Molecular cloning, expression pattern, and chemical analysis of heat shock protein 70 (HSP70) in the mudskipper Boleophthalmus pectinirostris: Evidence for its role in regulating spermatogenesis.

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  • Additional Information
    • Source:
      Publisher: Elsevier/North-Holland Country of Publication: Netherlands NLM ID: 7706761 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0038 (Electronic) Linking ISSN: 03781119 NLM ISO Abbreviation: Gene Subsets: MEDLINE
    • Publication Information:
      Original Publication: Amsterdam, Elsevier/North-Holland, 1976-
    • Subject Terms:
    • Abstract:
      Heat shock protein 70 (HSP70) is molecular chaperone that is important for reproductive biological processes. In this study, a full length HSP70 from the mudskipper (Boleophthalmus pectinirostris) was characterized. It was found to contain: a 108 bp 5'-untranslated region, a 208 bp 3'-untranslated region, and a 1953 bp open reading frame, which encodes a protein of 650 amino acids with a theoretical molecular weight of 71.1 kDa and an isoelectric point of 5.17. RT-PCR analysis revealed that HSP70 was ubiquitously expressed in all major tissues with differential expression levels. This suggests that HSP70 has vital and conserved biological functions. HSP70 was localized mainly in the cytoplasm of germinal cells, indicating an important role of this protein during spermatogenesis. In response to heat stress, the testes presented abnormal morphology in connective tissues, in which HSP70 immunoreactivity was not observed. HSP70 mRNA expression in the gill, liver, and testes was significantly increased, which suggests that HSP70 plays an important role in protection against heat stress.
      (Copyright © 2015 Elsevier B.V. All rights reserved.)
    • Contributed Indexing:
      Keywords: Boleophthalmus pectinirostris; HSP70; Immunohistochemistry; Injury; Testis
    • Accession Number:
      0 (Fish Proteins)
      0 (HSP70 Heat-Shock Proteins)
    • Publication Date:
      Date Created: 20150913 Date Completed: 20160318 Latest Revision: 20151126
    • Publication Date:
      20240829
    • Accession Number:
      10.1016/j.gene.2015.09.010
    • Accession Number:
      26361844