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Updated: Feb 10, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
Published on: December 29, 2021
Alpha-hemoglobin-stabilizing protein: an erythroid molecular chaperone
Maria Emília Favero1, Fernando Ferreira Costa
1Department of Pathology, Clinical Analysis and Toxicology, University Hospital, State University of Londrina (UEL), Avenida Robert Koch, 60, Vila Operária, 86038-350 Londrina, PR, Brazil.
Abstract:
Alpha-hemoglobin-stabilizing protein (AHSP) is an erythroid-specific protein that acts as a molecular chaperone for the free α chains of hemoglobin. Evidence strongly suggests that AHSP participates in hemoglobin synthesis and may act to neutralize the cytotoxic effects of excess free alpha-globin subunits that accumulate both in normal and beta-thalassemic erythroid precursor cells. As such, AHSP seems to be essential for normal erythropoiesis, and impaired upregulation of AHSP may lead to premature erythroid cell death, resulting in ineffective erythropoiesis. Reduced AHSP mRNA expression has been associated with clinical variability in some cases of β-thalassemia. It has been shown that αHb variants may also impair AHSP-αHb interactions, leading to pathological conditions that resemble α-thalassemia syndromes. The aim of this paper is to summarize current information concerning the structure and function of AHSP, focusing on its role in normal erythropoiesis and its relevance in health and disease.
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