Internalized proteins directed into accumulative compartments of mosquito oocytes by the specific ligand, vitellogenin.
We have investigated the internalization pathways for a specific protein, vitellogenin, and a non-specific protein, horseradish peroxidase, in the mosquito oocyte in vivo. The internalized proteins were localized by electron microscopical immunocytochemistry or autoradiography; the relationship of their destination compartments with lysosomes was monitored by visualization of acid phosphatase. Proteins internalized by the oocyte follow either a specific accumulative route or a lysosomal degradative route. Via coated vesicles, both proteins enter the same compartment, the endosome, where they dissociate from membrane-binding sites. The route to their final destination depends on the presence of the specific ligand. In its absence, the degradative route is followed, and the endosome with non-specific protein fuses with lysosomes. In the presence of the specific ligand, the accumulative route is followed, and both specific and non-specific proteins are delivered into an accumulative compartment, the transitional yolk body. During the transformation of the transitional yolk body into the final storage compartment, a mature yolk body, vitellogenin undergoes crystallization, whereas the non-specific protein is concentrated in small vesicular extensions of the compartmental membrane. These vesicles are separated from the yolk bodies and apparently deliver the non-specific protein into the lysosomal system. We concluded that any protein bound to the membrane would be internalized by the oocyte, but only binding of the specific ligand to its receptor serves as a transmembrane signal stimulating the formation of accumulative compartments.
D000135:Acid Phosphatase / Q000378:metabolism; D000330:Aedes / Q000378:metabolism* / Q000648:ultrastructure; D000818:Animals; D005260:Female; D006651:Histocytochemistry; D006735:Horseradish Peroxidase / Q000378:metabolism; D008854:Microscopy, Electron; D009865:Oocytes / Q000378:metabolism / Q000648:ultrastructure; D011506:Proteins / Q000378:metabolism*; D014819:Vitellogenins / Q000502:physiology*
D011506:Proteins; D014819:Vitellogenins; D006735:Horseradish Peroxidase; D000135:Acid Phosphatase