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热休克蛋白与红系发育 被引量:1

Heat shock proteins and erythropoiesis
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摘要 热休克蛋白(heat shock protein, HSP)是一类广泛存在且高度保守的分子伴侣蛋白质,参与生物体多种生理生化过程的调控。红细胞生成起源于造血干细胞,发育调控高度特化且机制复杂。在生理性红细胞发育过程中,红系细胞的增殖与分化、血红蛋白的合成与降解及线粒体自噬等生命活动都需要热休克蛋白的参与。不仅如此,越来越多的证据表明,地中海贫血、纯红细胞再生障碍性贫血及骨髓异常增生综合征等红细胞异常相关疾病的发生与热休克蛋白的异常表达有关。因此,全面了解红系发育中热休克蛋白的作用与机制将有助于阐明这些红细胞异常相关疾病的发生机理,并由此探索更多的治疗策略。该文就目前热休克蛋白与红系发育相关的研究进行综述,并对相关疾病诊疗研究新方向提出展望。 Heat shock proteins(HSPs) are highly conserved and ubiquitous molecular chaperones that regulate various physiological and biochemical processes. Mature erythrocytes originate from hematopoietic stem cells. The regulation of erythrocyte development is highly specialized and the mechanisms are complex. Interestingly, HSPs are required in almost all stages of physiological erythropoiesis, including the proliferation and differentiation of erythroid cells, the synthesis and degradation of hemoglobin and mitophagy. Moreover, increasing evidence shows that the development of certain red blood cell disorders, such as thalassemia, pure erythrocyte aplastic anemia, and myelodysplastic syndromes are associated with dysregulated heat shock proteins. Therefore, a comprehensive understanding of how heat shock proteins regulate erythropoiesis will help to clarify the pathogenesis of these diseases, and further explore more treatment strategies. In this review, we describe current researches on the roles of heat shock proteins in erythroid development to provide knowledge basis and a new therapeutic idea for the future treatment of erythrocytes disorders.
作者 刘瑞 罗赛群 孙曙明 刘静 陈慧勇 LIU Rui;LUO Sai-Qun;SUN Shu-Ming;LIU Jing;CHEN Hui-Yong(School of Life Sciences,Central South University,Changsha 410011,China;Key Laboratory of Basic and Applied Hematology in Hunan Province,Central South University,Changsha 410078,China)
出处 《生命科学》 CSCD 北大核心 2022年第3期294-301,共8页 Chinese Bulletin of Life Sciences
基金 国家重点研发计划(2018YFA0107800) 国家自然科学基金项目(81920108004、81770107) 湖南省重点研发计划(2022SK2037) 湖南省自然科学基金项目(2021JJ30892) 长沙市自然科学基金项目(kq2014139)。
关键词 热休克蛋白 红细胞生成 分子伴侣 血红蛋白 线粒体 heat shock protein erythropoiesis chaperone hemoglobin mitochondria
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