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Proteomic Analysis of Zebrafish Caudal Fin Regeneration
News

Proteomic Analysis of Zebrafish Caudal Fin Regeneration

Proteomic Analysis of Zebrafish Caudal Fin Regeneration
News

Proteomic Analysis of Zebrafish Caudal Fin Regeneration

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Abstract
The epimorphic regeneration of zebrafish caudal fin is rapid and complete. The spectrum of proteome changes due to regeneration were analyzed among control (0), 1, 12, 24, 48 and 72 hours post amputation involving quantitative differential proteomics analysis based on two dimensional gel electrophoresis matrix-assisted laser desorption/ionization and differential in-gel electrophoresis Orbitrap analysis. A total of 96 proteins were found differentially regulated between the control non-regenerating and regenerating tissues of different time points for having at least 1.5 fold changes. 90 proteins were identified as differentially regulated for regeneration based on differential in-gel electrophoresis analysis between the control and regenerating tissues. 35 proteins were characterized for its expression in all the five regenerating time points against the control samples. The proteins identified and associated with regeneration were found to be directly allied with various molecular, biological and cellular functions. Based on network pathway analysis the identified proteome dataset for regeneration was majorly associated in maintaining cellular structure and architecture. Also the proteins were found associated for the cytoskeleton remodeling pathway and cellular immune defense mechanism. The major proteins which were found differentially regulated during zebrafish caudal fin regeneration includes keratin and its 10 isoforms, Cofilin 2, annexin a1, skeletal alpha 1 actin and structural proteins. Annexin A1 was found to be exclusively undergoing phosphorylation during regeneration. The obtained differential proteome and the direct association of the various proteins might lead to a new understanding of the regeneration mechanism.

The article is published online in the journal Molecular & Cellular Proteomics and is free to access.

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