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Volumn 130, Issue 11, 2017, Pages 1347-1356

AG-348 enhances pyruvate kinase activity in red blood cells from patients with pyruvate kinase deficiency

(25)  Kung, Charles a   Hixon, Jeff a,c   Kosinski, Penelope A a   Cianchetta, Giovanni a   Histen, Gavin a   Chen, Yue a   Hill, Collin a,d   Gross, Stefan a   Si, Yaguang a   Johnson, Kendall a   Delabarre, Byron a,e   Luo, Zhiyong b   Gu, Zhiwei b   Yao, Gui b   Tang, Huachun b   Fang, Cheng b   Xu, Yingxia b   Lv, Xiaobing b   Biller, Scott a   Su, Shin San Michael a,f   more..


Author keywords

[No Author keywords available]

Indexed keywords

2,3 DIPHOSPHOGLYCERIC ACID; ADENOSINE TRIPHOSPHATE; AG 348; ENZYME ACTIVATOR; N (4 (4 (CYCLOPROPYLMETHYL)PIPERAZINE 1 CARBONYL)PHENYL)QUINAZOLINE 8 SULFONAMIDE; PYRUVATE KINASE; QUINOLONE DERIVATIVE; SULFONAMIDE; UNCLASSIFIED DRUG; AG-348; QUINOLINE DERIVATIVE; RECOMBINANT PROTEIN;

EID: 85029477346     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2016-11-753525     Document Type: Article
Times cited : (81)

References (39)
  • 1
    • 33645821325 scopus 로고
    • Apropos of 3 new types of hemolytic anemia in children. Infantile pyknocytosis. Familial hemolytic anemia with erythrocytic inclusions and pigmenturia. Anemia caused by pyruvate-kinase deficiency
    • in French
    • Germain D. Apropos of 3 new types of hemolytic anemia in children. Infantile pyknocytosis. Familial hemolytic anemia with erythrocytic inclusions and pigmenturia. Anemia caused by pyruvate-kinase deficiency [in French]. Pediatrie. 1962;17: 323-326.
    • (1962) Pediatrie , vol.17 , pp. 323-326
    • Germain, D.1
  • 2
    • 0013366142 scopus 로고
    • Pyruvate kinase (PK) deficiency hereditary nonspherocytic hemolytic anemia
    • Tanaka KR, Valentine WN, Miwa S. Pyruvate kinase (PK) deficiency hereditary nonspherocytic hemolytic anemia. Blood. 1962;19(3):267-295.
    • (1962) Blood , vol.19 , Issue.3 , pp. 267-295
    • Tanaka, K.R.1    Valentine, W.N.2    Miwa, S.3
  • 3
    • 75549114155 scopus 로고
    • Erythrocyte pyruvate kinase deficiency resulting in congenital nonspherocytic hemolytic anemia
    • Oski FA, Diamond LK. Erythrocyte pyruvate kinase deficiency resulting in congenital nonspherocytic hemolytic anemia. N Engl J Med. 1963;269:763-770.
    • (1963) N Engl J Med. , vol.269 , pp. 763-770
    • Oski, F.A.1    Diamond, L.K.2
  • 4
    • 50549218894 scopus 로고
    • Haemolytic anaemia due to pyruvate-kinase deficiency
    • Brunetti P, Puxeddu A, Nenci G, Migliorini E. Haemolytic anaemia due to pyruvate-kinase deficiency. Lancet. 1963;282(7300):169-170.
    • (1963) Lancet , vol.282 , Issue.7300 , pp. 169-170
    • Brunetti, P.1    Puxeddu, A.2    Nenci, G.3    Migliorini, E.4
  • 5
    • 84939566700 scopus 로고    scopus 로고
    • Erythrocyte pyruvate kinase deficiency: 2015 status report
    • Grace RF, Zanella A, Neufeld EJ, et al. Erythrocyte pyruvate kinase deficiency: 2015 status report. Am J Hematol. 2015;90(9):825-830.
    • (2015) Am J Hematol , vol.90 , Issue.9 , pp. 825-830
    • Grace, R.F.1    Zanella, A.2    Neufeld, E.J.3
  • 6
    • 0034431029 scopus 로고    scopus 로고
    • Red cell pyruvate kinase deficiency: From genetics to clinical manifestations
    • Zanella A, Bianchi P. Red cell pyruvate kinase deficiency: from genetics to clinical manifestations. Best Pract Res Clin Haematol. 2000;13(1):57-81.
    • (2000) Best Pract Res Clin Haematol , vol.13 , Issue.1 , pp. 57-81
    • Zanella, A.1    Bianchi, P.2
  • 7
    • 84948094800 scopus 로고    scopus 로고
    • Pyruvate kinase: Function, regulation and role in cancer
    • Israelsen WJ, Vander Heiden MG. Pyruvate kinase: function, regulation and role in cancer. Semin Cell Dev Biol. 2015;43:43-51.
    • (2015) Semin Cell Dev Biol. , vol.43 , pp. 43-51
    • Israelsen, W.J.1    Vander Heiden, M.G.2
  • 8
    • 28844488320 scopus 로고    scopus 로고
    • The energy-less red blood cell is lost: Erythrocyte enzyme abnormalities of glycolysis
    • van Wijk R, van Solinge WW. The energy-less red blood cell is lost: erythrocyte enzyme abnormalities of glycolysis. Blood. 2005;106(13): 4034-4042.
    • (2005) Blood , vol.106 , Issue.13 , pp. 4034-4042
    • Van Wijk, R.1    Van Solinge, W.W.2
  • 9
    • 0032520197 scopus 로고    scopus 로고
    • The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate
    • Jurica MS, Mesecar A, Heath PJ, Shi W, Nowak T, Stoddard BL. The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate. Structure. 1998;6(2):195-210.
    • (1998) Structure , vol.6 , Issue.2 , pp. 195-210
    • Jurica, M.S.1    Mesecar, A.2    Heath, P.J.3    Shi, W.4    Nowak, T.5    Stoddard, B.L.6
  • 10
    • 0030978311 scopus 로고    scopus 로고
    • Molecular characterization of PK-LR gene in pyruvate kinase-deficient Italian patients
    • Zanella A, Bianchi P, Baronciani L, et al. Molecular characterization of PK-LR gene in pyruvate kinase-deficient Italian patients. Blood. 1997;89(10):3847-3852.
    • (1997) Blood , vol.89 , Issue.10 , pp. 3847-3852
    • Zanella, A.1    Bianchi, P.2    Baronciani, L.3
  • 11
    • 0035892103 scopus 로고    scopus 로고
    • Human erythrocyte pyruvate kinase: Characterization of the recombinant enzyme and a mutant form (R510Q) causing nonspherocytic hemolytic anemia
    • Wang C, Chiarelli LR, Bianchi P, et al. Human erythrocyte pyruvate kinase: characterization of the recombinant enzyme and a mutant form (R510Q) causing nonspherocytic hemolytic anemia. Blood. 2001;98(10):3113-3120.
    • (2001) Blood , vol.98 , Issue.10 , pp. 3113-3120
    • Wang, C.1    Chiarelli, L.R.2    Bianchi, P.3
  • 12
    • 22144484881 scopus 로고    scopus 로고
    • Red cell pyruvate kinase deficiency: Molecular and clinical aspects
    • Zanella A, Fermo E, Bianchi P, Valentini G. Red cell pyruvate kinase deficiency: molecular and clinical aspects. Br J Haematol. 2005;130(1): 11-25.
    • (2005) Br J Haematol , vol.130 , Issue.1 , pp. 11-25
    • Zanella, A.1    Fermo, E.2    Bianchi, P.3    Valentini, G.4
  • 13
    • 84949537443 scopus 로고    scopus 로고
    • Generation of a high number of healthy erythroid cells from gene-edited pyruvate kinase deficiency patient-specific induced pluripotent stem cells
    • Garate Z, Quintana-Bustamante O, Crane AM, et al. Generation of a high number of healthy erythroid cells from gene-edited pyruvate kinase deficiency patient-specific induced pluripotent stem cells. Stem Cell Rep. 2015;5(6):1053-1066.
    • (2015) Stem Cell Rep , vol.5 , Issue.6 , pp. 1053-1066
    • Garate, Z.1    Quintana-Bustamante, O.2    Crane, A.M.3
  • 14
    • 84982082493 scopus 로고    scopus 로고
    • Safe and efficient gene therapy for pyruvate kinase deficiency
    • Garcia-Gomez M, Calabria A, Garcia-Bravo M, et al. Safe and efficient gene therapy for pyruvate kinase deficiency. Mol Ther. 2016;24(7): 1187-1198.
    • (2016) Mol Ther , vol.24 , Issue.7 , pp. 1187-1198
    • Garcia-Gomez, M.1    Calabria, A.2    Garcia-Bravo, M.3
  • 15
    • 73849125332 scopus 로고    scopus 로고
    • Rescue of pyruvate kinase deficiency in mice by gene therapy using the human isoenzyme
    • Meza NW, Alonso-Ferrero ME, Navarro S, et al. Rescue of pyruvate kinase deficiency in mice by gene therapy using the human isoenzyme. Mol Ther. 2009;17(12):2000-2009.
    • (2009) Mol Ther , vol.17 , Issue.12 , pp. 2000-2009
    • Meza, N.W.1    Alonso-Ferrero, M.E.2    Navarro, S.3
  • 16
    • 0016668294 scopus 로고
    • Normalisation of red blood cell pyruvate kinase in pyruvate kinase deficiency by riboflavin treatment
    • Staal GE, van Berkel TJ, Nijessen JG, Koster JF. Normalisation of red blood cell pyruvate kinase in pyruvate kinase deficiency by riboflavin treatment. Clin Chim Acta. 1975;60(3):323-327.
    • (1975) Clin Chim Acta , vol.60 , Issue.3 , pp. 323-327
    • Staal, G.E.1    Van Berkel, T.J.2    Nijessen, J.G.3    Koster, J.F.4
  • 17
    • 0017124910 scopus 로고
    • Effect of riboflavin treatment on human red cell pyruvate kinase deficiency
    • Blume KG, Arnold H, Hasslinger K, Löhr GW. Effect of riboflavin treatment on human red cell pyruvate kinase deficiency. Clin Chim Acta. 1976; 71(2):331-334.
    • (1976) Clin Chim Acta , vol.71 , Issue.2 , pp. 331-334
    • Blume, K.G.1    Arnold, H.2    Hasslinger, K.3    Löhr, G.W.4
  • 18
    • 84960340828 scopus 로고    scopus 로고
    • ML265: A potent PKM2 activator induces tetramerization and reduces tumor formation and size in a mouse xenograft model
    • Bethesda, MD: National Center for Biotechnology Information; Accessed 24 November 2016
    • Walsh MJ, Brimacombe KR, Anastasiou D, et al. ML265: a potent PKM2 activator induces tetramerization and reduces tumor formation and size in a mouse xenograft model. In: Probe Reports from the NIH Molecular Libraries Program. Bethesda, MD: National Center for Biotechnology Information; 2010-2013. Available at: http://www.ncbi.nlm.nih.gov/books/NBK153222/. Accessed 24 November 2016.
    • (2010) Probe Reports from The NIH Molecular Libraries Program
    • Walsh, M.J.1    Brimacombe, K.R.2    Anastasiou, D.3
  • 19
    • 84866697915 scopus 로고    scopus 로고
    • Small molecule activation of PKM2 in cancer cells induces serine auxotrophy
    • Kung C, Hixon J, Choe S, et al. Small molecule activation of PKM2 in cancer cells induces serine auxotrophy. Chem Biol. 2012;19(9):1187-1198.
    • (2012) Chem Biol. , vol.19 , Issue.9 , pp. 1187-1198
    • Kung, C.1    Hixon, J.2    Choe, S.3
  • 20
    • 18544366712 scopus 로고    scopus 로고
    • Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia
    • Valentini G, Chiarelli LR, Fortin R, et al. Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia. J Biol Chem. 2002;277(26): 23807-23814.
    • (2002) J Biol Chem. , vol.277 , Issue.26 , pp. 23807-23814
    • Valentini, G.1    Chiarelli, L.R.2    Fortin, R.3
  • 21
    • 84959219073 scopus 로고    scopus 로고
    • Red blood cell PK deficiency: An update of PK-LR gene mutation database
    • Canu G, De Bonis M, Minucci A, Capoluongo E. Red blood cell PK deficiency: an update of PK-LR gene mutation database. Blood Cells Mol Dis. 2016;57:100-109.
    • (2016) Blood Cells Mol Dis. , vol.57 , pp. 100-109
    • Canu, G.1    De Bonis, M.2    Minucci, A.3    Capoluongo, E.4
  • 22
    • 0028569458 scopus 로고
    • Erythrocyte pyruvate kinase deficiency. The influence of physiologically important metabolites on the function of normal and defective enzymes
    • Lakomek M, Winkler H, Pekrun A, et al. Erythrocyte pyruvate kinase deficiency. The influence of physiologically important metabolites on the function of normal and defective enzymes. Enzyme Protein. 1994-1995;48(3):149-163.
    • (1994) Enzyme Protein. , vol.48 , Issue.3 , pp. 149-163
    • Lakomek, M.1    Winkler, H.2    Pekrun, A.3
  • 23
    • 0014573517 scopus 로고
    • A low Km phosphoenolpyruvate mutant in the Amish with red cell pyruvate kinase deficiency
    • Oski FA, Bowman H. A low Km phosphoenolpyruvate mutant in the Amish with red cell pyruvate kinase deficiency. Br J Haematol. 1969;17(3):289-297.
    • (1969) Br J Haematol , vol.17 , Issue.3 , pp. 289-297
    • Oski, F.A.1    Bowman, H.2
  • 25
    • 0020402181 scopus 로고
    • Aging of the erythrocyte. XIV. ATP content does decrease
    • Bartosz G, Grzelińska E, Wagner J. Aging of the erythrocyte. XIV. ATP content does decrease. Experientia. 1982;38(5):575.
    • (1982) Experientia , vol.38 , Issue.5 , pp. 575
    • Bartosz, G.1    Grzelińska, E.2    Wagner, J.3
  • 26
    • 0026536473 scopus 로고
    • PH, temperature and lactate production in human red blood cells: Implications for blood storage and glycolytic control
    • Guppy M, Attwood PV, Hansen IA, Sabaratnam R, Frisina J, Whisson ME. pH, temperature and lactate production in human red blood cells: implications for blood storage and glycolytic control. Vox Sang. 1992;62(2):70-75.
    • (1992) Vox Sang , vol.62 , Issue.2 , pp. 70-75
    • Guppy, M.1    Attwood, P.V.2    Hansen, I.A.3    Sabaratnam, R.4    Frisina, J.5    Whisson, M.E.6
  • 27
    • 0014410425 scopus 로고
    • Lifespan and organ sequestration of the red cells in pyruvate kinase deficiency
    • Nathan DG, Oski FA, Miller DR, Gardner FH. Lifespan and organ sequestration of the red cells in pyruvate kinase deficiency. N Engl J Med. 1968; 278(2):73-81.
    • (1968) N Engl J Med , vol.278 , Issue.2 , pp. 73-81
    • Nathan, D.G.1    Oski, F.A.2    Miller, D.R.3    Gardner, F.H.4
  • 29
    • 0017255183 scopus 로고
    • Salicylate-induced injury of pyruvate-kinase-deficient erythrocytes
    • Glader BE. Salicylate-induced injury of pyruvate-kinase-deficient erythrocytes. N Engl J Med. 1976;294(17):916-918.
    • (1976) N Engl J Med. , vol.294 , Issue.17 , pp. 916-918
    • Glader, B.E.1
  • 30
    • 0018564931 scopus 로고
    • Quinine protects pyruvate-kinase deficient red cells from dehydration
    • Koller CA, Orringer EP, Parker JC. Quinine protects pyruvate-kinase deficient red cells from dehydration. Am J Hematol. 1979;7(3):193-199.
    • (1979) Am J Hematol , vol.7 , Issue.3 , pp. 193-199
    • Koller, C.A.1    Orringer, E.P.2    Parker, J.C.3
  • 31
    • 0042925526 scopus 로고    scopus 로고
    • Ineffective erythropoiesis in the spleen of a patient with pyruvate kinase deficiency
    • Aizawa S, Kohdera U, Hiramoto M, et al. Ineffective erythropoiesis in the spleen of a patient with pyruvate kinase deficiency. Am J Hematol. 2003;74(1):68-72.
    • (2003) Am J Hematol , vol.74 , Issue.1 , pp. 68-72
    • Aizawa, S.1    Kohdera, U.2    Hiramoto, M.3
  • 32
    • 70349416600 scopus 로고    scopus 로고
    • Adenosine triphosphate depletion of erythrocytes simulates the phenotype associated with pyruvate kinase deficiency and confers protection against Plasmodium falciparum in vitro
    • Ayi K, Liles WC, Gros P, Kain KC. Adenosine triphosphate depletion of erythrocytes simulates the phenotype associated with pyruvate kinase deficiency and confers protection against Plasmodium falciparum in vitro. J Infect Dis. 2009; 200(8):1289-1299.
    • (2009) J Infect Dis , vol.200 , Issue.8 , pp. 1289-1299
    • Ayi, K.1    Liles, W.C.2    Gros, P.3    Kain, K.C.4
  • 34
    • 14844292862 scopus 로고    scopus 로고
    • Ex vivo generation of fully mature human red blood cells from hematopoietic stem cells
    • Giarratana MC, Kobari L, Lapillonne H, et al. Ex vivo generation of fully mature human red blood cells from hematopoietic stem cells. Nat Biotechnol. 2005;23(1):69-74.
    • (2005) Nat Biotechnol , vol.23 , Issue.1 , pp. 69-74
    • Giarratana, M.C.1    Kobari, L.2    Lapillonne, H.3
  • 35
    • 85029478783 scopus 로고    scopus 로고
    • Effects of AG-348, a pyruvate kinase activator, on anemia and hemolysis in patients with pyruvate kinase deficiency: Early data from the DRIVE PK study
    • abstract
    • Grace RF, Rose C, Layton DM, et al. Effects of AG-348, a pyruvate kinase activator, on anemia and hemolysis in patients with pyruvate kinase deficiency: early data from the DRIVE PK study [abstract]. Haematologica. 2016;101(s1). Abstract S466.
    • (2016) Haematologica , vol.101 , Issue.s1
    • Grace, R.F.1    Rose, C.2    Layton, D.M.3
  • 36
    • 76549120274 scopus 로고    scopus 로고
    • Metabolic remodeling of the human red blood cell membrane
    • Park Y, Best CA, Auth T, et al. Metabolic remodeling of the human red blood cell membrane. Proc Natl Acad Sci USA. 2010; 107(4):1289-1294.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.4 , pp. 1289-1294
    • Park, Y.1    Best, C.A.2    Auth, T.3
  • 37
    • 0014506945 scopus 로고
    • Metabolic dependence of red cell deformability
    • Weed RI, LaCelle PL, Merrill EW. Metabolic dependence of red cell deformability. J Clin Invest. 1969;48(5):795-809.
    • (1969) J Clin Invest , vol.48 , Issue.5 , pp. 795-809
    • Weed, R.I.1    LaCelle, P.L.2    Merrill, E.W.3
  • 38
    • 84861816666 scopus 로고    scopus 로고
    • Integrated protein quality-control pathways regulate free α-globin in murine β-thalassemia
    • Khandros E, Thom CS, D’Souza J, Weiss MJ. Integrated protein quality-control pathways regulate free α-globin in murine β-thalassemia. Blood. 2012;119(22):5265-5275.
    • (2012) Blood , vol.119 , Issue.22 , pp. 5265-5275
    • Khandros, E.1    Thom, C.S.2    D’Souza, J.3    Weiss, M.J.4


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