科研之友
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摘要
Heat shock proteins (HSPs) are induced upon elevated temperature in fishes. HSPs also function as molecular chaperones for cellular proteins, including steroid hormone receptors. Estrogen receptors (ERs) are critical for the hormone signaling necessary during the liver production of the yolk precursor protein vitellogenin in oviparous vertebrates. Considering the possible regulatory role of HSPs on the ER signaling pathway, the present study characterized the mRNA expression of all known isoforms of HSP70 (hsp70a, hsp70b), HSP90 (hsp90a1a, hsp90a1b, hsp90a2a, hsp90a2b, hsp90bl, hsp90b2), and ERs (er alpha 1, er alpha 2, er beta 1, er beta 2) in Rainbow Trout hepatocytes following an acute heat shock (1 hat 25 degrees C) compared to a control treatment (12 degrees C). The results showed that the mRNA levels of hsp70a, hsp70b, hsp90a1b, hsp90a2a, and hsp90b2 were significantly increased after heat shock, while er alpha 1 mRNA levels were significantly reduced by this treatment. hsp9Oal a, hsp90a2b, hsp90b1, er alpha 2, er beta 1 and er beta 2 were unaffected by this acute hyperthermic treatment. Comparatively, the responses of the two hsp70 isoforms were much greater than the hsp90 isoforms. Acute heat shock treatment of hepatocytes followed by a 24 h exposure to 17 beta-estradiol (E2) exposure also resulted in decreased expression of er alpha 1 mRNA, but not vitellogenin (vtg) mRNA. This study showed that some hsp70 and hsp90 isoforms display a robust response to an acute hyperthermic treatment in Rainbow Trout hepatocytes. Among the transcripts measured here, the er alpha 1 isoform uniquely showed significantly decreased mRNA levels upon acute heat treatment.
- 出版日期2016-11
- 单位中国水产科学研究院
