Issue 1
Journal for Veterinary Medicine, Biotechnology and Biosafety
Volume
2, Issue 1, May 2016, Pages 20–28
ISSN 2411-3174 (print version) ISSN 2411-0388
(online version)
SNPS OF CALPAIN/CALPASTATIN
SYSTEM GENES IN COMMERCIAL POPULATION OF ABERDEEN ANGUS IN KHARKIV REGION,
EASTERN UKRAINE
Fedota
O. M.
V.
N. Karazin Kharkiv National University, Kharkiv, Ukraine, e-mail: afedota@mail.ru
Ruban
S. Yu.
Institute of Animal Breeding and Genetics nd. a. M. V. Zubets of NAAS, Chubynske, Ukraine
Lysenko N. G.*
V.
N. Karazin Kharkiv National University, Kharkiv, Ukraine
Kolisnyk
A. I.
PE
‘Agrofirma Svitanok’, Novoselivka, Ukraine
Goraichuk
I. V.
National
Scientific Center ‘Institute of Experimental and Clinical Veterinary
Medicine’, Kharkiv, Ukraine
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PDF (print version)
Citation for print version: Fedota, O. M., Ruban, S. Yu., Lysenko, N. G.,
Kolisnyk, A. I. and Goraichuk, I. V. (2016) ‘SNPS of Calpain/Calpastatin
system genes in commercial population of Aberdeen Angus in Kharkiv Region,
Eastern Ukraine’, Journal
for Veterinary Medicine, Biotechnology and Biosafety, 2(1),
pp. 20–28.
Download
PDF (online version)
Citation for online version: Fedota, O. M., Ruban, S. Yu., Lysenko, N. G.,
Kolisnyk, A. I. and Goraichuk, I. V. (2016) ‘SNPS of Calpain/Calpastatin
system genes in commercial population of Aberdeen Angus in Kharkiv Region,
Eastern Ukraine’, Journal
for Veterinary Medicine, Biotechnology and Biosafety.
[Online] 2(1), pp. 20–28. Available at: http://jvmbbs.kharkov.ua/archive/2016/volume2/issue1/oJVMBBS_2016021_020-028.pdf
Summary. The
calpain proteolytic system — the micromolar calcium-activated neutral
protease μ-calpain encoded by the CAPN1 gene, and its inhibitor —
calpastatin — encoded by the CAST gene, is involved in biological
processes regulation by partial degradation of substrates — cytoskeletal
proteins, signaling molecules and enzymes. Calpain system dysfunction caused by
mutations or Ca2+ elevation is associated primarily with diseases
affecting central nervous and cardiovascular systems, as well as skeletal
muscles. For cattle breeding purposes the calpain hyperactivity in the presence
of excess calcium ions (calcium passes out due to cell death) is considered to
be desirable offering the possibility to obtain more tender meat. This study is
aimed to analyze the polymorphic variants CAPN316 and CAST282 of
calpain and calpastatin genes in Aberdeen-Angus bred within Kharkiv region and
to compare obtained result with commercial herds of other countries. For the
SNP genotyping, PCR-RFLP methods were set up. Testing deviation from the
Hardy-Weinberg equilibrium was performed using Pearson’s chi-squared
test. Spearman’s correlation coefficient was used to measure the strength
of association between two characteristics. Cluster analysis was used to
classify the allele frequencies obtained within similar data obtained for
cattle in other countries. The allele and genotype frequencies of SNP CAPN316
(AF252504.2:g.5709C>G) in calpain gene are: C — 0.398
and G — 0.602; CC — 13.6%, CG — 52.3%
and GG — 34.1%. The allele and genotype frequencies of SNP CAST282
(AY_008267.1:g.282C>G) in calpastatin gene are: C —
0.807 and G — 0.193; CC — 63.6%, CG —
34.1% and GG — 2.3%. Group-to-group variability in allele C
frequency for SNP CAPN316 (0.37%) is higher than CAST282 (0.06%),
due to the modulating effect of the calpastatin. The Aberdeen-Angus herd of
Kharkiv region are comparable to the European commercial beef cattle herds by
allele frequencies. Association between latitudinal zonation and frequency of
allele C in cattle herds was demonstrated (R = 0.53, p < 0.05).
Keywords: Aberdeen-Angus
breed, calpain gene, calpastatin gene, SNP, meat tenderness
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http://dx.doi.org/10.2527/jas.2006-512
