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Vitellogenesis in spiders: first analysis of protein changes in different reproductive stages of Polybetes pythagoricus
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...
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Published in: | Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology Biochemical, systemic, and environmental physiology, 2019-08, Vol.189 (3-4), p.335-350 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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. |
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ISSN: | 0174-1578 1432-136X |
DOI: | 10.1007/s00360-019-01217-9 |