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Regulating glycolysis and heat shock proteins in Gannan yaks (Bos grunniens) in response to hypoxia of the Qinghai–Tibet Plateau

Glycolysis and heat shock proteins (HSPs) play an important role in hypoxia-intolerant species during hypoxia conditions. This study was conducted to evaluate the differences of glycolysis and heat shock proteins (HSPs) in Gannan yaks (Bos grunniens), with the main goal of understanding how the resp...

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Autores principales: Wen, Yuliang, Wang, Jiqing, Liu, Xiu, Li, Shaobin, Hu, Jiang, Luo, Yuzhu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Copernicus GmbH 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8386194/
https://www.ncbi.nlm.nih.gov/pubmed/34458561
http://dx.doi.org/10.5194/aab-64-345-2021
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author Wen, Yuliang
Wang, Jiqing
Liu, Xiu
Li, Shaobin
Hu, Jiang
Luo, Yuzhu
author_facet Wen, Yuliang
Wang, Jiqing
Liu, Xiu
Li, Shaobin
Hu, Jiang
Luo, Yuzhu
author_sort Wen, Yuliang
collection PubMed
description Glycolysis and heat shock proteins (HSPs) play an important role in hypoxia-intolerant species during hypoxia conditions. This study was conducted to evaluate the differences of glycolysis and heat shock proteins (HSPs) in Gannan yaks (Bos grunniens), with the main goal of understanding how the response to hypoxia changes with altitude. Here, the genes and enzymes of glycolysis and HSPs were detected in heart, liver, lung, kidney, and longissimus dorsi from Gannan yaks at different altitude (2500 and 3500  [Formula: see text]) using qPCR, western blot, and enzyme kits. The results showed that the expression of HIF1A and PDK4 was increased with altitude ([Formula: see text]) in above tissues. Significantly increased lactate dehydrogenase (LDH), adenosine triphosphate (ATP), and nicotinamide adenine dinucleotide (NADH) levels and the ratio of NADH/NAD [Formula: see text] were also observed in heart, lung, and longissimus dorsi tissues ([Formula: see text]), as well as a decreased citric acid (CA) level ([Formula: see text]). Furthermore, we observed significant global increases in the protein and mRNA expression levels of both the ATP-independent HSP27 and the ATP-dependent HSP60 during hypoxic conditions ([Formula: see text]). These findings revealed that hypoxia-reprogrammed glucose metabolism promotes energy supply via up-regulated glycolysis and weakness of the tricarboxylic acid (TCA) cycle. HSPs were activated and the prioritization of cytoprotective protein chaperone functions over energy conservation in yak under hypoxic conditions. These results are useful to better understand the unique adaptability of yak, allowing them to survive in hypoxia conditions.
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spelling pubmed-83861942021-08-26 Regulating glycolysis and heat shock proteins in Gannan yaks (Bos grunniens) in response to hypoxia of the Qinghai–Tibet Plateau Wen, Yuliang Wang, Jiqing Liu, Xiu Li, Shaobin Hu, Jiang Luo, Yuzhu Arch Anim Breed Original Study Glycolysis and heat shock proteins (HSPs) play an important role in hypoxia-intolerant species during hypoxia conditions. This study was conducted to evaluate the differences of glycolysis and heat shock proteins (HSPs) in Gannan yaks (Bos grunniens), with the main goal of understanding how the response to hypoxia changes with altitude. Here, the genes and enzymes of glycolysis and HSPs were detected in heart, liver, lung, kidney, and longissimus dorsi from Gannan yaks at different altitude (2500 and 3500  [Formula: see text]) using qPCR, western blot, and enzyme kits. The results showed that the expression of HIF1A and PDK4 was increased with altitude ([Formula: see text]) in above tissues. Significantly increased lactate dehydrogenase (LDH), adenosine triphosphate (ATP), and nicotinamide adenine dinucleotide (NADH) levels and the ratio of NADH/NAD [Formula: see text] were also observed in heart, lung, and longissimus dorsi tissues ([Formula: see text]), as well as a decreased citric acid (CA) level ([Formula: see text]). Furthermore, we observed significant global increases in the protein and mRNA expression levels of both the ATP-independent HSP27 and the ATP-dependent HSP60 during hypoxic conditions ([Formula: see text]). These findings revealed that hypoxia-reprogrammed glucose metabolism promotes energy supply via up-regulated glycolysis and weakness of the tricarboxylic acid (TCA) cycle. HSPs were activated and the prioritization of cytoprotective protein chaperone functions over energy conservation in yak under hypoxic conditions. These results are useful to better understand the unique adaptability of yak, allowing them to survive in hypoxia conditions. Copernicus GmbH 2021-08-19 /pmc/articles/PMC8386194/ /pubmed/34458561 http://dx.doi.org/10.5194/aab-64-345-2021 Text en Copyright: © 2021 Yuliang Wen et al. https://creativecommons.org/licenses/by/4.0/This work is licensed under the Creative Commons Attribution 4.0 International License. To view a copy of this licence, visit https://creativecommons.org/licenses/by/4.0/
spellingShingle Original Study
Wen, Yuliang
Wang, Jiqing
Liu, Xiu
Li, Shaobin
Hu, Jiang
Luo, Yuzhu
Regulating glycolysis and heat shock proteins in Gannan yaks (Bos grunniens) in response to hypoxia of the Qinghai–Tibet Plateau
title Regulating glycolysis and heat shock proteins in Gannan yaks (Bos grunniens) in response to hypoxia of the Qinghai–Tibet Plateau
title_full Regulating glycolysis and heat shock proteins in Gannan yaks (Bos grunniens) in response to hypoxia of the Qinghai–Tibet Plateau
title_fullStr Regulating glycolysis and heat shock proteins in Gannan yaks (Bos grunniens) in response to hypoxia of the Qinghai–Tibet Plateau
title_full_unstemmed Regulating glycolysis and heat shock proteins in Gannan yaks (Bos grunniens) in response to hypoxia of the Qinghai–Tibet Plateau
title_short Regulating glycolysis and heat shock proteins in Gannan yaks (Bos grunniens) in response to hypoxia of the Qinghai–Tibet Plateau
title_sort regulating glycolysis and heat shock proteins in gannan yaks (bos grunniens) in response to hypoxia of the qinghai–tibet plateau
topic Original Study
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8386194/
https://www.ncbi.nlm.nih.gov/pubmed/34458561
http://dx.doi.org/10.5194/aab-64-345-2021
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