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In sickle cell disease, there was a significant increase in incubated Heinz body formation (p &lt; .001), a decrease in reduced glutathione concentration (p &lt; .01), an increase in glucose\u20106\u2010phosphate dehydrogenase activity (p &lt; .01), and a decrease in glutathione reductase activity (p &lt; .005). The patients with sickle cell disease had an absolute increase in the activity of the pentose shunt in the intact red cell after methylene blue stimulation (p &lt; .05) and in red cell hemolysates (p &lt; .025). Heinz body formation (r = .75) and pentose shunt activity in red cell hemolysates (r = .83) were strongly related to the degree of reticulocytosis. Although there was a correlation between the pentose shunt activity in the stimulated red cell and in red cell hemolysates for the patients with hemolytic anemia (r = .58), stimulated shunt activity did not increase as the hemolysate shunt activity increased for the patients with sickle cell disease. There were very strong relationships between the ATP concentration and the reticulocyte count (r = .80) and the hemolysate pentose shunt activity (r = .77) in sickle cell disease. These data suggest that in spite of an absolute increase in stimulated pentose shunt activity, there is a relative suppression of stimulated shunt activity in the youngest sickle erythrocytes. This may be related, in part, to the inhibitory effects of high concentrations of ATP on the activity of glucose\u20106\u2010phosphate dehydrogenase.<\/jats:p>","DOI":"10.1002\/ajh.2830150102","type":"journal-article","created":{"date-parts":[[2007,2,21]],"date-time":"2007-02-21T09:51:24Z","timestamp":1172051484000},"page":"1-13","source":"Crossref","is-referenced-by-count":55,"title":["Impaired pentose phosphate shunt function in sickle cell disease: A potential mechanism for increased heinz body formation and membrane lipid peroxidation"],"prefix":"10.1002","volume":"15","author":[{"given":"Neil A.","family":"Lachant","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Warren D.","family":"Davidson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kouichi R.","family":"Tanaka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2006,7,11]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"crossref","first-page":"624","DOI":"10.1001\/archinte.1974.00320160118010","article-title":"Hemolysis in sickle cell disease","volume":"133","author":"Bensinger TA","year":"1974","journal-title":"Arch Int Med"},{"key":"e_1_2_1_3_2","first-page":"849","volume-title":"Clinical Hematology","author":"Wintrobe MM","year":"1981"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2141.1969.tb01403.x"},{"key":"e_1_2_1_5_2","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1182\/blood.V41.5.653.653","article-title":"The sickle\u2010unsickle cycle: A cause of cell fragmentation and deformation","volume":"41","author":"Padilla F","year":"1973","journal-title":"Blood"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM197810122991504"},{"key":"e_1_2_1_7_2","doi-asserted-by":"publisher","DOI":"10.1182\/blood.V58.6.1057.1057"},{"key":"e_1_2_1_8_2","first-page":"174","volume-title":"Sickle Cell Disease, Diagnosis, Management, Education, and Research","author":"Abramson N","year":"1973"},{"key":"e_1_2_1_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0002-9343(80)80008-8"},{"key":"e_1_2_1_10_2","first-page":"1067","article-title":"Red cell membrane peroxidation and superoxide dismutase (EC.1.15.1.1) in sickle cell anemia","volume":"36","author":"Nair CR","year":"1977","journal-title":"Fed Proc"},{"key":"e_1_2_1_11_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2141.1979.tb05851.x"},{"key":"e_1_2_1_12_2","first-page":"1076","article-title":"Lipid membrane peroxidation, vitamin E, and the generation of irreversible sickled cells in sickle cells in sickle cell anemia","volume":"25","author":"Bowie J","year":"1979","journal-title":"Clin Chem"},{"key":"e_1_2_1_13_2","first-page":"721A","article-title":"Sickle cell oxidant damage and its treatment","volume":"29","author":"Wetterstroem N","year":"1981","journal-title":"Clin Res"},{"key":"e_1_2_1_14_2","first-page":"519A","article-title":"A novel phospholipid in irreversible sickled erythrocytes: Evidence for a possible role of in vivo peroxidation for membrane damage","volume":"29","author":"Jain SK","year":"1981","journal-title":"Clin Res"},{"key":"e_1_2_1_15_2","first-page":"183","article-title":"Association of lipid peroxidation and polymerization of membrane proteins with erythrocyte aging","volume":"40","author":"Hochstein P","year":"1981","journal-title":"Fed Proc"},{"key":"e_1_2_1_16_2","first-page":"542","article-title":"Abnormal vitamin E and glutathione peroxidase levels in sickle cell anemia","volume":"94","author":"Chiu D","year":"1979","journal-title":"J Lab Clin Med"},{"key":"e_1_2_1_17_2","first-page":"328","article-title":"The removal of leukocytes and platelets from whole blood","volume":"88","author":"Beutler E","year":"1976","journal-title":"J Lab Clin Med"},{"key":"e_1_2_1_18_2","first-page":"81","article-title":"Erythrocyte enzymes in groups of Rattus norvegicus with genetic differences in 2,3\u2010diphosphoglycerate levels","volume":"62","author":"Noble NA","year":"1979","journal-title":"Comp Biochem Physiol"},{"key":"e_1_2_1_19_2","first-page":"40","article-title":"The hemolytic effect of primaquine. 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