Abstract
DURING the normal human perinatal period foetal haemoglobin (Hb F; α2γ2) is replaced by the major and minor adult haemoglobins, Hbs A (α2β2) and A2 (α2δ2) respectively1,2. Little is known about the mechanisms involved in the switch from γ- to β- and δ-chain production2 but there is evidence that if the switch could be even partially prevented, so allowing continued production of γ chains into adult life, it might be possible to improve the outlook for patients with the common genetic disorders of β-chain production, particularly sickle-cell anaemia and β thalassaemia1. Investigation of the control of human haemoglobin switching has been hampered by the lack of a suitable animal model since none of the small mammals commonly used in the laboratory have a true foetal haemoglobin3. However, the developmental changes in the haemoglobins of the sheep broadly mirror those observed in man; two embryonic haemoglobins are replaced early in gestation by a single foetal haemoglobin4 which in turn is replaced by the adult haemoglobins at about the time of birth5,6. The two adult haemoglobins of the sheep, Hb A and Hb B, are determined by pairs of alleles for their respective β chains, βA and βB. We have examined the switch from foetal to adult haemoglobin in the sheep to determine whether it is sufficiently similar to that in man to provide a suitable model for studying the control mechanisms involved in haemoglobin switching. In addition, we have carried out preliminary experiments to determine whether the switch may be under hormonal control.
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WOOD, W., PEARCE, K., CLEGG, J. et al. Switch from foetal to adult haemoglobin synthesis in normal and hypophysectomised sheep. Nature 264, 799–801 (1976). https://doi.org/10.1038/264799a0
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DOI: https://doi.org/10.1038/264799a0
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