Cryopreservation-induced alterations in protein composition of rainbow trout semen

Proteomics. 2015 Aug;15(15):2643-54. doi: 10.1002/pmic.201400525. Epub 2015 Apr 29.

Abstract

The aim of this study was to detect cryopreservation-induced alterations in the protein composition of rainbow trout semen using two independent methods 1DE SDS-PAGE prefractionation combined with LC-MS/MS and 2D difference gel electrophoresis followed by MALDI-TOF/TOF identification. Here, we show the first comprehensive dataset of changes in rainbow trout semen proteome after cryopreservation, with a total of 73 identified proteins released from sperm to extracellular fluid, including mitochondrial, cytoskeletal, nuclear, and cytosolic proteins. Our study provides new information about proteins released from sperm, their relation to sperm structure and function, and changes of metabolism of sperm cells as a result of cryopreservation. The identified proteins represent potential markers of cryoinjures of sperm structures and markers of the disturbances of particular sperm metabolic pathways. Further studies will allow to decipher the precise function of the proteins altered during rainbow trout cryopreservation and are useful for the development of extensive diagnostic tests of sperm cryoinjures and for the successful improvement of sperm cryopreservation of this economically important species.

Keywords: Animal proteomics; DIGE; Fish; Freezing-thawing; Semen; Shotgun proteomics.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chromatography, Liquid
  • Cryopreservation / methods*
  • Electrophoresis, Gel, Two-Dimensional
  • Electrophoresis, Polyacrylamide Gel
  • Fish Proteins / analysis*
  • Fish Proteins / metabolism
  • Male
  • Molecular Sequence Annotation
  • Oncorhynchus mykiss / metabolism*
  • Proteome / analysis*
  • Proteome / metabolism
  • Proteomics / methods
  • Semen / cytology
  • Semen / metabolism*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Sperm Motility
  • Spermatozoa / metabolism*
  • Tandem Mass Spectrometry

Substances

  • Fish Proteins
  • Proteome