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Of Very Low Density Lipoprotein and Vitellogenin (Multifunctional Receptors/Cell Growth/Endocytosis) STEFANO STIFANI, DWAYNE L

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Of Very Low Density Lipoprotein and Vitellogenin (Multifunctional Receptors/Cell Growth/Endocytosis) STEFANO STIFANI, DWAYNE L Proc. Natl. Acad. Sci. USA Vol. 87, pp. 1955-1959, March 1990 Cell Biology A single chicken oocyte plasma membrane protein mediates uptake of very low density lipoprotein and vitellogenin (multifunctional receptors/cell growth/endocytosis) STEFANO STIFANI, DWAYNE L. BARBER, JOHANNES NIMPF, AND WOLFGANG J. SCHNEIDER* Department of Biochemistry and Lipid and Lipoprotein Research Group, University of Alberta, Edmonton, AB T6G 2S2, Canada Communicated by Daniel Steinberg, December 18, 1989 ABSTRACT Specific cell-surface receptors mediate the tions), we observed that high concentrations of unlabeled uptake of plasma proteins into growing oocytes of oviparous VTG and VLDL competed with the binding of both '251- species, thereby forming yolk. Quantitatively the most impor- labeled VTG and VLDL to chicken oocyte membrane ex- tant yolk precursors are the lipoproteins, very low density tracts, further suggesting the presence of one bifunctional lipoprotein, and vitellogenin. We show that a single major receptor. In the light ofthe pivotal role of receptor-mediated chicken oocyte plasma membrane protein with an apparent endocytosis of yolk proteins in the reproductive effort of the molecular mass of95 kDa as determined by SDS/PAGE under hen, coupled to the inability of the oocyte to synthesize yolk nonreducing conditions is the receptor for both ofthese ligands. proteins (3), it seemed reasonable to us that one and the same Binding activities for the two ligands copurified on ligand chicken oocyte plasma membrane receptor would be respon- affinity matrices and were inhibited by the same antibody sible for the import ofthe major yolk lipoproteins, VLDL and preparations, and the ligands competed with each other for VTG. However, it is entirely possible that the receptors are binding to the 95-kDa protein. In addition to these biochemical different molecules, since direct evidence for their identity and immunological lines of evidence for the identity of the has not been provided. vitellogenin receptor with the very low density lipoprotein In the studies reported here, we took advantage of our receptor, genetic proof was obtained. We have previously biochemical and immunological tools for the identification shown that the mutant nonlaying "restricted-ovulator" hen and characterization of chicken oocyte receptors, as well as carries a defect in the gene responsible for functional expression of a powerful genetic model for addressing this question, of the oocyte 95-kDa protein. Here we demonstrate that this namely the mutant "restricted-ovulator" (R/O) strain of single gene defect in the restricted-ovulator hen has detrimental chickens (4, 5). As we have reported (4), R/O hens fail to consequences for the binding not only of very low density express functional oocyte receptors for VLDL. Since the lipoprotein but also of vitellogenin to the 95-kDa receptor R/O phenotype has been clearly shown to be due to a normally present in oocytes. The intriguing bifunctionality of single-gene defect (6, 7), we reasoned that demonstration of this chicken oocyte membrane protein possibly relates to its absence or gross reduction of binding activity for VTG in crucial role in receptor-mediated control of oocyte growth. ovarian membranes ofthe R/O hen should provide additional convincing evidence for the presence of a single receptor for VLDL and VTG on chicken oocytes. Specific cell-surface receptors mediate the endocytosis ofthe major yolk components, very low density lipoprotein (VLDL) (1) and vitellogenin (VTG) (2) by growing oocytes of MATERIALS AND METHODS the laying hen. By ligand blotting, we have identified (1) the Materials, Animals, and Diets. We obtained CNBr- chicken oocyte VLDL receptor as a protein with an apparent activated Sepharose 4B (catalogue no. 17-04300-01) and molecular mass of 95 kDa, as determined by SDS/PAGE in Sephadex G-200, superfine, from Pharmacia. All other ma- the absence of sulfhydryl-reducing agents (1). With the same terials were from reported sources (1, 2). White Leghorn hens biochemical tool as used for the identification of the VLDL and roosters were purchased from the Department ofAnimal receptor, namely ligand blotting, a protein to which we Science, The University of Alberta, and maintained as de- assigned an apparent molecular mass of 96 kDa under iden- scribed (1, 2). Oocytes were also collected during slaughter tical experimental conditions has been shown to be the by permission of Lilydale Poultry Sales (Edmonton, AB). receptor for VTG on the chicken oocyte plasma membrane R/O hens were selected from hatchlings kindly provided by (2). Interestingly, a polyclonal rabbit IgG fraction raised J. James Bitgood (Poultry Science Department, University of against the pure bovine low density lipoprotein (LDL) re- Wisconsin, Madison) and maintained as described (4). ceptor recognized the VLDL receptor (1) and immunopre- Preparation of Antibodies. Polyclonal rabbit antibodies cipitated VTG-binding activity from chicken oocyte mem- against the bovine LDL receptor (1) and the chicken oocyte brane extracts (2). Furthermore, receptor-binding of VTG VTG receptor (2) were raised. Polyclonal antibodies against and VLDL was abolished by reductive methylation of lysine the VLDL-Sepharose affinity-purified receptor were ob- residues in both ligands, and exposure of oocyte membrane tained by immunization of adult female New Zealand rabbits extracts to sulfhydryl-reducing agents abolished the ability to as described (4). bind the two ligands (1, 2). Lipoprotein Isolation and Radioiodination. Lipoprotein These findings of essentially identical apparent molecular fractions (1) and VTG (2) were isolated and radiolabeled with masses, immunological properties, and biochemical proper- 1251. Lipoprotein concentrations are expressed in terms of ties suggested to us a close relationship, if not identity of the protein content determined by a modification (8) of the chicken oocyte receptors for VLDL and VTG. In preliminary method of Lowry et al. (9) using bovine serum albumin as competitive filtration binding assays (unpublished observa- standard. The publication costs of this article were defrayed in part by page charge Abbreviations: Apo, apolipoprotein; (V)LDL, (very) low density payment. This article must therefore be hereby marked "advertisement" lipoprotein; VTG, vitellogenin; R/O, restricted ovulator. in accordance with 18 U.S.C. §1734 solely to indicate this fact. *To whom reprint requests should be addressed. 1955 Downloaded by guest on September 26, 2021 1956 Cell Biology: Stifani et al. Proc. Natl. Acad. Sci. USA 87 (1990) Preparation and Solubilization of Membrane Fractions and 1251 -VTG 1251 -VLDL Filtration Assay. Oocyte membranes (1) and ovarian mem- A B C n p p branes from laying hens and R/O hens (4) were prepared and extracted with either octylglucoside or Triton X-100. Lipo- protein binding to membrane detergent extracts was deter- kDa mined by a solid-phase filtration procedure with 125I-labeled 200- VLDL (1) or VTG (2). Electrophoresis and Blotting Procedures. One-dimensional 97 - SDS/polyacrylamide gel electrophoresis was performed ac- cording to Laemmli (10) on 4.5-18% gradient or 8% slab gels. 43- If not indicated otherwise, samples were prepared in the .. v absence of dithiothreitol and without heating (nonreducing 29- -' conditions). Gels were electrophoresed, calibrated, and stained (1), and electrophoretic transfer of proteins to nitro- cellulose (11) was performed. Ligand blotting was carried out with 125I-labeled VTG or VLDL as reported (1, 2, and 12). e e -i r- I Affinity Chromatography: VTG-Sepharose 4B. VTG was n co 1= Ina coupled to CNBr-activated Sepharose 4B according to the manufacturer's instructions (13), by using 30 mg of VTG per FIG. 1. Ligand blotting of oocyte membrane proteins. Oocyte g of dry gel. The VTG-Sepharose 4B was stored at 40C in a membrane Triton extract (20 ,g ofprotein per lane) was subjected to buffer containing 25 mM Tris'HCl (pH 7.8), 50 mM NaCl, 2 electrophoresis on a 4.5-18% SDS/polyacrylamide gradient slab gel mM CaCl2, and 0.02% NaN3. Affinity chromatography was and then transferred to nitrocellulose and analyzed by ligand blotting. performed at 40C using columns of 1-cm diameter containing Lanes A-C were incubated with 125I-labeled VTG (1251-VTG; 2.8 approximately 10 mg of immobilized VTG. Columns were ,ug/ml; 250 cpm/ng) with the following additions. Lanes: A, none; B, unlabeled VTG at 140 /Ag/ml; C, unlabeled VLDL at 140 jug/ml. equilibrated with buffer containing 50 mM Tris HCl (pH 7.8), Lanes D-F were incubated in the presence of 1251-labeled VLDL 4mM CaCl2, and 0.2% Triton X-100 (buffer A) prior to sample (_251-VLDL; 1.7 ,ug/ml; 95 cpm/ng) with the following additions. application. Samples, consisting of 200 ,ul of chicken oocyte Lanes: D, none; E, unlabeled VLDL at 85 Zg/ml; F, unlabeled VTG membrane Triton X-100 extracts (800 ,g of protein), were at 85 Ag/ml. The positions of migration of the molecular mass mixed with 2 vol of buffer A and applied to and recycled over standards are indicated. The autoradiograph was exposed for 14 hr. the affinity columns for a total of 2 hr. Columns were then washed with 50 bed-volumes of a buffer containing 50 mM above the 200-kDa standard, also observed with both ligands. Tris-HCl (pH 7.8), 4 mM CaCl2, and 0.1% Triton X-100 The intensity of this band varied widely in different prepa- (buffer B) and material was eluted with 2 bed-volumes of a rations of oocyte membrane extracts and is likely related to solution of 0.5 M NH40H. The eluted fractions were imme- di- or oligomeric forms of the receptor such as described for diately dialyzed against a buffer containing 25 mM Tris HCl the mammalian LDL receptor (15). (pH 7.8), 50 mM NaCl, and 2 mM CaCl2 and subsequently To further investigate the properties of the 95-kDa pro- concentrated to approximately one-fifth of the initial volume tein(s), oocyte membrane detergent extracts were subjected by using Amicon Centricon-30 microconcentrators.
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