PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2014 | 17 | 3 |

Tytuł artykułu

Use biochemical markers to evaluate the quality of fresh and cryopreserved semen from the arctic fox (Vulpes lagopus)

Treść / Zawartość

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The aim of this study was to use biochemical markers to evaluate the quality of fresh and cryopreserved semen from the arctic fox (Vulpes lagopus). Twenty-three manually collected ejaculates were analysed for the main indicators of semen quality (sperm concentration and ejaculate volume). Sperm motility and percentage of morphologically normal and abnormal spermatozoa were determined according to the stage of cryopreservation (fresh - measurement A; equilibrated - measurement B; frozen/thawed - measurement C). Furthermore, the seminal plasma and supernatants were analysed after equilibration and freeze/thawing for the activity of the enzymes alkaline phosphatase (ALP), acid phosphatase (AcP), lactate dehydrogenase (LDH) and aspartate aminotransferase (AspAT), and for the activity of acrosin inhibitors (AP). The mean concentration of sperm was 625.1 million/cm3, and ejaculate volume averaged 1.6 cm3. Seminal plasma was characterized by the highest activity of alkaline phosphatase (3.43×103 U/l) and lowest activity of acrosin inhibitors (4.55×103 U/l). After equilibration, the supernatants showed the highest activity of acid phosphatase (94.9 U/l) and after freeze-thawing, they showed a high activity of lactate dehydrogenase (535.8 U/l) and aspartate aminotransferase (577.1 U/l), which indicates that these proteins had leaked from spermatozoa into the extracellular medium during the biotechnique of semen cryopreservation. In addition, several significant relationships were found between some indicators of semen quality and plasma and/or supernatant enzyme activity.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

17

Numer

3

Opis fizyczny

p.427-432,ref.

Twórcy

autor
  • Chair of Biochemistry and Toxicology of the Environment, Faculty of Animal Breeding and Biology, University of Technology and Life Sciences, Mazowiecka 28, 85-084 Bydgoszcz, Poland
autor
  • Department of Molecular Andrology, Institute of Animal Reproduction and Food Research, Polish Academy of Sciences, Bydgoska 7, 10-747 Olsztyn, Poland
  • Department of Molecular Andrology, Institute of Animal Reproduction and Food Research, Polish Academy of Sciences, Bydgoska 7, 10-747 Olsztyn, Poland
autor
  • Department of Molecular Andrology, Institute of Animal Reproduction and Food Research, Polish Academy of Sciences, Bydgoska 7, 10-747 Olsztyn, Poland
  • Chair of Biochemistry and Toxicology of the Environment, Faculty of Animal Breeding and Biology, University of Technology and Life Sciences, Mazowiecka 28, 85-084 Bydgoszcz, Poland
autor
  • Chair of Biochemistry and Toxicology of the Environment, Faculty of Animal Breeding and Biology, University of Technology and Life Sciences, Mazowiecka 28, 85-084 Bydgoszcz, Poland

Bibliografia

  • Blom E (1981) The morphological estimation of the spermatozoa defects of bull. II. The proposal of a new classification of spermatozoa defects. Med Weter 37: 239-242.
  • Borkowski K, Strzeżek J (1994) The use of biochemical indicators to evaluate the quality. Med Weter 50: 200-202.
  • Christiansen IJ, Schmidt M, Mitchell TC (1985): Reproduction in the fox. VI Further investigations on the freezing of semen. Arsberetning, Institut for Sterilitetsforskning, Kongelige Veterinaer og Landbohojskole 28: 78-83.
  • De Leeuw FE, Chen HC, Colenbrander B, Verkleij AJ (1990) Cold-induced ultrastructural changes in bull and boar sperm plasma membranes. Cryobiology 27: 171-183.
  • De Souza F, Barreto CS, Lopes MD (2007) Characteristics of seminal plasma proteins and their correlation with canine semen analysis. Theriogenology 68: 100-106.
  • Fraser L, Wysocki P, Ciereszko A, Płucienniczak G, Kotłowska M, Kordan W, Wojtczak M, Dietrich G, Strzeżek J (2006) Application of biochemical markers for identification of biological properties of animal semen. Reprod Biol 6: 5-20.
  • Geiger R, Fritz H (1983) Trypsin. In: Bergmayer HU (ed) Methods of enzymatic analysis. vol. 5, Verlag Chemie, Weinheim, pp 121-124.
  • Hofmo PO, Andersen Berg K (1989) Electron microscopical studies of membrane injuries in blue fox spermatozoa subjected to the process of freezing and thawing. Cryobiology 26: 124-131.
  • Kutzler MA, Solter PF, Hoffman WE, Volkmann DH (2003) Characterization and localization of alkaline phosphatase in canine seminal plasma and gonadal tissues. Theriogenology 60: 299-306.
  • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurements with the Folin phenol reagent. J Biol Chem 193: 265-275.
  • Miller RR Jr, Cornett CL, Waterhouse KE, Farstad W (2005) Comparative aspects of sperm membrane fatty acid composition in silver (Vulpes vulpes) and blue (Alopex lagopus) foxes, and their relationship to cell cryopreservation. Cryobiology 51: 66-75.
  • Mogielnicka-Brzozowska M, Fraser L, Czarzasta J, Kordan W (2012) Isolation and characterization of zinc-binding proteins of canine seminal plasma. Pol J Vet Sci 15: 493-498.
  • Niżański W, Bielas W (2003) Comparison of the effect of consecutive stages of cryopreservation on spermatozoal properties in dogs and boars and preliminary results of artificial insemination with frozen-thawed semen. Med Weter 59: 898-904.
  • Schäfer-Somi S, Fro¨hlich T, Schwendenwein I (2013) Measurement of alkaline phosphatase in canine seminal plasma - an update. Reprod Domest Anim 48: e10-12.
  • Stasiak K, Janicki B (2007) Activity of the trypsin inhibitor on the semen plasma of the polar fox Alopex lagopus L. during the reproductive season. Med Weter 63: 990-993.
  • Watson PF, Plummer JM (1985) The responses of boar sperm membranes to cold shock and cooling, In: Johnson LA, Larsson K, (eds) Deep freezing of boar semen. Swedish University of Agricultural Sciences, Uppsala, pp 113-127.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-437aa63c-1068-41cb-a33f-d5e520efb579
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.