Beutler E, 1994. G6PD deficiency. Blood 84: 3613–3636.
Beutler E, 1996. G6PD: population genetics and clinical manifestations. Blood Rev 10: 45–52.
Beutler E, 1959. The hemolytic effect of primaquine and related compounds: a review. Blood 14: 103–139.
Baird JK, Fryauff DJ, Basri H, Bangs MJ, Subianto B, Wiady I, Purnomo, Leksana B, Masbar S, Richie TL, Jones TR, Tjitra E, Wignall ES, Hoffman SL, 1995. Primaquine for prophylaxis against malaria among nonimmune transmigrants in Irian Jaya, Indonesia. Am J Trop Med Hyg 52: 479–484.
Baird JK, Fryauff DJ, Hoffman SL, 2003. Primaquine for prevention of malaria in travelers. Clin Infect Dis 37: 1659–1667.
Baird JK, Hoffman SL, 2004. Primaquine therapy for malaria. Clin Infect Dis 39: 1336–1345.
Baird JK, 1998. Primaquine as anti-relapse therapy for Plasmodium vivax. Trans R Soc Trop Med Hyg 92: 687.
Baird JK, Surjadjaja C, 2011. Consideration of ethics in primaquine therapy against malaria transmission. Trends Parasitol 27: 11–16.
World Health Organization, 2006. Guidelines for the Treatment of Malaria. Second edition. Geneva: World Health Organization, 52–58.
Beutler E, 1969. Drug-induced hemolytic anemia. Pharmacol Rev 21: 73–103.
Pretsch W, Charles DJ, Merkle S, 1988. X-linked glucose-6-phosphate dehydrogenase deficiency in Mus musculus. Biochem Genet 26: 89–103.
Spolarics Z, Condon MR, Siddiqi M, Machiedo GW, Deitch EA, 2004. Red blood cell dysfunction in septic glucose-6-phosphate dehydrogenase-deficient mice. Am J Physiol Heart Circ Physiol 286: H2118–H2126.
Wilmanski J, Siddiqi M, Deitch EA, Spolarics Z, 2005. Augmented IL-10 production and redox-dependent signaling pathways in glucose-6-phosphate dehydrogenase-deficient mouse peritoneal macrophages. J Leukoc Biol 78: 85–94.
Spolarics Z, Siddiqi M, Siegel JH, Garcia ZC, Stein DS, Ong H, Livingston DH, Denny T, Deitch EA, 2001. Increased incidence of sepsis and altered monocyte functions in severely injured type A- glucose-6-phosphate dehydrogenase-deficient African American trauma patients. Crit Care Med 29: 728–736.
Beutler E, Duparc S; G6PD Deficiency Working Group, 2007. Glucose-6-phosphate dehydrogenase deficiency and antimalarial drug development. Am J Trop Med Hyg 77: 779–789.
Vale N, Moreira R, Gomes P, 2009. Primaquine revisited six decades after its discovery. Eur J Med Chem 44: 937–953.
Johns JL, Shooshtari MP, Christopher MM, 2008. Development of a technique for quantification of reticulocytes and assessment of erythrocyte regenerative capacity in birds. Am J Vet Res 69: 1067–1072.
Nobes PR, Carter AB, 1990. Reticulocyte counting using flow cytometry. J Clin Pathol 43: 675–678.
Summerfield M, Tudhope GR, 1979. Spectrophotometric method applicable to in vitro studies of Heinz body formation in erythrocytes. Acta Haematol 61: 222–225.
Watanabe J, Grijalva V, Hama S, Barbour K, Berger F, Navab M, Fogelman A, Reddy S, 2009. Hemoglobin and its scavenger protein haptoglobin associate with ApoA-1-containing particles and influence the inflammatory properties and function of high density lipoprotein. J Biol Chem 284: 18292–18301.
Neifer S, Jung A, Bienzle U, 1991. Characterization of erythrocytic glucose-6-phosphate dehydrogenase in a mouse strain with reduced G6PD activity. Biomed Biochim Acta 50: 233–238.
Reagan-Shaw S, Nihal M, Ahmad N, 2007. Dose translation from animal to human studies revisited. FASEB J 22: 659–661.
Alving AS, Johnson CF, Tarlov AR, Brewer GJ, Kellrmeyer RW, Carson PE, 1960. Mitigation of the hemolytic effect of primaquine and enhancement of its action against exoerythrocytic forms of the Chesson strain of Plasmodium vivax by intermittent regimens of drug administration: a preliminary report. Bull World Health Organ 22: 621–631.
Charoenlarp R, Areekul S, Pholpothi T, Harinasuta T, 1973. The course of primaquine-induced hemolysis in G-6_PD deficient Thais. J Med Assoc Thail 56: 392–397.
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Anti-malarial 8-aminoquinolines drugs cause acute hemolytic anemia in individuals with glucose-6-phosphate dehydrogenase deficiency (G6PDD). Efforts to develop non-hemolytic 8-aminoquinolines have been severely limited caused by the lack of a predictive in vivo animal model of hemolytic potential that would allow screening of candidate compounds. This report describes a G6PDD mouse model with a phenotype closely resembling the G6PDD phenotype found in the African A-type G6PDD human. These G6PDD mice, given different doses of primaquine, which used as a reference hemolytic drug, display a full array of hemolytic anemia parameters, consistently and reproducibly. The hemolytic and therapeutic indexes were generated for evaluation of hemotoxicity of drugs. This model demonstrated a complete hemolytic toxicity response to another known hemolytic antimalarial drug, pamaquine, but no response to non-hemolytic drugs, chloroquine and mefloquine. These results suggest that this model is suitable for evaluation of selected 8-AQ type candidate antimalarial drugs for their hemolytic potential.
Financial support: This study was supported by the Military Infectious Diseases Research Program (MIDRP) Award #RQ0031_09_WR and the U.S. Army Medical Research & Materiel Command (USAMRMC) and the Telemedicine & Advanced Technology Research Center (TATRC), at Fort Detrick, MD, under award number: W81XWH-07-2-0095. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
Authors' addresses: Peng Zhang, Xiugong Gao, Hiroshi Ishida, Jack Amnuaysirikul, Peter J. Weina, Max Grogl, Michael T. O'Neil, Qigui Li, Diana Caridha, Colin Ohrt, Mark Hickman, Alan J. Magill, and Prabhati Ray, Walter Reed Army Institute of Research - Experimental Therapeutics, Silver Spring, MD, E-mails: peng.zhang@amedd.army.mil, Xiugong.Gao@fda.hhs.gov, hiroshi.ishida@amedd.army.mil, Jack.Amnuaysirikul@us.army.mil, peter.weina@us.army.mil, Max.Grogl@amedd.army.mil, michael.t.oneil@us.army.mil, Qigui.Li@us.army.mil, Diana.Caridha2@us.army.mil, Colin.Ohrt@amedd.army.mil, Mark.Hickman@amedd.army.mil, Alan.Magill@us.army.mil, alan.magill@gatesfoundation.org, and prabhati.ray@us.army.mil.
Beutler E, 1994. G6PD deficiency. Blood 84: 3613–3636.
Beutler E, 1996. G6PD: population genetics and clinical manifestations. Blood Rev 10: 45–52.
Beutler E, 1959. The hemolytic effect of primaquine and related compounds: a review. Blood 14: 103–139.
Baird JK, Fryauff DJ, Basri H, Bangs MJ, Subianto B, Wiady I, Purnomo, Leksana B, Masbar S, Richie TL, Jones TR, Tjitra E, Wignall ES, Hoffman SL, 1995. Primaquine for prophylaxis against malaria among nonimmune transmigrants in Irian Jaya, Indonesia. Am J Trop Med Hyg 52: 479–484.
Baird JK, Fryauff DJ, Hoffman SL, 2003. Primaquine for prevention of malaria in travelers. Clin Infect Dis 37: 1659–1667.
Baird JK, Hoffman SL, 2004. Primaquine therapy for malaria. Clin Infect Dis 39: 1336–1345.
Baird JK, 1998. Primaquine as anti-relapse therapy for Plasmodium vivax. Trans R Soc Trop Med Hyg 92: 687.
Baird JK, Surjadjaja C, 2011. Consideration of ethics in primaquine therapy against malaria transmission. Trends Parasitol 27: 11–16.
World Health Organization, 2006. Guidelines for the Treatment of Malaria. Second edition. Geneva: World Health Organization, 52–58.
Beutler E, 1969. Drug-induced hemolytic anemia. Pharmacol Rev 21: 73–103.
Pretsch W, Charles DJ, Merkle S, 1988. X-linked glucose-6-phosphate dehydrogenase deficiency in Mus musculus. Biochem Genet 26: 89–103.
Spolarics Z, Condon MR, Siddiqi M, Machiedo GW, Deitch EA, 2004. Red blood cell dysfunction in septic glucose-6-phosphate dehydrogenase-deficient mice. Am J Physiol Heart Circ Physiol 286: H2118–H2126.
Wilmanski J, Siddiqi M, Deitch EA, Spolarics Z, 2005. Augmented IL-10 production and redox-dependent signaling pathways in glucose-6-phosphate dehydrogenase-deficient mouse peritoneal macrophages. J Leukoc Biol 78: 85–94.
Spolarics Z, Siddiqi M, Siegel JH, Garcia ZC, Stein DS, Ong H, Livingston DH, Denny T, Deitch EA, 2001. Increased incidence of sepsis and altered monocyte functions in severely injured type A- glucose-6-phosphate dehydrogenase-deficient African American trauma patients. Crit Care Med 29: 728–736.
Beutler E, Duparc S; G6PD Deficiency Working Group, 2007. Glucose-6-phosphate dehydrogenase deficiency and antimalarial drug development. Am J Trop Med Hyg 77: 779–789.
Vale N, Moreira R, Gomes P, 2009. Primaquine revisited six decades after its discovery. Eur J Med Chem 44: 937–953.
Johns JL, Shooshtari MP, Christopher MM, 2008. Development of a technique for quantification of reticulocytes and assessment of erythrocyte regenerative capacity in birds. Am J Vet Res 69: 1067–1072.
Nobes PR, Carter AB, 1990. Reticulocyte counting using flow cytometry. J Clin Pathol 43: 675–678.
Summerfield M, Tudhope GR, 1979. Spectrophotometric method applicable to in vitro studies of Heinz body formation in erythrocytes. Acta Haematol 61: 222–225.
Watanabe J, Grijalva V, Hama S, Barbour K, Berger F, Navab M, Fogelman A, Reddy S, 2009. Hemoglobin and its scavenger protein haptoglobin associate with ApoA-1-containing particles and influence the inflammatory properties and function of high density lipoprotein. J Biol Chem 284: 18292–18301.
Neifer S, Jung A, Bienzle U, 1991. Characterization of erythrocytic glucose-6-phosphate dehydrogenase in a mouse strain with reduced G6PD activity. Biomed Biochim Acta 50: 233–238.
Reagan-Shaw S, Nihal M, Ahmad N, 2007. Dose translation from animal to human studies revisited. FASEB J 22: 659–661.
Alving AS, Johnson CF, Tarlov AR, Brewer GJ, Kellrmeyer RW, Carson PE, 1960. Mitigation of the hemolytic effect of primaquine and enhancement of its action against exoerythrocytic forms of the Chesson strain of Plasmodium vivax by intermittent regimens of drug administration: a preliminary report. Bull World Health Organ 22: 621–631.
Charoenlarp R, Areekul S, Pholpothi T, Harinasuta T, 1973. The course of primaquine-induced hemolysis in G-6_PD deficient Thais. J Med Assoc Thail 56: 392–397.
Past two years | Past Year | Past 30 Days | |
---|---|---|---|
Abstract Views | 1179 | 1037 | 226 |
Full Text Views | 366 | 16 | 4 |
PDF Downloads | 106 | 13 | 0 |