معلومه

s,r hbsil

Stadhouders R, Aktuna S, Thongjuea S, Aghajanirefah A, Pourfarzad F, van Ijcken W, Lenhard B, Rooks H, Best S, Menzel S, Grosveld F, Thein.

Sickle cell disease (SCD) was the first human monogenic disorder to be characterized at the molecular level (1).

It results from the substitution of glutamic acid by valine at position 6 of the β-chain of hemoglobin.

The clinical manifestations of SCD arise from the tendency of sickle hemoglobin (known as Hb S or α) to polymerize at reduced oxygen tensions and deform red cells into the characteristic rigid sickle cell shape.

Such inflexible red cells cannot pass through the microcirculation efficiently, and this results in anemia (due to destruction of the red cells) and intermittent vasoocclusion causing tissue damage and pain (2).

Although all patients with homozygous SCD have exactly the same molecular defect, there is considerable clinical variation, ranging from death in early childhood (3) to a normal life span with few complications (4).

Genetic modifiers of SCD include α-thalassemia (5), and it has been known for many years that patients with increased levels of fetal Hb (Hb F or α2γ2) often tend to have a relatively mild clinical course (2) because Hb F reduces the tendency of Hb S to polymerise within the red cell.

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The difference in the r2 is the result of the presence of the ancestral sequence. QTL modulates HbF production primarily through MYB, HBSIL, both, or neither.

Sickle cell disease (SCD) was the first human monogenic disorder to be characterized at the molecular level (1).

It results from the substitution of glutamic acid by valine at position 6 of the β-chain of hemoglobin.

The clinical manifestations of SCD arise from the tendency of sickle hemoglobin (known as Hb S or α) to polymerize at reduced oxygen tensions and deform red cells into the characteristic rigid sickle cell shape.

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