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Sickle cell anemia

Griffin P. Rodgers, Constance T. Noguchi, Alan N. Schechter
From: Science & Medicine: Volume 1 Number 4: Page 48 (October 1994)

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Abstract: Substitution of an amino acid at one position on the beta chain makes sickle hemoglobin less soluble than normal hemoglobin by providing an intermolecular contact that permits polymerization upon deoxygenation. Genetic and biophysical achievements have been only slowly followed by effective therapy, in part because there is no good animal model for sickle cell disease. Recent clinical trials have been designed to derepress the beta-like globin gene gamma that makes fetal hemoglobin and thus to decrease the amount of hemoglobin that polymerizes. This appears to ameliorate the hemolytic anemia and painful vaso-occlusive crises of sickle cell anemia and may offer longer-term survival to afflicted patients.

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