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The responsive expression of heat shock protein 22 gene in zhikong scallop Chlamys farreri against a bacterial challenge
- Zhang, Lei, Wang, Lingling, Zhao, Jianmin, Qiu, Limei, Song, Linsheng, Dong, Chaohua, Li, Fengmei
- Aquaculture research 2010 v.41 no.2 pp. 257-266
- Chlamys, apoptosis, complementary DNA, gene expression, genes, gills, gonads, heart, heat shock proteins, hepatopancreas, isoelectric point, kidneys, molecular weight, muscles, open reading frames, scallops, signal peptide
- HSP22 is a member of a small HSP subfamily contributing to the growth, transformation and apoptosis of the cell as well as acting as a molecular chaperone. In the present study, CfHSP22 cDNA was cloned from Chlamys farreri by the rapid amplification of cDNA ends technique. The full-length cDNA of CfHSP22 was of 1279 bp, consisting of a 5′-terminal untranslated region (5′UTR) of 122 bp, a 3′UTR of 581 bp with a canonical polyadenylation signal sequence AATAAA and a poly(A) tail, and an open reading frame of 576 bp encoding a polypeptide with a molecular mass of 22.21 kDa and a predicted isoelectric point of 9.69. There was an α-crystallin domain, a hallmark of the sHSP subfamily, in the C-terminus, and the deduced amino acid sequence of CfHSP22 showed high similarity to previously identified HSP22s. CfHSP22 was constitutively expressed in the haemocyte, muscle, kidney, gonad, gill, heart and hepatopancreas, and the expression level in the hepatopancreas was higher than that in the other tissues. CfHSP22 transcription was up-regulated and reached a maximal level at 12 h after the bacterial challenge, and then declined progressively to the original level at 48 h. These results suggested that CfHSP22 perhaps play a critical role in response to the bacterial challenge in haemocytes of scallop C. farreri.