Huihui WANG,Xiaolong TANG,Yan WANG,et al.Function of Lactate Dehydrogenase in Cardiac and Skeletal Muscle of Phrynocephalus Lizard in Relation to High-Altitude Adaptation[J].Asian Herpetological Research(AHR),2018,9(4):258-273.[doi:10.16373/j.cnki.ahr.170075]
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Function of Lactate Dehydrogenase in Cardiac and Skeletal Muscle of Phrynocephalus Lizard in Relation to High-Altitude Adaptation
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Asian Herpetological Research[ISSN:2095-0357/CN:51-1735/Q]

Issue:
2018 VoI.9 No.4
Page:
258-273
Research Field:
Publishing date:
2018-12-25

Info

Title:
Function of Lactate Dehydrogenase in Cardiac and Skeletal Muscle of Phrynocephalus Lizard in Relation to High-Altitude Adaptation
Author(s):
Huihui WANG1;  Xiaolong TANG1*;  Yan WANG1;  Yuxia FENG1;  Peng PU1;  Shengkang MEN1;  Youli ZHAO2;  Zhennan PENG3 and Qiang CHEN1*
1 Institute of Biochemistry and Molecular Biology, School of Life Science, Lanzhou University, Lanzhou 730000, China
2 Lanzhou University Second Hospital, Lanzhou 730000, China
3 School of Life Science, Lanzhou University, Lanzhou 730000, China
Keywords:
lactate dehydrogenase (LDH);  high altitude;  adaptation;  anaerobic metabolism;  Phrynocephalus erythrurus
PACS:
-
DOI:
10.16373/j.cnki.ahr.170075
Abstract:
Poikilothermic animals living in high-altitude environments can be greatly affected by the anaerobic metabolism and lactate recycling, which are catalyzed by an enzyme called lactate dehydrogenase (LDH). However, the function and possible regulatory mechanisms of their anaerobic glycolysis remained elusive. We compared the difference in LDH between a native high-altitude (4 353 m) lizard, Phrynocephalus erythrurus, and a closely related species, Phrynocephalus przewalskii that lives in intermediate altitude environment (1 400 m). The activity of LDH, the concentration of lactate, the distribution of isoenzyme, and the mRNA amounts of Ldh-A and Ldh-B were determined. In cardiac muscle, the lactate-forming activity of P. erythrurus in LDH was higher than of P. przewalskii LDH at all three temperatures tested (10 °C, 25 °C and 35 °C), while lactate-oxidation activity of LDH was significantly different between the two species only at 25 °C and 35 °C. In skeletal muscle, both lactate-forming and lactate-oxidation rates of P. erythrurus were lower than that of P. przewalskii. There was a higher proportion of H subunit and a significantly higher expression of Ldh-B, with a concomitant decrease of lactate concentration in P. erythrurus. These results indicate that P. erythrurus may have a strong potential for anaerobic metabolism, which is likely adapted to the hypoxic environment at high altitudes. Furthermore, P. erythrurus is capable of oxidizing more lactate than P. przewalskii. The Ldh-A cDNA of the two species consists of a 999 bp open reading frame (ORF), which encodes 332 amino acids, while Ldh-B cDNA consists of a 1 002 bp ORF encoding 333 amino acids. LDHA has the same amino acid sequence between the two species, but three amino acid substitutions (V12I, N21S and N318K) were observed in LDHB. Structure analysis of LDH indicated that the substitutions of residues Val12 and Asp21 in P. erythrurus could be responsible for the high-altitude adaptation. The LDH characteristics of LDH in P. erythrurus suggest unique adaptation strategies of anaerobic metabolism in hypoxia and cold environments at high altitudes for poikilothermic animals.

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Last Update: 2018-12-26