Hemoglobin setif and in vitro pseudosickling noted in a family with co-existent α and β thalassemia

Raik, Eva; Powell, E.; Fleming, P. J.; Gordon, Susan

doi:10.3109/00313028309085174

Cited by 10 publications

(3 citation statements)

References 6 publications

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“…Incubation of hemoglobin Setif-containing cells in high salt accelerates hemoglobin aggregation, the loss of deformability and cell sickling due to cell dehydration (increase in MCHC), and the further decrease of hemoglobin solubility. The proportion of hemoglobin A in the individual with co-existence of a-thalassemia and heterozygous hemoglobin Setif (40% of the mutant hemoglobin) [5] is comparable to hemoglobin A levels in erythrocytes from individuals with sickle trait (AS). AS erythrocytes can sickle when fully deoxygenated in vitro and the hemoglobin cell lysate can be made to aggregate.…”

Section: Discussionmentioning

confidence: 99%

“…Blood was obtained from individuals heterozygous for hemoglobin Setif including one individual who was a compound heterozygote for Setif/a-thalassemia [2,5]. Samples were collected in Sydney in ACD anticoagulant solution and air freighted on ice.…”

Section: Methodsmentioning

confidence: 99%

“…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.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%