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Effect of heat shock protein 70 polymorphism on thermotolerance in Tharparkar cattle
AIM: Out of various members of heat shock protein (HSP) superfamily which act a molecular chaperon by binding to the denaturing protein thus stabilizing them and preserving their activity, HSP70 are of major importance in thermotolerance development. Thus, present investigation aimed at a screening...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Veterinary World
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4819358/ https://www.ncbi.nlm.nih.gov/pubmed/27051194 http://dx.doi.org/10.14202/vetworld.2016.113-117 |
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author | Bhat, Sandip Kumar, Pushpendra Kashyap, Neeraj Deshmukh, Bharti Dige, Mahesh Shivanand Bhushan, Bharat Chauhan, Anuj Kumar, Amit Singh, Gyanendra |
author_facet | Bhat, Sandip Kumar, Pushpendra Kashyap, Neeraj Deshmukh, Bharti Dige, Mahesh Shivanand Bhushan, Bharat Chauhan, Anuj Kumar, Amit Singh, Gyanendra |
author_sort | Bhat, Sandip |
collection | PubMed |
description | AIM: Out of various members of heat shock protein (HSP) superfamily which act a molecular chaperon by binding to the denaturing protein thus stabilizing them and preserving their activity, HSP70 are of major importance in thermotolerance development. Thus, present investigation aimed at a screening of HSP70 gene for polymorphisms and possible differences in thermotolerance in Tharparkar breed of cattle. MATERIALS AND METHODS: A 295 bp fragment of HSP70 gene was subjected to polymerase chain reaction-single-strand conformation polymorphism (SSCP) followed by sequencing of different SSCP patterns in 64 Tharparkar cattle. A comparative thermotolerance of identified genotypes was analyzed using heat tolerance coefficients (HTCs) of animals for different seasons. RESULTS: Three SSCP patterns and consequently two alleles namely A and B were documented in one fragment of HSP70 gene. On sequencing, one single-nucleotide polymorphism with G > T substitution was found at a position that led to a change of amino acid aspartate to tyrosine in allele A. It was found that in maintaining near normal average rectal temperature, genotype AA was superior (p≤0.01). Genotype AA, thus, was found to be most thermotolerant genotype with the highest HTC (p≤0.01). CONCLUSION: The polymorphism at HSP70 is expected to be a potent determinant for heat tolerance in cattle, which may aid in selection for thermotolerance in cattle. |
format | Online Article Text |
id | pubmed-4819358 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Veterinary World |
record_format | MEDLINE/PubMed |
spelling | pubmed-48193582016-04-05 Effect of heat shock protein 70 polymorphism on thermotolerance in Tharparkar cattle Bhat, Sandip Kumar, Pushpendra Kashyap, Neeraj Deshmukh, Bharti Dige, Mahesh Shivanand Bhushan, Bharat Chauhan, Anuj Kumar, Amit Singh, Gyanendra Vet World Research Article AIM: Out of various members of heat shock protein (HSP) superfamily which act a molecular chaperon by binding to the denaturing protein thus stabilizing them and preserving their activity, HSP70 are of major importance in thermotolerance development. Thus, present investigation aimed at a screening of HSP70 gene for polymorphisms and possible differences in thermotolerance in Tharparkar breed of cattle. MATERIALS AND METHODS: A 295 bp fragment of HSP70 gene was subjected to polymerase chain reaction-single-strand conformation polymorphism (SSCP) followed by sequencing of different SSCP patterns in 64 Tharparkar cattle. A comparative thermotolerance of identified genotypes was analyzed using heat tolerance coefficients (HTCs) of animals for different seasons. RESULTS: Three SSCP patterns and consequently two alleles namely A and B were documented in one fragment of HSP70 gene. On sequencing, one single-nucleotide polymorphism with G > T substitution was found at a position that led to a change of amino acid aspartate to tyrosine in allele A. It was found that in maintaining near normal average rectal temperature, genotype AA was superior (p≤0.01). Genotype AA, thus, was found to be most thermotolerant genotype with the highest HTC (p≤0.01). CONCLUSION: The polymorphism at HSP70 is expected to be a potent determinant for heat tolerance in cattle, which may aid in selection for thermotolerance in cattle. Veterinary World 2016-02 2016-02-03 /pmc/articles/PMC4819358/ /pubmed/27051194 http://dx.doi.org/10.14202/vetworld.2016.113-117 Text en Copyright: © Bhat, et al. http://creativecommons.org/licenses/by/4.0 Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Bhat, Sandip Kumar, Pushpendra Kashyap, Neeraj Deshmukh, Bharti Dige, Mahesh Shivanand Bhushan, Bharat Chauhan, Anuj Kumar, Amit Singh, Gyanendra Effect of heat shock protein 70 polymorphism on thermotolerance in Tharparkar cattle |
title | Effect of heat shock protein 70 polymorphism on thermotolerance in Tharparkar cattle |
title_full | Effect of heat shock protein 70 polymorphism on thermotolerance in Tharparkar cattle |
title_fullStr | Effect of heat shock protein 70 polymorphism on thermotolerance in Tharparkar cattle |
title_full_unstemmed | Effect of heat shock protein 70 polymorphism on thermotolerance in Tharparkar cattle |
title_short | Effect of heat shock protein 70 polymorphism on thermotolerance in Tharparkar cattle |
title_sort | effect of heat shock protein 70 polymorphism on thermotolerance in tharparkar cattle |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4819358/ https://www.ncbi.nlm.nih.gov/pubmed/27051194 http://dx.doi.org/10.14202/vetworld.2016.113-117 |
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