Identification of cDNAs encoding HSP70 and HSP90 in the abalone Haliotis tuberculata: Transcriptional induction in response to thermal stress in hemocyte primary culture

Comp Biochem Physiol B Biochem Mol Biol. 2007 Apr;146(4):540-50. doi: 10.1016/j.cbpb.2006.12.006. Epub 2006 Dec 28.

Abstract

Heat-shock proteins are a multigene family of proteins whose expression is induced by a variety of stress factors. This work reports the cloning and sequencing of HSP70 and HSP90 cDNAs in the gastropod Haliotis tuberculata. The deduced amino acid sequences of both HSP70 and HSP90 from H. tuberculata shared a high degree of homology with their homologues in other species, including typical eukaryotic HSP70 and HSP90 signature sequences. We examined their transcription expression pattern in abalone hemocytes exposed to thermal stress. Real-time PCR analysis indicated that both HSP70 and HSP90 mRNA were expressed in control animals but rapidly increased after heat-shock.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Survival
  • Cells, Cultured
  • Cloning, Molecular / methods
  • DNA, Complementary
  • Gastropoda / physiology*
  • Gene Expression Regulation
  • HSP70 Heat-Shock Proteins / genetics*
  • HSP70 Heat-Shock Proteins / metabolism
  • HSP90 Heat-Shock Proteins / genetics*
  • HSP90 Heat-Shock Proteins / metabolism
  • Heat-Shock Response / genetics*
  • Hemocytes / cytology
  • Hemocytes / physiology*
  • Molecular Sequence Data
  • RNA, Messenger
  • Sequence Homology, Amino Acid
  • Transcription, Genetic

Substances

  • DNA, Complementary
  • HSP70 Heat-Shock Proteins
  • HSP90 Heat-Shock Proteins
  • RNA, Messenger

Associated data

  • GENBANK/AM283515
  • GENBANK/AM283516