The role of alpha-hemoglobin stabilizing protein in adult human hemoglobin assembly

Monday, October 24, 2011 — Poster Session I
Noon – 2:00 p.m.	Natcher Conference Center	NHLBI	BIOCHEM/CHEM-19

Authors

• T Mollan
• Y Xiang
• E Khandros
• M Weiss
• A Alayash
• J Olson

Abstract

Hemoglobin biosynthesis in erythrocyte precursors involves several steps. The correct ratios and concentrations of normal alpha and beta globin proteins must be expressed; apoproteins must be folded correctly; heme must be synthesized and incorporated into these globins rapidly; and the individual subunits must be rapidly and correctly assembled into heterotetramers. These events occur on a large scale in vivo, and dysregulation causes serious clinical disorders such as thalassemia syndromes. Recent work has implicated a conserved erythroid protein known as Alpha-Hemoglobin Stabilizing Protein (AHSP) as a participant in these events. Current evidence suggests that AHSP facilitates one or more early-stage post-translational hemoglobin biosynthetic events. In this work, recent experimental results are discussed in light of several current models describing globin subunit folding, heme uptake, assembly, and denaturation during hemoglobin synthesis. Particular attention is devoted to molecular interactions with AHSP that relate to Alpha chain oxidation and the ability of alpha chains to associate with partner beta chains.

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