Heat Shock Protein 40 (HSP40) in Pacific White Shrimp (Litopenaeus vannamei): Molecular Cloning, Tissue Distribution and Ontogeny, Response to Temperature, Acidity/Alkalinity and Salinity Stresses, and Potential Role in Ovarian Development
Heat Shock Protein 40 (HSP40) in Pacific White Shrimp (Litopenaeus vannamei): Molecular Cloning, Tissue Distribution and Ontogeny, Response to Temperature, Acidity/Alkalinity and Salinity Stresses, and Potential Role in Ovarian Development
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太平洋白虾（Litopenaeus vannamei）中的热休克蛋白 40 (HSP40)：分子克隆、组织分布和个体发育、对温度、酸度/碱度和盐度应激的响应以及在卵巢发育中的潜在作用
DOI：
10.3389/fphys.2018.01784
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发表时间：
2018-12-12
影响因子：
4
通讯作者：
Ren, Chunhua
中科院分区：
文献类型：
--
作者：
Chen, Ting;Lin, Tiehao;Ren, Chunhua
热休克蛋白（Heat shock proteins，HSPs）是一类由细胞在应激反应中产生的保守蛋白质家族，是一种具有管家和细胞保护功能的分子伴侣。热休克蛋白40（HSP 40）是热休克蛋白70（HSP 70）的辅助分子伴侣，参与ATP水解的调节。不像它的辅助因子HSP 70，目前知之甚少的生物学功能的HSP 40在甲壳类物种，如对虾。本研究从南美白色对虾中克隆了编码HSP 40的cDNA（Lv-HSP 40）。Lv-HSP 40的结构特征表明其属于Ⅰ型HSP 40。肌肉、鳃和肝胰腺是Lv-HSP 40转录表达的主要部位。在这些组织中，Lv-HSP 40 mRNA主要表达于心肌细胞、上皮细胞和肝胰腺细胞。在急性热胁迫条件下，Lv-HSP 40在这3种组织中的转录水平均受到显著诱导，而低pH胁迫仅上调肝胰腺和鳃中的Lv-HSP 40 mRNA。在个体发育过程中，Lv-HSP 40的转录水平在胚胎早期较高，在胚胎晚期和早期幼虫阶段急剧下降。卵巢是Lv-HSP 40 mRNA表达的另一个主要器官，Lv-HSP 40 mRNA主要表达于卵泡细胞，而在卵母细胞中仅检测到少量表达。卵巢Lv-HSP 40 mRNA水平在性腺发育过程中不断增加。通过RNA干扰沉默Lv-HSP 40基因可有效延迟单侧眼柄切除后的卵巢成熟。推测Lv-HSP 40在卵巢发育中的作用不依赖于其辅因子HSP 70、卵黄生成因子卵黄原蛋白（Vg）和卵黄原蛋白受体（VgR）。我们的研究为深入了解HSP 40在L.结论：（1）HSP 40是应激反应因子，（2）HSP 40参与胚胎和卵巢的发育。
Heat shock proteins (HSPs), a family of conserved proteins that are produced by cells in response to stresses, are known as molecular chaperones with a range of housekeeping and cellular protective functions. The 40 kD heat shock protein (HSP40) is a co-chaperone for HSP70 in the regulation of ATP hydrolysis. Unlike its well-documented cofactor HSP70, little is currently known regarding the biological functions of HSP40 in crustacean species such as penaeid shrimp. In the present study, the cDNA encoding HSP40 (Lv-HSP40) was identified from the Pacific white shrimp Litopenaeus vannamei, a highly significant commercial culture species. The structural organization indicates that Lv-HSP40 belongs to the type-I HSP40s. The muscle, gill, and hepatopancreas are the main sites of Lv-HSP40 transcript expression. Within these tissues, Lv-HSP40 mRNA were predominantly exhibited in the myocytes, epithelial cells and hepatopancreatic cells, respectively. Under acute thermal stress in the culture environment, Lv-HSP40 transcript levels are significantly induced in these three tissues, while low pH stress only upregulates Lv-HSP40 mRNA in the hepatopancreas and gill. During ontogenesis, Lv-HSP40 transcript levels are high at early embryonic stages and drop sharply at late embryonic and early larval stages. The ovary is another major organ of Lv-HSP40 mRNA expression in female shrimp, and Lv-HSP40 transcripts were mainly presented in the follicle cells but only weekly detected in the oocytes. Ovarian Lv-HSP40 mRNA levels increase continuously during gonadal development. Silencing of the Lv-HSP40 gene by RNA interference may effectively delay ovarian maturation after unilateral eyestalk ablation. The roles of Lv-HSP40 in ovarian development are speculated to be independent of its cofactor HSP70, and the vitellogenesis factor vitellogenin (Vg) and vitellogenin receptor (VgR). Our study, as a whole, provides new insights into the roles of HSP40 in multiple physiological processes in L. vannamei: (1) HSP40 is a responding factor during stressful conditions; and (2) HSP40 participates in embryonic and ovarian development.