Comparative proteomics of the developing fish (zebrafish and gilthead seabream) oocytes |
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Authors: | Tamar Ziv Tamar Gattegno Victoria Chapovetsky Hila Wolf Eilon Barnea Esther Lubzens Arie Admon |
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Institution: | aDepartment of Biology, Technion-Israel Institute of Technology, Haifa 32000, Israel;bDepartment of Marine Biology and Biotechnology, Israel Oceanographic & Limnological Research, Haifa 31080, Israel |
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Abstract: | The maturation process of fish oocytes involves both protein biosynthesis within the oocytes and uptake from the plasma. To follow the changes in the proteins repertoires of fish oocytes during maturation, we performed a large-scale proteomics analysis using one and two-dimensional electrophoresis, multi-dimensional protein identification technology (MudPIT) and tandem mass-spectrometry. A large number of proteins were identified and a map of the vitellogenin derived yolk proteins; lipovitellin and phosvitin, was established (the vitellogenin map), reflecting the posttranslational processing of the different vitellogenins gene-products and their accumulation. Such protein patterns are potentially useful for molecular staging and for quality-control of maturing oocytes. Furthermore, proteomics analyses of single oocytes were used to demonstrate molecular variability between morphologically similar oocytes of same or different fish specimens. Proteins of interest detected in this study include proteins that may serve as maternal factors, such as TCP1, serpin A1 and importin alpha1. The large similarity between the proteins repertoires of fish oocytes and other species, such as mammals and insects, demonstrate the evolutionary conservation of oocyte maturation across diverse species gap. |
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Keywords: | Oocytes Proteomics Fish Vitellogenin Molecular staging |
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