2020
DOI: 10.3389/fgene.2020.541944
|View full text |Cite
|
Sign up to set email alerts
|

Inhibition of Embryonic HSP 90 Function Promotes Variation of Cold Tolerance in Zebrafish

Abstract: Accumulating evidence indicates that heat shock protein 90 (HSP90) plays essential roles in modulation of phenotypic plasticity in vertebrate development, however, the roles of HSP90 in modulation of cold tolerance capacity in fish are still unclear. In the present study, we showed that transient inhibition of embryonic HSP90 function by a chemical inhibitor or low conductivity stress promoted variation of cold tolerance capacity in adult zebrafish. Further work showed that embryonic HSP90 inhibition enhanced … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

0
4
0

Year Published

2022
2022
2024
2024

Publication Types

Select...
6

Relationship

0
6

Authors

Journals

citations
Cited by 8 publications
(4 citation statements)
references
References 55 publications
(59 reference statements)
0
4
0
Order By: Relevance
“…(Basu et al, 2002). Strong evidence suggests that HSPs have critical roles in helping fish cope with environmental change (Weber and Bosworth, 2005), but 12 HSP genes were down-regulated differentially expressed in this study, and the differential expression levels of HSP genes seem to be different in different fish coping with cold stress, e.g., the HSP genes were up-regulated expressed in channel catfish, L. lota lota and Puntius tetrazona (Weber and Bosworth, 2005;Liu L. L. et al, 2020;Yang et al, 2021), while down-regulated expressed in O. latipes, D. rerio, and Oratosquilla oratoria (Ikeda et al, 2017;Lou et al, 2019;Han et al, 2020). In a similar situation, the focal adhesion pathway of Gasterosteus aculeatus was down-regulated expressed (Metzger and Schulte, 2018), which was similar to the result of H. nehereus, while L. polyactis was up-regulated expressed (Liu F. et al, 2020).…”
Section: Protein Modificationmentioning
confidence: 60%
See 1 more Smart Citation
“…(Basu et al, 2002). Strong evidence suggests that HSPs have critical roles in helping fish cope with environmental change (Weber and Bosworth, 2005), but 12 HSP genes were down-regulated differentially expressed in this study, and the differential expression levels of HSP genes seem to be different in different fish coping with cold stress, e.g., the HSP genes were up-regulated expressed in channel catfish, L. lota lota and Puntius tetrazona (Weber and Bosworth, 2005;Liu L. L. et al, 2020;Yang et al, 2021), while down-regulated expressed in O. latipes, D. rerio, and Oratosquilla oratoria (Ikeda et al, 2017;Lou et al, 2019;Han et al, 2020). In a similar situation, the focal adhesion pathway of Gasterosteus aculeatus was down-regulated expressed (Metzger and Schulte, 2018), which was similar to the result of H. nehereus, while L. polyactis was up-regulated expressed (Liu F. et al, 2020).…”
Section: Protein Modificationmentioning
confidence: 60%
“…This result was similar to the pathway enriched by other fish under cold stress, like the proteasome pathway in D. rerio (Long et al, 2013) and Pampus argenteus (Zhang et al, 2022), and protein processing in endoplasmic reticulum pathway in D. rerio (Long et al, 2013), Lota lota lota (Yang et al, 2021), and O. latipes (Ikeda et al, 2017). The ubiquitin proteasome system catalyzes the great majority of the protein degradation, including both the rapid degradation of misfolded and regulation proteins (Zhao et al, 2015), therefore, the ubiquitin protease system may clear the misfolded proteins and accelerate the renewal of damaged cells for H. nehereus under low-temperature environments (Han et al, 2020). Although the endoplasmic reticulum is the primary place of protein synthesis, it is also the site of protein degradation (Christianson and Ye, 2014).…”
Section: Protein Modificationmentioning
confidence: 99%
“…The heat shock protein 90 (HSP90) plays an essential role in the modulation of phenotypic plasticity in vertebrate development; however, the roles of HSP90 in the modulation of cold tolerance capacity in fish are still unclear [35]. A study by Han et al reports that the transient inhibition of the embryonic HSP90 function by a chemical inhibitor or by low conductivity stress promoted the variation in cold tolerance capacity in adult zebrafish [35]. The exposure to Cafodos induced a quick and temporary increase in HSP90 after 3 h, therefore confirming the main effects of the hydrogen peroxide contained in this illicit additive.…”
Section: Skinmentioning
confidence: 99%
“…Quite a few HSP genes have been identified in zebrafish, including several members of the HSP47, HSP70, and HSP90 families [160]. The heat shock response has been well studied in zebrafish, together with the role of HSPs during embryonic development [160][161][162][163][164]. Information on the inflammatory functions of zebrafish HSPs are scarcer but extracellular HSP60 has, for example, been shown to act as a leukocyte chemoattractant in hair cell or caudal fin injury models [165].…”
Section: Hspsmentioning
confidence: 99%