The role of alpha-hemoglobin stabilizing protein in redox chemistry, denaturation, and hemoglobin assembly.

ABSTRACT: Hemoglobin biosynthesis in erythrocyte precursors involves several steps. The correct ratios and concentrations of normal alpha (alpha) and beta (beta) globin proteins must be expressed; apoproteins must be folded correctly; heme must be synthesized and incorporated into these globins rapidly; and the individual alpha and beta 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 enhances alpha subunit stability and diminishes its participation in harmful redox chemistry

SUBMITTER: Mollan TL 

PROVIDER: S-EPMC2821148 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature