Normal human hemoglobin picks up oxygen in the lungs and delivers it to needy cells in order to keep their molecular and cellular engines operating at maximal efficiency.
Hemoglobin is comprised of pairs of alpha- and beta-globin chains in combination with heme. Recently, the small alpha hemoglobin?stabilizing protein (AHSP) was identified and found to specifically bind to and stabilize alpha-globin, limiting the toxic effects of excess alpha-globin in the inherited blood disorder beta-thalassemia.
In the July 2 issue of the Journal of Clinical Investigation, Mitchell Weiss and colleagues from The Children?s Hospital of Philadelphia show that, in mice, AHSP is important not only for dealing with newly synthesized excess alpha-globin, but also in the assembly and stabilization of normal amounts of hemoglobin, even when alpha-globin is deficient, indicating unique and previously unidentified roles for this molecule.
In an accompanying commentary, Arthur Bank from Columbia University discusses the identification of AHSP as a unique hemoglobin helper and the role it may play in diseases in which alpha- or beta-globin production is altered.
TITLE: An erythroid chaperone that facilitates folding of alpha-globin subunits for hemoglobin synthesis