Hemoglobin Bristol or β67(E11) Val→Asp in Japan

Ohba, Yusuke; Matsuoka, M; Miyaji, T; Shibuya, Tsunefumi; Sakuragawa, M

doi:10.3109/03630268508996986

Cited by 10 publications

(4 citation statements)

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“…According to this study and the previous analysis [ 1 - 3 , 6 , 7 , 8 ] that were carried out on the Hb Alesha-Bristol, it has been confirmed that this mutation is always caused as a result of a de novo mutation. It has also been reported in subjects of different origins, three from Japan, two from Russia, as well as one from each of German, Argentina, Brazil, China, and Britain, suggesting that this mutation is not dependent on especial origins [ 7 , 9 ] .…”

Section: Discussionsupporting

confidence: 73%

“…Unstable Hb Alesha is caused by a G>A mutation at codon 67 of β-globin gene [β67(E11)Val>Met, G TG> A TG], changing valine (Val) to methionine (Met) amino acids [ 1 - 3 ] . This unstable Hb variant was first named Hb Bristol and reported in a 15-year-old Russian boy with severe hemolytic anemia and also in a British patient in which structural study showed that Val was replaced to aspartate (Asp) at codon 67 [ 4 ] .…”

Section: Introductionmentioning

confidence: 99%

“…A complementary experiment using both protein and DNA sequencing of the British patient showed that the primary reported mutation of Hb Bristol known as βV67D that was performed by using protein study was not a correct one; the correct mutation of Hb Bristol was identical to Hb Alesha mutation (β 67[E11] Val to Met). This difference is due to a posttranslational mechanism in which the translated Met converts into an Asp residue [ 3 ] . The Met to Asp residue modification is probably done through an oxidative reaction due to the vicinity of the Met side chain to heme iron and the bound O 2 .…”

Section: Introductionmentioning

confidence: 99%

“…This alteration can consequently cause an unstable production of Hb molecule and a severe hemolysis [ 1 ]. Therefore, both Hb Bristol and Alesha have the same entity, and the disease is called Hb Bristol-Alesha [ 3 ] . In this investigation, for the first time, we pointed out a mutation called Hb Alesha in a six-year-old Iranian boy who suffered from a severe hemolytic anemia and required frequent blood transfusions with mild hepatosplenomegaly.…”

Section: Introductionmentioning

confidence: 99%

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A First Report of Hb Alesha [β67(E11)Val>Met, GTG>ATG] in an Iranian Patient

Hamid

Nezhad

Galehdari

et al. 2019

ibj

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Background:Hemoglobin (Hb) Alesha is a rare and very unstable Hb variant, resulting in disruption of the heme pocket and producing severe hemolysis in heterozygous statues. In this study, we describe the first report of this variant in an Iranian boy originated from south of Iran with severe hemolytic anemia and mild splenomegaly. Methods:A six-year-old boy from Khuzestan Province and his parents were studied. Gap-PCR and direct sequencing were performed to detect the -globin gene deletions and β-globin gene mutations, respectively. Results:The subject had a sporadic mutation GTG to ATG (Val [valine]>Met [methionine]) at codon 67 in heterozygous form on β-globin gene, which was not detected in his parents. Conclusion:Since both parents proved to be normal, this Hb variant could be considered as a de novo mutation, which is highly useful for prenatal diagnosis.

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Section: Discussionsupporting

confidence: 73%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

A First Report of Hb Alesha [β67(E11)Val>Met, GTG>ATG] in an Iranian Patient

Hamid

Nezhad

Galehdari

et al. 2019

ibj

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A Hemoglobin Variant Associated with Neonatal Cyanosis and Anemia

Crowley¹,

Mollan²,

Abdulmalik³

et al. 2011

N Engl J Med

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SUMMARY Globin-gene mutations are a rare but important cause of cyanosis. We identified a missense mutation in the fetal G γ-globin gene (HBG2) in a father and daughter with transient neonatal cyanosis and anemia. This new mutation modifies the ligand-binding pocket of fetal hemoglobin by means of two mechanisms. First, the relatively large side chain of methionine decreases both the affinity of oxygen for binding to the mutant hemoglobin subunit and the rate at which it does so. Second, the mutant methionine is converted to aspartic acid post-translationally, probably through oxidative mechanisms. The presence of this polar amino acid in the heme pocket is predicted to enhance hemoglobin denaturation, causing anemia.

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