ArticleFish physiology and biochemistry2015
Molecular characterization of heat-shock protein 90 gene and its expression in Gobiocypris rarus juveniles exposed to pentachlorophenol.
Article in Fish physiology and biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Molecular characterization of heat shock protein 70 and 90 genes and their expression analysis in air-breathing magur catfish (Clarias magur) while exposed to zinc oxide nanoparticles.Fish physiology and biochemistry · 2024Article
- Ultraviolet filters and heat shock proteins: effects in Chironomus riparius by benzophenone-3 and 4-methylbenzylidene camphor.Environmental science and pollution research international · 2018Article
- Orexin-A Rescues Chronic Copper-Dependent Behavioral and HSP90 Transcriptional Alterations in the Ornate Wrasse Brain.Neurotoxicity research · 2017Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat-shock protein 90 (HSP90) is an abundant and highly conserved molecular chaperone, and it fulfills a housekeeping function in contributing to the folding, maintenance of structural integrity, and proper regulation of a subset of cytosolic proteins. In this study, the full-length 2693-bp cDNA of HSP90 was cloned by rapid amplification of cDNA ends (RACE) technique from the liver of rare minnow (Gobiocypris rarus) for the first time, designated as GrHSP90. The complete coding sequence of GrHSP90 is 2181 bp in length, which encodes a polypeptide of 726 amino acids with a predicted molecular mass of 83.4 kDa and a theoretical isoelectric point of 4.90. Phylogenetic tree analysis indicated that deduced protein GrHSP90 had extensive sequence similarities to other fish HSP90s. Tissue distribution showed that GrHSP90 was constitutively expressed in a wide range of tissues including gill, blood, brain, fin, gonad, heart, intestine, kidney, liver, muscle, spleen, skin, and swim bladder. The highest expression was found in the gonad. Furthermore, significant increase in GrHSP90 mRNA in the liver was observed after exposure to pentachlorophenol ≥8 µg/L (p < 0.05). Our results suggest that GrHSP90 is indeed an ortholog of the HSP90 family and may be act as a biomarker to assess the effect of environmental contaminant.
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