Journal of Nutrition OpenSOurce Diets- www.ResearchDiets.com

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


Journal of Nutrition Vol. 125 No. 5 May 1995, pp. 1258-1266
Copyright © 1995 by American Society for Nutrition
This Article
Right arrow Full Text (PDF)
Right arrow Purchase Article
Right arrow View Shopping Cart
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Elkin, R. G.
Right arrow Articles by Schneider, W. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Elkin, R. G.
Right arrow Articles by Schneider, W. J.

Characterization of the Japanese Quail Oocyte Receptor for Very Low Density Lipoprotein and Vitellogenin1,2,

Robert G. Elkin3, Ian MacLachlan*, Marcela Hermann* and Wolfgang J. Schneider*

Department of Animal Sciences, Purdue University, West Lafayette, IN 47907-1151 * Department of Molecular Genetics, University and Biocenter Vienna, A-1030 Vienna, Austria

The plasma membrane receptor for VLDL and vitellogenin from oocytes of Japanese quail (Coturnix coturnix japonica) was characterized and compared with that of another domestic fowl, the chicken (Gallus domesticus). When visualized by ligand blotting with biotinylated or 125I-labeled lipoproteins, the quail VLDL/vitellogenin receptor had an apparent Mr of 95 kDa under nonreducing conditions, identical to that of the chicken receptor. Upon analysis by ligand blotting, binding of radiolabeled quail plasma VLDL to the quail oocyte receptor seemed to be saturable and exhibited high affinity (apparent Kd of 13.9 mg/L). Cross-reactivity, at the level of ligand recognition, was observed between quail and chicken VLDL/vitellogenin receptors, and immunological relatedness was demonstrated by Western blotting with a rabbit anti-chicken oocyte VLDL receptor antibody. In contrast, a species difference was observed in the apolipoprotein VLDL-II moiety of plasma VLDL. Chicken apolipoprotein VLDL-II, an 82-amino acid protein with a disulfide crosslink at residue 75 (the sole cysteine residue), existed as a homodimer of 9.5 kDa subunits and, to a lesser extent, as a monomer. Quail apolipoprotein VLDL-II existed only in monomeric form without reduction and lacked cysteine. The present results demonstrate that, despite a difference in an apolipoprotein moiety of VLDL, quail and chicken oocyte lipoprotein receptors share key structural and functional elements. This lends further support to the notion that receptor recognition is mediated by the common VLDL component, apolipoprotein B.


KEY WORDS: • quail • vitellogenin • VLDL • oocyte receptor • apolipoprotein VLDL-II

1 Journal paper no. 14027 of the Purdue University Agricultural Experiment Station. Supported in part by grants from the Indiana State Poultry Association, Inc., the Indiana State Egg Board and the Austrian Science Foundation (P-9040).

2 The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 USC section 1734 solely to indicate this fact.

3 To whom correspondence should be addressed. RGE also gratefully acknowledges the support of the Austrian-American Educational Commission and the U.S. Information Agency during his tenure at the University of Vienna as a Fulbright Research Scholar.

Manuscript received 25 April 1994. Revision accepted 17 October 1994.







Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]