-6) M) for crab Vg. Vitellogenin receptor was observed to have an increased affinity to crab Vg in the presence of Ca2+ and the binding was inhibited by suramin, suggesting similarities between crab VgR and low density lipoprotein receptor (LDLR) superfamily of receptor protein. Furthermore, the crab VgR showed significant binding ability to mammalian atherogenic lipoproteins such as LDL and VLDL. This suggests that there is a tight conservation of receptor binding sites between invertebrate (crab) Vg and vertebrate (rat) LDL and VLDL. (C) 2002 Wiley-Liss, Inc.
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