Hb Setif: G1 (94)α Asp → Tyr a new α chain hemoglobin variant with substitution of the residue involved in a hydrogen bond between unlike subunits

Wajcman, Henri; Belkhodja, O; Labie, Dominique

doi:10.1016/0014-5793(72)80645-8

Cited by 53 publications

(5 citation statements)

References 12 publications

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“…This miscegenation is reflected in the great variety of unusual hemoglobins identified in the cases referred to our laboratory: Hb Stanleyville II, Hb Douala and Hb Chelsea are from the African continent 2,23,24 ; Hb Jackson is found in Black Americans from Southwestern United States 25 ; Hb Westmead, Hb Kurosaki, Hb Ube-2, Hb Iwata and Hb Tamano are of Asian origin 2,26–29 ; Hb Hasharon, Hb Shaare Zedek, Hb Daneshgah-Tehran and Hb Setif are from the Middle East 2,30–32 ; Hb J-Paris, Hb I-Interlaken, Hb J-Rovigo, Hb Pontoise, Hb Cemenelum, Hb G-Norfolk and Hb Sunshine Seth are found in European populations 33–39 ; and Hb Icaria and Hb G-Pest are from Eastern Europe. 40,41 In this respect, different alpha-globin variants have been found in other Brazilian regions, such as in the state of Minas Gerais, where Hb Etobicoke, Hb Ottawa and Hb St. Luke's were detected for the first time in Brazil.…”

Section: Discussionmentioning

confidence: 93%

Investigating alpha-globin structural variants: a retrospective review of 135,000 Brazilian individuals

Kimura

Oliveira

Jorge

et al. 2015

Revista Brasileira de Hematologia e Hemoterapia

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BackgroundBrazil has a multiethnic population with a high diversity of hemoglobinopathies. While screenings for beta-globin mutations are far more common, alterations affecting alpha-globin genes are usually more silent and less well known. The aim of this study was to describe the results of a screening program for alpha-globin gene mutations in a representative sample of the Southeastern Brazilian population.MethodsA total of 135,000 individuals, including patients with clinical suspicion of hemoglobinopathies and their family members, randomly chosen individuals submitted to blood tests and blood donors who were abnormal hemoglobin carriers were analyzed. The variants were screened by alkaline and acid electrophoreses, isoelectric focusing and cation-exchange high performance liquid chromatography (HPLC) and the abnormal chains were investigated by reverse-phase high performance liquid chromatography (RP-HPLC). Mutations were identified by molecular analyses, and the oxygen affinity, heme–heme cooperativity and Bohr effect of the variants were evaluated by functional tests.ResultsFour new and 22 rare variants were detected in 98 families. Some of these variants were found in co-inheritance with other hemoglobinopathies. Of the rare hemoglobins, Hasharon, Stanleyville II and J-Rovigo were the most common, the first two being S-like and associated with alpha-thalassemia.ConclusionThe variability of alpha-globin alterations reflects the high degree of racial miscegenation and an intense internal migratory flow between different Brazilian regions. This diversity highlights the importance of programs for diagnosing hemoglobinopathies and preventing combinations that may lead to important clinical manifestations in multiethnic populations.

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Section: Discussionmentioning

confidence: 93%

Investigating alpha-globin structural variants: a retrospective review of 135,000 Brazilian individuals

Kimura

Oliveira

Jorge

et al. 2015

Revista Brasileira de Hematologia e Hemoterapia

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“…Abnormal haemoglobin-Hb Setif has been shown to cause psuedosickling in vitro when RBCs containing Hb Setif are incubated in normal saline or iodine containing buffer. Hb Setif was first described by Wajcman et al [4] in an Algerian family, and since then many cases have been reported in Iran [5] and Australia. Hb Setif containing RBCs show pseudosickling in vitro due to intracellular crystallisation of insoluble Hb [a94(G1)Asp ?…”

Section: Case Reportsmentioning

confidence: 94%

Pseudo-Sickle Anemia: Two Case Reports

Nangia

Sharma

Sethi

et al. 2014

Indian J Hematol Blood Transfus

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“…Abnormal hemoglobin Setif (a94 Asp -+ Tyr) was first reported in an Algerian family [3] followed by reports of several cases in Iran [4], in a Turkish Cypriot family in Australia [5], and in Saudi Arabia [6]. Erythrocytes from individuals heterozygous for hemoglobin Setif contain about 15% of the mutant hemoglobin, probably due to its reduced stability [3] and to the fact that it is an a-chain variant. Sickling has not been found in vivo and no change in erythrocyte oxygen affinity or clinical manifestations has been associated with heterozygous hemoglobin Setif [7] even when the percentage of hemoglobin Setif was as high as 40% (observed in an individual with coinherited thalassemia) 0 1991 Wiley-Liss, Inc.…”

Section: Introductionmentioning

confidence: 97%

Hemoglobin aggregation and pseudosickling in vitro of hemoglobin setif‐containing erythrocytes

et al. 1991

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Erythrocytes from individuals heterozygous for hemoglobin Setif (alpha 94 Asp----Tyr) sickle in vitro without deoxygenation when incubated in chloride buffer due to hemoglobin aggregation. We now report quantitative studies of hemoglobin polymerization and deformability in these cells. Hemoglobin polymer gradually increased in intact cells during a 24 h incubation period at 24 degrees C. After 24 hr, about 80% of the cells in 290 mOsm sodium chloride buffer contained polymer which appeared as short rods compared to greater than 99% containing polymer at 450 mOsm. Similar proportions of cells were morphologically sickled. Deformability of erythrocytes with 40% hemoglobin Setif incubated in 290 mOsm buffer at 37 degrees C decreased to 80% of normal by 210 min but in 450 mOsm decreased to 50% after only 30 min as measured by the ektacytometer. However, at 4 degrees C deformability remained normal even in 450 mOsm buffer. The solubility of gelled hemolysate containing 40% hemoglobin Setif was 24 g/dl and 21 g/dl at 290 and 459 mOsm buffer respectively. The gel persisted at 4 degrees C with a solubility of 26 g/dl, but melted when dialyzed into sodium phosphate or potassium phosphate buffer. These data suggest that hemoglobin polymerization, reduced deformability, and sickling of hemoglobin Setif-containing erythrocytes are related to reduced hemoglobin solubility. The rate and extent of intracellular polymerization in vitro are considerably reduced (as in the case of sickle trait) compared with erythrocytes from individuals with sickle cell anemia. Hence, the slower kinetics of hemoglobin aggregation in hemoglobin Setif-containing cells provide an alternate system for studying hemoglobin polymerization and abnormal rheology.

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Hb Setif: G1 (94)α Asp → Tyr a new α chain hemoglobin variant with substitution of the residue involved in a hydrogen bond between unlike subunits

Cited by 53 publications

References 12 publications

Investigating alpha-globin structural variants: a retrospective review of 135,000 Brazilian individuals

Investigating alpha-globin structural variants: a retrospective review of 135,000 Brazilian individuals

Pseudo-Sickle Anemia: Two Case Reports

Hemoglobin aggregation and pseudosickling in vitro of hemoglobin setif‐containing erythrocytes

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