info:eu-repo/semantics/article
Vitellogenesis in spiders: First analysis of protein changes in different reproductive stages of Polybetes pythagoricus
Fecha
2019-04-05Registro en:
Romero, Sofía Micaela; Laino, Aldana; Arrighetti, Florencia; García, C.F.; Cunningham, Monica Liliana; Vitellogenesis in spiders: First analysis of protein changes in different reproductive stages of Polybetes pythagoricus; Springer Verlag Berlín; Journal of Comparative Physiology B: Biochemical, Systems and Environmental Physiology; 189; 3-4; 05-4-2019; 335-350
0174-1578
CONICET Digital
CONICET
Autor
Romero, Sofía Micaela
Laino, Aldana
Arrighetti, Florencia
García, C.F.
Cunningham, Monica Liliana
Resumen
Vitellogenesis represents one of the most vital processes of oviparous species during which various proteins, carbohydrates, and lipids are synthesized and stored inside the developing oocytes. Through analyzing protein changes in the midgut diverticula, hemolymph, and ovaries of females throughout the different vitellogenic stages of the spider Polybetes pythagoricus, we determined the origin of the different proteins involved in the formation of lipovitellins (LVs) along with the existence of a linkage between the hemocyanin and this vital process. An increase in the total protein content of the midgut diverticula, hemolymph, and ovary occurred throughout vitellogenesis followed by a decrease in those levels after laying. The presence of hemocyanin in egg and in LV2, as well as its accumulation in the ovary throughout the vitellogenesis process, was determined. Considering that all biologic processes depend on the correct structure and function of proteins, this study establishes, for the first time for the Order Araneae, the coexistence of three different origins of vitellogenesis-related proteins: one predominantly ovarian involving peptides of 120, 75, 46, and 30 kDa; another extraovarian one originated from the midgut diverticula and represented by a 170 kDa peptide, and a third hemolymphatic one, represented by the 67 kDa peptide.