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      Differential expression of proteins and phosphoproteins during larval metamorphosis of the polychaete Capitella sp. I

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          Abstract

          Background

          The spontaneous metamorphosis of the polychaete Capitella sp. I larvae into juveniles requires minor morphological changes, including segment formation, body elongation, and loss of cilia. In this study, we investigated changes in the expression patterns of both proteins and phosphoproteins during the transition from larvae to juveniles in this species. We used two-dimensional gel electrophoresis (2-DE) followed by multiplex fluorescent staining and MALDI-TOF mass spectrometry analysis to identify the differentially expressed proteins as well as the protein and phosphoprotein profiles of both competent larvae and juveniles.

          Results

          Twenty-three differentially expressed proteins were identified in the two developmental stages. Expression patterns of two of those proteins were examined at the protein level by Western blot analysis while seven were further studied at the mRNA level by real-time PCR. Results showed that proteins related to cell division, cell migration, energy storage and oxidative stress were plentifully expressed in the competent larvae; in contrast, proteins involved in oxidative metabolism and transcriptional regulation were abundantly expressed in the juveniles.

          Conclusion

          It is likely that these differentially expressed proteins are involved in regulating the larval metamorphosis process and can be used as protein markers for studying molecular mechanisms associated with larval metamorphosis in polychaetes.

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          Most cited references45

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          Programmed cell death in animal development.

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            ATP synthase--a marvellous rotary engine of the cell.

            ATP synthase can be thought of as a complex of two motors--the ATP-driven F1 motor and the proton-driven Fo motor--that rotate in opposite directions. The mechanisms by which rotation and catalysis are coupled in the working enzyme are now being unravelled on a molecular scale.
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              Heat-shock protein 90, a chaperone for folding and regulation.

              D Picard (2002)
              Heat-shock protein 90 (Hsp90) is an abundant and highly conserved molecular chaperone that is essential for viability in eukaryotes. Hsp90 fulfills a housekeeping function in contributing to the folding, maintenance of structural integrity and proper regulation of a subset of cytosolic proteins. A remarkable proportion of its substrates are proteins involved in cell cycle control and signal transduction. Hsp90 acts with a cohort of Hsp90 co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. The large conformational flexibility of Hsp90 and a multitude of dynamic co-chaperone complexes contribute to generating functional diversity, and allow Hsp90 to assist a wide range of substrates.
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                Author and article information

                Journal
                Proteome Sci
                Proteome Science
                BioMed Central
                1477-5956
                2011
                3 September 2011
                : 9
                : 51
                Affiliations
                [1 ]KAUST Global Collaborative Research, Division of Life Science, Hong Kong University of Science and Technology, Hong Kong SAR, China
                Article
                1477-5956-9-51
                10.1186/1477-5956-9-51
                3180302
                21888661
                30bc8812-9d35-4bd7-b70b-4e3bc0b56ad4
                Copyright ©2011 Chandramouli et al; licensee BioMed Central Ltd.

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 19 April 2011
                : 3 September 2011
                Categories
                Research

                Molecular biology
                rt-pcr,2-de,phosphoproteome,larval metamorphosis,capitella sp. i,multiplexed proteomics

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