Theriogenology
Volume 74, Issue 3 , Pages 413-423, August 2010

Ice-age endurance: the effects of cryopreservation on proteins of sperm of common carp, Cyprinus carpio L

  • P. Li

      Affiliations

    • University of South Bohemia in Ceske Budejovice, Faculty of Fisheries and Protection of Waters, Research Institute of Fish Culture and Hydrobiology, Zatisi 728/II, 389 25 Vodnany, Czech Republic
    • Key Laboratory of Freshwater Biodiversity Conservation and Utilization, Ministry of Agriculture, Yangtze River Fisheries Research Institute, Chinese Academy of Fishery Science, Jingzhou, Hubei, China
    • Corresponding Author InformationCorresponding author: Tel.: (420) 387 774 611; fax: (420) 387 774 634
  • ,
  • M. Hulak

      Affiliations

    • University of South Bohemia in Ceske Budejovice, Faculty of Fisheries and Protection of Waters, Research Institute of Fish Culture and Hydrobiology, Zatisi 728/II, 389 25 Vodnany, Czech Republic
  • ,
  • P. Koubek

      Affiliations

    • Institute of Biotechnology, AS CR, v.v.i., Videnska 1083, 142 20 Prague 4, Czech Republic
  • ,
  • M. Sulc

      Affiliations

    • Institute of Microbiology, AS CR, v.v.i., Videnska 1083, 142 20 Prague 4, Czech Republic
  • ,
  • B. Dzyuba

      Affiliations

    • University of South Bohemia in Ceske Budejovice, Faculty of Fisheries and Protection of Waters, Research Institute of Fish Culture and Hydrobiology, Zatisi 728/II, 389 25 Vodnany, Czech Republic
    • Institute for Problems of Cryobiology and Cryomedicine of the National Academy of Sciences of Ukraine, Pereyaslavskaya str., 23, 61015 Kharkov, Ukraine
  • ,
  • S. Boryshpolets

      Affiliations

    • University of South Bohemia in Ceske Budejovice, Faculty of Fisheries and Protection of Waters, Research Institute of Fish Culture and Hydrobiology, Zatisi 728/II, 389 25 Vodnany, Czech Republic
  • ,
  • M. Rodina

      Affiliations

    • University of South Bohemia in Ceske Budejovice, Faculty of Fisheries and Protection of Waters, Research Institute of Fish Culture and Hydrobiology, Zatisi 728/II, 389 25 Vodnany, Czech Republic
  • ,
  • D. Gela

      Affiliations

    • University of South Bohemia in Ceske Budejovice, Faculty of Fisheries and Protection of Waters, Research Institute of Fish Culture and Hydrobiology, Zatisi 728/II, 389 25 Vodnany, Czech Republic
  • ,
  • P. Manaskova-Postlerova

      Affiliations

    • Institute of Biotechnology, AS CR, v.v.i., Videnska 1083, 142 20 Prague 4, Czech Republic
  • ,
  • J. Peknicova

      Affiliations

    • Institute of Biotechnology, AS CR, v.v.i., Videnska 1083, 142 20 Prague 4, Czech Republic
  • ,
  • O. Linhart

      Affiliations

    • University of South Bohemia in Ceske Budejovice, Faculty of Fisheries and Protection of Waters, Research Institute of Fish Culture and Hydrobiology, Zatisi 728/II, 389 25 Vodnany, Czech Republic

Received 21 January 2010; received in revised form 23 February 2010; accepted 28 February 2010. published online 07 June 2010.

Abstract 

Damage to spermatozoa during cryopreservation is regarded as a major obstacle to the expansion of sperm storage technology. The authors used two-dimensional polyacrylamide gel electrophoresis and matrix-associated laser desorption/ionization time-of-flight mass spectrometry to explore whether the protein profile of common carp (Cyprinus carpio) spermatozoa is affected by cryopreservation. Fourteen protein spots were significantly altered following cryopreservation. Eleven of these were identified: three as specific membrane proteins (N-ethylmaleimide-sensitive fusion protein attachment protein alpha, cofilin 2, and annexin A4) involved in membrane trafficking, organization, and cell movement; six as cytoplasmic enzymes (S-Adenosylhomocysteine hydrolase, Si:dkey-180p18.9 protein, lactate dehydrogenase B, phosphoglycerate kinase 1, transaldolase 1, and esterase D/formylglutathione hydrolase) involved in cell metabolism, oxidoreductase activity, and signal transduction; and two as transferrin variant C and F. Based on these findings, the authors hypothesize that transferrin in cryopreserved sperm may protect spermatozoa against oxidative damage during the freeze-thaw process. Cryopreservation caused changes in spermatozoa protein profiles that may lead to decreased spermatozoa velocity, motility, and fertilization success, and to subsequent ova hatching rate.

Keywords: Sperm quality, Cryodamage, Spermatozoa, Seminal plasma, Fish

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PII: S0093-691X(10)00139-1

doi:10.1016/j.theriogenology.2010.02.024

Theriogenology
Volume 74, Issue 3 , Pages 413-423, August 2010