Effects of a Single Sickling Event on the Mechanical Fragility of Sickle Cell Trait Erythrocytes

REFERENCES

• Ingram VM. A specific chemical difference between the globins of normal human and sickle cell anaemia haemoglobin. Nature. 1956;178(4537):792–794.
   PubMed Web of Science ®Google Scholar
• Murayama M. Molecular mechanism of red cell “sickling.” Science. 1966;153(732):145–149.
   PubMed Web of Science ®Google Scholar
• Gulley ML, Ross DW, Feo C, Orringer EP. The effect of cell hydration on the deformability of normal and sickle erythrocytes. Am J Hematol. 1982;13(4):283–291.
   PubMed Web of Science ®Google Scholar
• MacCallum RN, Lynch EC, Hellums JD, Alfrey Jr, CP. Fragility of abnormal erythrocytes evaluated by response to shear stress. J Lab Clin Med. 1975;85(1):67–74.
   PubMed Web of Science ®Google Scholar
• Nevaril CG, Lynch EC, Alfrey Jr, CP, Hellums JD. Erythrocyte damage and destruction induced by shearing stress. J Lab Clin Med. 1968;71(5):784–790.
   PubMed Web of Science ®Google Scholar
• Padilla F, Bromberg PA, Jensen WN. The sickle-unsickle cycle: a cause of cell fragmentation leading to permanently deformed cells. Blood. 1973;41(5):653–660.
   PubMed Web of Science ®Google Scholar
• Mohandas N, Hebbel RP. Erythrocyte deformability, fragility, and rheology. In: Embury SH, Hebbel RP, Mohandas N, Steinberg MH, Eds. Sickle Cell Disease. New York: Raven Press. 1994:205–216.
   Google Scholar
• Eaton WA, Hofrichter J. Sickle cell hemoglobin polymerization. Adv Protein Chem. 1990;40:63–279.
   PubMedGoogle Scholar
• Noguchi CT, Schechter AN. Sickle hemoglobin polymerization in solution and in cells. Annu Rev Biophys Biol. 1985;14(1):239–263.
   PubMedGoogle Scholar
• Shen SC, Castle WB, Fleming EM. Experimental and clinical observations of increased mechanical fragility of erythrocytes. Science. 1944;100(2600):387–389.
   PubMedGoogle Scholar
• Bensinger TA, Washington DC, Gillette MD. Hemolysis in sickle cell disease. Arch Intern Med. 1974;133(4):624–631.
   PubMedGoogle Scholar
• Rother RP, Bell L, Hillmen P, Gladwin MT. The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin—A novel mechanism of human disease. JAMA. 2005;293(13):1653–1662.
   PubMed Web of Science ®Google Scholar
• Schechter AN, Gladwin MT. Hemoglobin and the paracrine and endocrine functions of nitric oxide. N Engl J Med. 2003;348(15):1483–1485.
   PubMed Web of Science ®Google Scholar
• Reiter CD, Wang XD, Tanus-Santos JE, Cell-free hemoglobin limits nitric oxide bioavailability in sickle-cell disease. Nat Med. 2002;8(12):1383–1389.
   PubMed Web of Science ®Google Scholar
• Reiter CD, Gladwin MT. An emerging role for nitric oxide in sickle cell disease vascular homeostasis and therapy. Curr Opin Hematol. 2003;10(2):99–107.
   PubMed Web of Science ®Google Scholar
• Aslan M, Ryan TM, Adler B, Oxygen radical inhibition of nitric oxide-dependent vascular function in sickle cell disease. Proc Natl Acad Sci USA. 2001;98(26):15215–15220.
   PubMed Web of Science ®Google Scholar
• Minneci PC, Deans KJ, Zhi H, Hemolysis-associated endothelial dysfunction mediated by accelerated NO inactivation by decompartmentalized oxyhemoglobin. J Clin Invest. 2005;115(12):3409–3417.
   PubMed Web of Science ®Google Scholar
• Morris CR, Morris SM, Hagar W, Arginine therapy —A new treatment for pulmonary hypertension in sickle cell disease? Am J Resp Crit Care. 2003;168(1):63–69.
   PubMed Web of Science ®Google Scholar
• Morris CR, Vichinsky EP, Kato GJ, Gladwin MT, Hazen S, Morris SM. Arginine metabolism, pulmonary hypertension, and sickle cell disease—In reply. JAMA. 2005;294(19):2433–2434.
   PubMed Web of Science ®Google Scholar
• Gladwin MT, Sachdev V, Jison ML, Pulmonary hypertension as a risk factor for death in patients with sickle cell disease. N Engl J Med. 2004;350(9):886–895.
   PubMed Web of Science ®Google Scholar
• Nolan VG, Wyszynski DF, Farrer LA, Steinberg MH. Hemolysis-associated priapism in sickle cell disease. Blood 2005;106(9):3264–3267.
   PubMed Web of Science ®Google Scholar
• Alayash AI, Patel RP, Cashon RE. Redox reactions of hemoglobin and myoglobin: Biological and toxicological implications. Antioxid Redox Sign. 2001;3(2):313–327.
   PubMed Web of Science ®Google Scholar
• Alayash AI. Oxygen therapeutics: can we tame haemoglobin? Nat Rev Drug Discov. 2004;3(2):152–159.
   PubMed Web of Science ®Google Scholar
• Balla J, Jacob HS, Balla G, Nath K, Eaton JW, Vercellotti GM. Endothelial-cell heme uptake from heme-proteins—induction of sensitization and desensitization to oxidant damage. Proc Natl Acad Sci USA. 1993;90(20):9285–9289.
   PubMed Web of Science ®Google Scholar
• Jeney V, Balla J, Yachie A, Pro-oxidant and cytotoxic effects of circulating heme. Blood. 2002;100(3):879–887.
   PubMed Web of Science ®Google Scholar
• Porto BN, Alves LS, Fernandez PL, Heme induces neutrophil migration and reactive oxygen species generation through signaling pathways characteristic of chemotactic receptors. J Biol Chem. 2007;282(33):24430–24436.
   PubMed Web of Science ®Google Scholar
• Frei AC, Guo Y, Jones DW, Vascular dysfunction in a murine model of severe hemolysis. Blood. 2008;112(2):398–405.
   PubMed Web of Science ®Google Scholar
• Liu SC, Zhai S, Palek J. Detection of hemin release during Hemoglobin-S denaturation. Blood. 1988;71(6):1755–1758.
   PubMed Web of Science ®Google Scholar
• Crosby WH. The metabolism of hemoglobin and bile pigment in hemolytic disease. Am J Med. 1955;18(1):112–122.
   PubMed Web of Science ®Google Scholar
• Kato GJ, Gladwin MT. Mechanisms and clinical complications of hemolysis in sickle cell disease and thalassemia. In: Steinberg MH, Forget BG, Higgs DR, Nagel RL, Eds. Disorders of Hemoglobin Genetics, Pathophysiology, and Clinical Management. New York: Cambridge University Press; 2009:201–224.
   Google Scholar
• Eaton JW, Jacob HS, White JG. Membrane abnormalities of irreversibly sickled cells. Semin Hematol. 1979;16(1):52–64.
   PubMed Web of Science ®Google Scholar
• Kaul DK, Fabry ME, Nagel RL. Vasooclusion by sickle cells—evidence for selective trapping of dense red-cells. Blood. 1986;68(5):1162–1166.
   PubMed Web of Science ®Google Scholar
• McCurdy PR, Sherman AS. Irreversibly sickled cells and red-cell survival in sickle-cell anemia - study with both DF32P and CR-51. Am J Med. 1978;64(2):253–258.
   PubMed Web of Science ®Google Scholar
• Noguchi CT, Schechter AN. The intracellular polymerization of sickle hemoglobin and its relevance to sickle-cell disease. Blood. 1981;58(6):1057–1068.
   PubMed Web of Science ®Google Scholar
• Rodgers G, Noguchi CT, Schechter AN. Irreversibly sickled erythrocytes in sickle cell anemia: a quantitative reappraisal. Am J Hematol. 1985;20(1):17–23.
   PubMed Web of Science ®Google Scholar
• Goodman SR. The irreversibly sickled cell: a perspective. Cell Mol Biol. 2004;50(1):53–58.
   PubMed Web of Science ®Google Scholar
• Hebbel RP, Eaton JW, Balasingam M, Steinberg MH. Spontaneous oxygen radical generation by sickle erythrocytes. J Clin Invest. 1982;70(6):1253–1259.
   PubMed Web of Science ®Google Scholar
• Hsu LL, Champion HC, Campbell-Lee SA, Hemolysis in sickle cell mice causes pulmonary hypertension due to global impairment in nitric oxide bioavailability. Blood. 2007;109(7):3088–3098.
   PubMed Web of Science ®Google Scholar
• Wood KC, Hebbel RP, Lefer DJ, Granger DN. Critical role of endothelial cell-derived nitric oxide synthase in sickle cell disease-induced microvascular dysfunction. Free Radic Biol Med. 2006;40(8):1443–1453.
   PubMed Web of Science ®Google Scholar
• Hebbel RP. Beyond hemoglobin polymerization—the red-blood cell membrane and sickle disease pathophysiology. Blood. 1991;77(2):214–237.
   PubMed Web of Science ®Google Scholar
• Hebbel RP, Miller WJ. Phagocytosis of sickle erythrocytes - immunological and oxidative determinants of hemolytic-anemia. Blood. 1984;64(3):733–741.
   PubMed Web of Science ®Google Scholar
• Das SK, Nair RC. Superoxide-dismutase, glutathione-peroxidase, catalase and lipid-peroxidation of normal and sickled erythrocytes. Br J Haematol. 1980;44(1):87–92.
   PubMed Web of Science ®Google Scholar
• Jain SK, Shohet SB. A novel phospholipid in irrevresibly sickled cells - evidence for in vivo peroxidative membrane damage in sickle-cell disease. Blood. 1984;63(2):362–367.
   PubMed Web of Science ®Google Scholar
• Platt OS, Falcone JF, Lux SE. Molecular defects in the sickle erythrocyte skeleton—abnormal spectrin binding to sickle inside-out vesicles. J Clin Invest. 1985;75(1):266–271.
   PubMed Web of Science ®Google Scholar
• Rank BH, Carlsson J, Hebbel RP. Abnormal redox status of membrane-protein thiols in sickle erythrocytes. J Clin Invest. 1985;75(5):1531–1537.
   PubMed Web of Science ®Google Scholar
• Schwartz RS, Rybicki AC, Heath RH, Lubin BH. Protein 4.1 in sickle erythrocytes—evidence for oxidative damage. J Biol Chem. 1987;262(32):15666–15672.
   PubMed Web of Science ®Google Scholar
• Shalev O, Hebbel RP. Catalysis of soluble hemoglobin oxidation by free iron on sickle red cell membranes. Blood. 1996;87(9):3948–3952.
   PubMed Web of Science ®Google Scholar
• Riceevans C, Omorphos SC, Baysal E. Sickle-cell membranes and oxidative damage. Biochem J. 1986;237(1):265–269.
   PubMed Web of Science ®Google Scholar
• Kuypers FA, Scott MD, Schott MA, Lubin B, Chiu DTY. Use of ektacytometry to determine red-cell susceptibility to oxidative stress. J Lab Clin Med. 1990;116(4):535–545.
   PubMed Web of Science ®Google Scholar
• Goldbloom RB, Fischer E, Reinhold J, Hsia DY. Studies on the mechanical fragility of erythrocytes: I. Normal values for infants and children. Blood. 1953;8(2):165–169.
   PubMed Web of Science ®Google Scholar
• Claster S, Vichinsky EP. Managing sickle cell disease. BMJ. 2003;327(7424):1151–1155.
   PubMed Web of Science ®Google Scholar
• Stroncek DF, Rainer T, Sharon V, Sickle Hb polymerization in RBC components from donors with sickle cell trait prevents effective WBC reduction by filtration. Transfusion. 2002;42(11):1466–1472.
   PubMed Web of Science ®Google Scholar
• Gupta AK, Kirchner KA, Nicholson R, Effects of α-thalassemia and sickle polymerization tendency on the urine-concentrating defect of individuals with sickle-cell trait. J Clin Invest. 1991;88(6):1963–1968.
   PubMed Web of Science ®Google Scholar
• Gupta AK, Kirchner KA, Nicholson R, Hyposthenuria in sickle-cell trait (Hb AS) correlates with percent Hemoglobin S (Hb S). Clin Res. 1990;38(4):A985–A985.
   Google Scholar
• Helzlsouer KJ, Hayden FG, Rogol AD. Severe metabolic complications in a cross-country runner with sickle-cell trait. JAMA. 1983;249(6):777–779.
   PubMed Web of Science ®Google Scholar
• Noguchi CT, Torchia DA, Schechter AN. Polymerization of hemoglobin in sickle trait erythrocytes and lysates. J Biol Chem. 1981;256(9):4168–4171.
   PubMed Web of Science ®Google Scholar
• Hedayati B, Anson K, Patel U. Focal renal infarction: an unusual cause of haematuria in a patient with sickle cell trait. Br J Radiol. 2007;80(953):e105–106.
   Google Scholar
• Antonini E, Brunori M. Hemoglobin and Myoglobin in Their Reactions with Ligands. Amsterdam: North Holland Publishing Company. 1971.
   Google Scholar
• Huang Z, Hearne L, Irby CE, King SB, Ballas SK, Kim-Shapiro DB. Kinetics of increased deformability of deoxygenated sickle cells upon oxygenation. Biophys J. 2003;85(4):2374–2383.
   PubMed Web of Science ®Google Scholar
• Huang Z, Louderback JG, King SB, Ballas SK, Kim-Shapiro DB. In vitro exposure to hydroxyurea reduces sickle red blood cell deformability. Am J Hematol. 2001;67(3):151–156.
   PubMed Web of Science ®Google Scholar
• Groner W, Mohandas N, Bessis M. New optical technique for measuring erythrocyte deformability with the ektacytometer. Clin Chem. 1980;26(10):1435–1442.
   PubMed Web of Science ®Google Scholar
• Mohandas N, Clark MR, Jacobs MS, Shohet SB. Analysis of factors regulating erythrocyte deformability. J Clin Invest. 1980;66(3):563–573.
   PubMed Web of Science ®Google Scholar
• Schubothe H, Fok FP. The quantitative estimation of mechanical haemolysis for clinical application. Br J Haematol. 1960;6(1):350–354.
   PubMed Web of Science ®Google Scholar