In:
Israeli Journal of Aquaculture - Bamidgeh, SAABRON PRESS, Vol. 70 ( 2018-1-1)
Abstract:
Heat shock proteins (HSPs) play an important role in protecting organisms against various stressors. Heat shock protein 40 (HSP40) is a class of the heat shock protein family and performs a function as co-chaperone of HSP70. In this study, an HSP40 gene from the mud crab Scylla paramamosain (SpHSP40) was identified and characterized. The full-length cDNA of SpHSP40 was 1904 bp, containing an open reading frame (ORF) of 1191 bp, a 5´UTR of 118 bp, and a 3´UTR of 595 bp. The deduced amino acid sequence of SpHSP40 contained all four classical HSP40 family signatures. Quantitative real-time PCR analysis revealed that SpHSP40 transcript was expressed in a wide range of tissues, while strong expression was observed in the hepatopancreas. In order to understand the response of heat shock proteins induced by nitrite exposure, expression levels of HSPs (SpHSP90, SpHSP70, SpHSP60 and SpHSP40) mRNA in the hepatopancreas and gills were investigated. Results show that HSPs (SpHSP90, SpHSP70, SpHSP60 and SpHSP40) were up-regulated displaying a time-dependent pattern in response to nitrite stress. All these results indicate that HSPs play an important role in mediating environmental stress in mud crabs.
Type of Medium:
Online Resource
ISSN:
0792-156X
,
0792-156X
Language:
English
Publisher:
SAABRON PRESS
Publication Date:
2018
detail.hit.zdb_id:
291787-7
detail.hit.zdb_id:
2542938-3
SSG:
21,3
