Proteome profile of zebrafish caudal fin based on one-dimensional gel electrophoresis LCMS/MS and two-dimensional gel electrophoresis MALDI MS/MS analysis.
Zebrafish (Danio rerio) is the widely used vertebrate model animal for understanding the complexity of development and disease process. Zebrafish has been also extensively used in understanding the mechanism of regeneration for its extensive capability of regenerating fins and other tissues. We have analyzed the proteome profile of zebrafish caudal fin in its native state based on one-dimensional gel electrophoresis LCMS/MS and two-dimensional gel electrophoresis MS/MS analyses. A total of 417 proteins were identified as zebrafish fin tissue specific, which includes 397 proteins identified based on one-dimensional gel electrophoresis LCMS/MS analysis and 101 proteins identified based on two-dimensional gel electrophoresis MALDI MS/MS. The proteins mapped to the zebrafish fin tissue were shown to be involved in various biological activities related to development, apoptosis, signaling and metabolic process. Focal adhesion, regulation of actin cytoskeleton, cancer-related pathways, mitogen-activated protein kinase signaling, antigen processing and presentation, and proteasome are some of the important pathways associated with the identified proteome data set of the zebrafish fin.
Centre for Cellular and Molecular Biology (CCMB), Council for Scientific and Industrial Research (CSIR), Hyderabad, India.
Sachin K
SK
Singh
Mula G Meena
MG
Lakshmi
Sandeep
S
Saxena
Cherukuvada V Brahmendra
CV
Swamy
Mohammed M
MM
Idris
D058500:Animal Fins / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D005260:Female; D029941:Fish Proteins / Q000737:chemistry / Q000378:metabolism; D008297:Male; D008969:Molecular Sequence Data; D020543:Proteome / Q000737:chemistry* / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods; D053719:Tandem Mass Spectrometry / Q000379:methods; D015027:Zebrafish / Q000378:metabolism*
D029941:Fish Proteins; D020543:Proteome