The binding of very low density and low density lipoproteins to the plasma membrane of the hen's oocyte. A morphological study.

The binding of lipoproteins to the oocyte plasma membrane of the domestic fowl (Gallus domesticus) was examined by electron microscopy in preparations of the ovarian follicle in the main phase of yolk formation. Numerous particles, 26 nm in diameter, were present on the untreated membrane. They were dissociated from the membrane by incubation at 4 degrees C in buffer at pH 6.2 and with heparin at pH 7.4. Added calcium was not required for binding, though the number of bound particles was reduced by treatment with EDTA. Very low density (VLD) lipoproteins from laying hen's plasma were found to bind to the denuded membrane and to correspond in size to the native particles. The results suggest that the binding characteristics are similar in quality to those determined for the binding of low density (LD) lipoproteins to mammalian cells. The oocytes, however, bound 100-fold more particles per unit length of membrane. VLD and LD lipoproteins from immature hens also adhered to the denuded membrane, although their apoprotein composition was very different from that of laying hen VLD lipoproteins. LD lipoproteins from immature hens and VLD lipoproteins from laying hens both contained apo-B, which formed about 80 and 35%, respectively, of the total apolipoproteins. Apo-VLDL-II is the other major apoprotein identified in laying-hen VLD lipoproteins. Apo-VLDL-II was not positively identified as a component of immature-hen LD lipoproteins and could only have been present as a minor component.(ABSTRACT TRUNCATED AT 250 WORDS)