Expression of lactate dehydrogenase is induced during hypoxia via HIF-1 in the mud crab Scylla paramamosain

Comp Biochem Physiol C Toxicol Pharmacol. 2019 Nov:225:108563. doi: 10.1016/j.cbpc.2019.108563. Epub 2019 Jul 2.

Abstract

Lactate dehydrogenase (LDH) is a key enzyme involved in anaerobic metabolism in most organisms. In the present study, we determined the structure and function of LDH sequence in Scylla paramamosain (SpLDH) by gene cloning, expression and RNA interference techniques in order to explore the genetic characteristics of LDH and its relationship with HIF-1 during hypoxia. The full-length cDNA was 1453 bp with an open reading frame (ORF) of 996 bp, and encoded a polypeptide of 332 amino acids. Homology analysis showed that the SpLDH gene is highly similar to arthropods. The SpLDH transcript increased after hypoxia in all tested tissues. The silencing of HIF-1 blocked the increase in LDH mRNA and activity, which were induced by hypoxia in gill and muscle tissues. Our results indicated that SpLDH expression was regulated transcriptionally by HIF-1.

Keywords: Gene silencing; Hypoxia; Hypoxia-inducible factor-1α; Lactate dehydrogenase; Scylla paramamosain.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arthropod Proteins* / classification
  • Arthropod Proteins* / genetics
  • Arthropod Proteins* / physiology
  • Brachyura* / enzymology
  • Brachyura* / genetics
  • Cloning, Molecular
  • DNA, Complementary
  • Hypoxia / metabolism*
  • Hypoxia-Inducible Factor 1, alpha Subunit / metabolism
  • L-Lactate Dehydrogenase* / classification
  • L-Lactate Dehydrogenase* / genetics
  • L-Lactate Dehydrogenase* / physiology
  • Open Reading Frames
  • Phylogeny
  • Sequence Alignment

Substances

  • Arthropod Proteins
  • DNA, Complementary
  • Hypoxia-Inducible Factor 1, alpha Subunit
  • L-Lactate Dehydrogenase