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Measurement of Heme Synthesis Levels in Mammalian Cells
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Published on: July 9, 2015

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[Role of alpha-hemoglobin molecular chaperone in the hemoglobin formation and clinical expression of some

C Vasseur1, V Baudin-Creuza1

  • 1Institut 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.

Transfusion Clinique Et Biologique : Journal De La Societe Francaise De Transfusion Sanguine
|March 1, 2015
PubMed

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.

Keywords:
AHSP alpha-hemoglobin chaperoneAHSP chaperon de l’alpha-hémoglobineGlobules rougesHemoglobinHémoglobineMarker of erythroid precursorsMarqueur érythroïdeRed blood cellThalassemiasThalassémies

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