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Globin Biosynthesis in Erythroid Bursts of Heterozygous α or β Thalassaemia
Author(s) -
Steinberg Martin H.,
Coleman Mary B.,
Pressley Annette,
Adams Junius G.
Publication year - 1981
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1981.tb02761.x
Subject(s) - globin , alpha (finance) , alpha globulin , microbiology and biotechnology , alpha chain , hemoglobinopathy , beta (programming language) , biology , sickle cell anemia , cell , peripheral blood mononuclear cell , chemistry , gene , hemolytic anemia , biochemistry , immunology , in vitro , medicine , construct validity , nursing , computer science , patient satisfaction , programming language
S ummary . We examined globin chain synthesis in erythroid bursts (BFU‐E) of patients with heterozygous α or β thalassaemia. BFU‐E were cloned from circulating mononuclear cells, labelled with [H]leucine and globin chains purified by gel filtration and column chromatography. In six patients heterozygous for β thalassaemia, globin synthesis in BFU‐E was nearly balanced, with an α/non α ratio of 1.05 0α12. These BFU‐E produced 33.8 12.7%γ globin chain, an amount similar ( P >1 0.05) to that found in 10 controls with sickle cell anaemia (25.6 6.7) but greater ( P <0.05) than that of five normal controls (17.2 2.2). The balanced globin synthesis appeared due to the large amounts of γ chain made by BFU‐E. In two α thalassaemia carriers, who also had sickle cell trait, the BFU‐E α/non‐α ratio was 0.67 and 0.79. These BFU‐E produced 15% and 20%γ chain and 39% and 45%β S globin. The synthesis of β S globin in BFU‐E exceeded the erythrocyte levels of 20% and 29% HbS and indicated nearly equal expression of β A and β B globin genes in these proliferating erythroid precursors. This provides further evidence that the low levels of HbS in sickle cell carriers with α thalassaemia are due to post‐translational events resulting from the differing affinity of β S and β A globin for α chain and the destruction of excessive β S chain.