Abstract
HAEMOGLOBIN H (Hb H; β4) disease results from a reduced rate of synthesis of the α chains of human adult haemoglobin (Hb A; α2β2). In the absence of sufficient α chains, excess (β chains form β4 tetramers which are unstable, precipitate and cause a shortened red cell survival1. Hb H disease is one of the α-thalassaemia syndromes. These disorders usually result from interactions of three α-thalassaemia (α thal) genes; α thal 1, α thal 2 and Hb Constant Spring. In many human populations the α-chain loci are duplicated, that is, there are two per haploid genome2. The gene α thal 1 results from a deletion of both of the pair of haploid α-chain genes3,4, α thal 2 from a deletion of one of the pair5, and Hb Constant Spring from a chain termination mutation affecting one of the linked loci which markedly reduces the output of α chains and produces a phenotype almost identical to α thal 2(ref. 6). Haemoglobin H disease results from the inheritance of α thal 1 together with either α thal 2 or Hb Constant Spring. There have been occasional reports of an acquired form of Hb H disease occurring in association with leukaemia or related myeloproliferative disorders7–12. We have studied the blood and bone marrow of a patient with acquired Hb H disease and we report here that it has a completely different molecular basis from the genetic form.
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OLD, J., LONGLEY, J., WOOD, W. et al. Molecular basis for acquired haemoglobin H disease. Nature 269, 524–525 (1977). https://doi.org/10.1038/269524a0
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DOI: https://doi.org/10.1038/269524a0
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