Vasseur C, Baudin-Creuza V
Institut national de la santé et de la recherche médicale (INSERM) U955, équipe 2, université Paris Est Créteil, 5, avenue Gustave-Eiffel, 94000 Créteil, France; Laboratoire d'excellence des globules rouges (GR-EX), 75015 Paris, France.
Institut national de la santé et de la recherche médicale (INSERM) U955, équipe 2, université Paris Est Créteil, 5, avenue Gustave-Eiffel, 94000 Créteil, France; Laboratoire d'excellence des globules rouges (GR-EX), 75015 Paris, France.
Transfus Clin Biol. 2015 Mar;22(1):49-57. doi: 10.1016/j.tracli.2015.01.002. Epub 2015 Feb 25.
Alpha-hemoglobin stabilizing protein (AHSP), described as a chaperone of alpha-hemoglobin (α-Hb), is synthesized at a high concentration in the erythroid precursors. AHSP specifically recognizes the G and H helices of α-Hb and forms a stable complex with free α-Hb until its association with the partner β-subunits. Unlike the free β-Hb which are soluble and form homologous tetramers, freshly synthesized α-Hb chains are highly unstable molecular species which precipitate and generate reactive oxygen species within the erythrocyte precursors of the bone marrow leading to apoptosis and ineffective erythropoiesis. AHSP protects the free α-Hb chains in maintaining it in the soluble state. In this review, we report data from the literature and our laboratory concerning the key role of AHSP in the biosynthesis of Hb and its possible involvement in some disorders of the red blood cell as well as the hemoglobinopathies and we discuss its use as a prognostic tool in thalassemia syndromes.
α-血红蛋白稳定蛋白（AHSP），被描述为α-血红蛋白（α-Hb）的伴侣蛋白，在红系前体细胞中高浓度合成。AHSP特异性识别α-Hb的G螺旋和H螺旋，并与游离的α-Hb形成稳定复合物，直至其与伴侣β亚基结合。与可溶并形成同源四聚体的游离β-Hb不同，新合成的α-Hb链是高度不稳定的分子，会在骨髓的红系前体细胞内沉淀并产生活性氧，导致细胞凋亡和无效造血。AHSP通过将游离的α-Hb链维持在可溶状态来对其进行保护。在本综述中，我们报告了来自文献和我们实验室的数据，这些数据涉及AHSP在血红蛋白生物合成中的关键作用及其可能参与的一些红细胞疾病以及血红蛋白病，并且我们讨论了其作为地中海贫血综合征预后工具的用途。
