Synthesis and organization of vitellogenin and vitellin molecules from the land crab Potamon potamios.
We have previously reported that vitellogenin (Vg) of some female animals contained four polypeptides with molecular mass of 181, 115, 105 and 85 kDa, whereas Vg of most animals contained three polypeptides with molecular mass of 115, 105 and 85 kDa. In the present investigation, we examined whether the 181 kDa polypeptide is the precursor of 115 and 105 kDa Vg and vitellin (Vn) polypeptides. Labeling studies, using [35S]methionine on normal vitellogenic animals, showed that the radioactivity was distributed first among the 181 and 85 kDa polypeptides. SDS-PAGE analysis of purified hemolymph Vg from eyestalk ablated female animals revealed in most animals two polypeptides with an apparent molecular mass of 181 and 85 kDa. These results from in vivo experiments corroborated the view that the 115 and 105 kDa Vg and Vn polypeptides are derived from heaviest 181 kDa polypeptide. In addition it was demonstrated that hepatopancreas and ovary of Potamon potamios incubated in vitro with [35S]methionine synthesized five polypeptides with apparent molecular mass of 224, 181, 115, 105, and 85 kDa while the hepatopancreas appeared to secrete the 181, 115, 105 and 85 kDa polypeptides. The major 115, 105 and 85 kDa polypeptides were found to be components of egg Vn, while the 224 kDa polypeptide was found to be minor component of Vg and Vn from hepatopancreas and ovary extracts, respectively. We conclude that the Vn polypeptides produced by ovary are similar to those produced by hepatopancreas.
Pateraki
L E
LE
Department of Biology, University of Crete, Heraklion, Greece.
Stratakis
E
E
D000818:Animals; D003386:Brachyura; D004527:Egg Proteins / Q000032:analysis / Q000096:biosynthesis*; D005260:Female; D010063:Ovum / Q000378:metabolism; D011498:Protein Precursors / Q000378:metabolism; D014819:Vitellogenins / Q000032:analysis / Q000096:biosynthesis*
D004527:Egg Proteins; D011498:Protein Precursors; D014819:Vitellogenins