Cloning, characterization and cadmium inducibility of metallothionein in the testes of the mudskipper Boleophthalmus pectinirostris

Cloning, characterization and cadmium inducibility of metallothionein in the testes of the mudskipper Boleophthalmus pectinirostris
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DOI:
10.1016/j.ecoenv.2015.04.055
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发表时间:
2015-09-01
影响因子:
6.8
通讯作者:
Zhu, Jun-Quan
Zhu, Jun-Quan
中科院分区:
环境科学与生态学2区
文献类型:
--
作者:
Han, Ying-Li;Sheng, Zhang;Zhu, Jun-Quan

文献摘要

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金属硫蛋白(Metals thioneins,MTS)是富含半胱氨酸、低分子量、重金属结合的蛋白质分子。MT由于其丰富的半胱氨酸参与了活体动物体内的金属动态平衡和解毒。为了研究MT在弹涂鱼精子发生过程中的作用,我们确定了MT的全长,包括83个碱基的5‘非翻译区、110个碱基的3’非翻译区和一个183个碱基的开放阅读框。其他物种的MT序列之间的蛋白质比对显示出高度的相似性和很强的同源性,半胱氨酸残基对MT的金属结合亲和力至关重要。MT主要定位于生精细胞的胞浆,提示MT在精子发生和睾丸保护中起作用。镉(Cd)暴露后,睾丸组织出现形态异常和MT基因表达异常,提示睾丸MT对Cd反应敏感。因此,我们认为MTS在小球藻精子发生和睾丸对Cd毒害的保护中起着重要作用。(C)2015 Elsevier Inc.保留所有权利。
Metallothioneins (MTs) are cysteine-rich, low molecular weight, and heavy metal-binding protein molecules. MT participates in metallic homeostasis and detoxification in living animals due to its abundant cysteine. In order to investigate the functions of MT during spermiogenesis in the mudskipper (Boleophthalmus pectinirostris), we identified the MT complete which contains: an 83 bp 5' untranslated region, a 110 bp 3' untranslated region, and a 183 bp open reading frame. The protein alignment between MT sequences of other species shows a high similarity and a strong identity in cysteine residues vital for the metal-binding affinity of MT. The localizations of MT were mainly in the cytoplasm of germinal cells, indicating a role in spermatogenesis and testis protection. After the cadmium (Cd) exposure, the testis presents abnormal morphology and MT mRNA expression, both of which indicate a sensitive response of testis MT to Cd. Therefore, we suggest that MTs play an important role in spermatogenesis and testes protection against Cd toxicity in B. pectinirostris. (C) 2015 Elsevier Inc. All rights reserved.