메뉴 건너뛰기




Volumn 21, Issue 11, 2014, Pages 1486-1496

Inhibition of AMP deaminase activity does not improve glucose control in rodent models of insulin resistance or diabetes

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE MONOPHOSPHATE DEAMINASE; ADENOSINE MONOPHOSPHATE DEAMINASE INHIBITOR; GLUCOSE; HYDROLASE INHIBITOR; INSULIN; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; AMPD1 PROTEIN, MOUSE; ENZYME INHIBITOR; GLUCOSE BLOOD LEVEL; MOLECULAR LIBRARY; PROTEIN BINDING; RECOMBINANT PROTEIN;

EID: 84911490585     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2014.09.011     Document Type: Article
Times cited : (20)

References (50)
  • 6
    • 84862493914 scopus 로고    scopus 로고
    • AMP-activated protein kinase: New regulation, new roles?
    • D. Carling, C. Thornton, A. Woods, and M.J. Sanders AMP-activated protein kinase: new regulation, new roles? Biochem. J. 445 2012 11 27
    • (2012) Biochem. J. , vol.445 , pp. 11-27
    • Carling, D.1    Thornton, C.2    Woods, A.3    Sanders, M.J.4
  • 7
    • 0030272559 scopus 로고    scopus 로고
    • A comparison of AMP degradation in the perfused rat heart during 2-deoxy-D-glucose perfusion and anoxia. Part I: The release of adenosine and inosine
    • W. Chen, J. Hoerter, and M. Guéron A comparison of AMP degradation in the perfused rat heart during 2-deoxy-D-glucose perfusion and anoxia. Part I: The release of adenosine and inosine J. Mol. Cell. Cardiol. 28 1996 2163 2174
    • (1996) J. Mol. Cell. Cardiol. , vol.28 , pp. 2163-2174
    • Chen, W.1    Hoerter, J.2    Guéron, M.3
  • 8
    • 33748679351 scopus 로고    scopus 로고
    • The impact of the AMPD1 gene polymorphism on exercise capacity, other prognostic parameters, and survival in patients with stable congestive heart failure: A study in 686 consecutive patients
    • P. de Groote, N. Lamblin, N. Helbecque, F. Mouquet, X. Hermant, P. Amouyel, J. Dallongeville, and C. Bauters The impact of the AMPD1 gene polymorphism on exercise capacity, other prognostic parameters, and survival in patients with stable congestive heart failure: a study in 686 consecutive patients Am. Heart J. 152 2006 736 741
    • (2006) Am. Heart J. , vol.152 , pp. 736-741
    • De Groote, P.1    Lamblin, N.2    Helbecque, N.3    Mouquet, F.4    Hermant, X.5    Amouyel, P.6    Dallongeville, J.7    Bauters, C.8
  • 10
    • 0038666831 scopus 로고
    • Nucleotides and Adenosine Monophosphate Deaminase Activity of Muscle in Primary Hypokalaemic Periodic Paralysis
    • A.G. Engel, C.S. Potter, and J.W. Rosevear Nucleotides and Adenosine Monophosphate Deaminase Activity of Muscle in Primary Hypokalaemic Periodic Paralysis Nature 202 1964 670 672
    • (1964) Nature , vol.202 , pp. 670-672
    • Engel, A.G.1    Potter, C.S.2    Rosevear, J.W.3
  • 14
    • 0018200117 scopus 로고
    • Myoadenylate deaminase deficiency: A new disease of muscle
    • W.N. Fishbein, V.W. Armbrustmacher, and J.L. Griffin Myoadenylate deaminase deficiency: a new disease of muscle Science 200 1978 545 548
    • (1978) Science , vol.200 , pp. 545-548
    • Fishbein, W.N.1    Armbrustmacher, V.W.2    Griffin, J.L.3
  • 16
    • 84869837353 scopus 로고    scopus 로고
    • Direct AMP-activated protein kinase activators: A review of evidence from the patent literature
    • F. Giordanetto, and D. Karis Direct AMP-activated protein kinase activators: a review of evidence from the patent literature Expert Opin Ther Pat 22 2012 1467 1477
    • (2012) Expert Opin Ther Pat , vol.22 , pp. 1467-1477
    • Giordanetto, F.1    Karis, D.2
  • 17
    • 20144387995 scopus 로고    scopus 로고
    • Variation in the gene for muscle-specific AMP deaminase is associated with insulin clearance, a highly heritable trait
    • M.O. Goodarzi, K.D. Taylor, X. Guo, M.J. Quiñones, J. Cui, X. Li, T. Hang, H. Yang, E. Holmes, and W.A. Hsueh Variation in the gene for muscle-specific AMP deaminase is associated with insulin clearance, a highly heritable trait Diabetes 54 2005 1222 1227
    • (2005) Diabetes , vol.54 , pp. 1222-1227
    • Goodarzi, M.O.1    Taylor, K.D.2    Guo, X.3    Quiñones, M.J.4    Cui, J.5    Li, X.6    Hang, T.7    Yang, H.8    Holmes, E.9    Hsueh, W.A.10
  • 18
    • 34848861463 scopus 로고    scopus 로고
    • The energy sensor AMP-activated protein kinase directly regulates the mammalian FOXO3 transcription factor
    • E.L. Greer, P.R. Oskoui, M.R. Banko, J.M. Maniar, M.P. Gygi, S.P. Gygi, and A. Brunet The energy sensor AMP-activated protein kinase directly regulates the mammalian FOXO3 transcription factor J. Biol. Chem. 282 2007 30107 30119
    • (2007) J. Biol. Chem. , vol.282 , pp. 30107-30119
    • Greer, E.L.1    Oskoui, P.R.2    Banko, M.R.3    Maniar, J.M.4    Gygi, M.P.5    Gygi, S.P.6    Brunet, A.7
  • 19
    • 0037297179 scopus 로고    scopus 로고
    • Expression, purification, and inhibition of in vitro proteolysis of human AMPD2 (isoform L) recombinant enzymes
    • A.L. Haas, and R.L. Sabina Expression, purification, and inhibition of in vitro proteolysis of human AMPD2 (isoform L) recombinant enzymes Protein Expr. Purif. 27 2003 293 303
    • (2003) Protein Expr. Purif. , vol.27 , pp. 293-303
    • Haas, A.L.1    Sabina, R.L.2
  • 20
    • 84868005485 scopus 로고    scopus 로고
    • AMP-activated protein kinase: A target for drugs both ancient and modern
    • D.G. Hardie, F.A. Ross, and S.A. Hawley AMP-activated protein kinase: a target for drugs both ancient and modern Chem. Biol. 19 2012 1222 1236
    • (2012) Chem. Biol. , vol.19 , pp. 1222-1236
    • Hardie, D.G.1    Ross, F.A.2    Hawley, S.A.3
  • 21
    • 84858782079 scopus 로고    scopus 로고
    • AMPK: A nutrient and energy sensor that maintains energy homeostasis
    • D.G. Hardie, F.A. Ross, and S.A. Hawley AMPK: a nutrient and energy sensor that maintains energy homeostasis Nat. Rev. Mol. Cell Biol. 13 2012 251 262
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 251-262
    • Hardie, D.G.1    Ross, F.A.2    Hawley, S.A.3
  • 22
    • 0031862828 scopus 로고    scopus 로고
    • Design, synthesis, and structure-activity relationships of the first highly potent, selective, and bioavailable adenosine 5′-monophosphate deaminase inhibitors
    • S.R. Kasibhatla, B.C. Bookser, J.R. Appleman, G. Probst, W. Xiao, J.M. Fujitaki, and M.D. Erion Design, synthesis, and structure-activity relationships of the first highly potent, selective, and bioavailable adenosine 5′-monophosphate deaminase inhibitors Adv. Exp. Med. Biol. 431 1998 849 852
    • (1998) Adv. Exp. Med. Biol. , vol.431 , pp. 849-852
    • Kasibhatla, S.R.1    Bookser, B.C.2    Appleman, J.R.3    Probst, G.4    Xiao, W.5    Fujitaki, J.M.6    Erion, M.D.7
  • 23
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • J. Kim, M. Kundu, B. Viollet, and K.L. Guan AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1 Nat. Cell Biol. 13 2011 132 141
    • (2011) Nat. Cell Biol. , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 24
    • 0030983676 scopus 로고    scopus 로고
    • Metformin hydrochloride: An antihyperglycemic agent
    • T.B. Klepser, and M.W. Kelly Metformin hydrochloride: an antihyperglycemic agent Am. J. Health Syst. Pharm. 54 1997 893 903
    • (1997) Am. J. Health Syst. Pharm. , vol.54 , pp. 893-903
    • Klepser, T.B.1    Kelly, M.W.2
  • 25
    • 80053411075 scopus 로고    scopus 로고
    • Suppression of 5′-nucleotidase enzymes promotes AMP-activated protein kinase (AMPK) phosphorylation and metabolism in human and mouse skeletal muscle
    • S.S. Kulkarni, H.K. Karlsson, F. Szekeres, A.V. Chibalin, A. Krook, and J.R. Zierath Suppression of 5′-nucleotidase enzymes promotes AMP-activated protein kinase (AMPK) phosphorylation and metabolism in human and mouse skeletal muscle J. Biol. Chem. 286 2011 34567 34574
    • (2011) J. Biol. Chem. , vol.286 , pp. 34567-34574
    • Kulkarni, S.S.1    Karlsson, H.K.2    Szekeres, F.3    Chibalin, A.V.4    Krook, A.5    Zierath, J.R.6
  • 26
    • 78149476877 scopus 로고    scopus 로고
    • The association of AMPK with ULK1 regulates autophagy
    • J.W. Lee, S. Park, Y. Takahashi, and H.G. Wang The association of AMPK with ULK1 regulates autophagy PLoS ONE 5 2010 e15394
    • (2010) PLoS ONE , vol.5 , pp. 15394
    • Lee, J.W.1    Park, S.2    Takahashi, Y.3    Wang, H.G.4
  • 28
    • 77956536452 scopus 로고    scopus 로고
    • Synthesis and Biochemical Testing of 3-(Carboxyphenylethyl)imidazo[2,1-f][1,2,4]triazines as Inhibitors of AMP Deaminase
    • S.D. Lindell, S. Maechling, and R.L. Sabina Synthesis and Biochemical Testing of 3-(Carboxyphenylethyl)imidazo[2,1-f][1,2,4]triazines as Inhibitors of AMP Deaminase ACS Med Chem Lett 1 2010 286 289
    • (2010) ACS Med Chem Lett , vol.1 , pp. 286-289
    • Lindell, S.D.1    Maechling, S.2    Sabina, R.L.3
  • 29
    • 0036847135 scopus 로고    scopus 로고
    • AZ 242, a novel PPARalpha/gamma agonist with beneficial effects on insulin resistance and carbohydrate and lipid metabolism in ob/ob mice and obese Zucker rats
    • B. Ljung, K. Bamberg, B. Dahllöf, A. Kjellstedt, N.D. Oakes, J. Ostling, L. Svensson, and G. Camejo AZ 242, a novel PPARalpha/gamma agonist with beneficial effects on insulin resistance and carbohydrate and lipid metabolism in ob/ob mice and obese Zucker rats J. Lipid Res. 43 2002 1855 1863
    • (2002) J. Lipid Res. , vol.43 , pp. 1855-1863
    • Ljung, B.1    Bamberg, K.2    Dahllöf, B.3    Kjellstedt, A.4    Oakes, N.D.5    Ostling, J.6    Svensson, L.7    Camejo, G.8
  • 30
    • 0020533372 scopus 로고
    • Revised methods for the Salmonella mutagenicity test
    • D.M. Maron, and B.N. Ames Revised methods for the Salmonella mutagenicity test Mutat. Res. 113 1983 173 215
    • (1983) Mutat. Res. , vol.113 , pp. 173-215
    • Maron, D.M.1    Ames, B.N.2
  • 32
    • 0028834213 scopus 로고
    • Muscle AMP deaminase deficiency in 2% of a healthy population
    • B. Norman, B. Glenmark, and E. Jansson Muscle AMP deaminase deficiency in 2% of a healthy population Muscle Nerve 18 1995 239 241
    • (1995) Muscle Nerve , vol.18 , pp. 239-241
    • Norman, B.1    Glenmark, B.2    Jansson, E.3
  • 33
    • 0034973952 scopus 로고    scopus 로고
    • Regulation of skeletal muscle ATP catabolism by AMPD1 genotype during sprint exercise in asymptomatic subjects
    • B. Norman, R.L. Sabina, and E. Jansson Regulation of skeletal muscle ATP catabolism by AMPD1 genotype during sprint exercise in asymptomatic subjects J. Appl. Physiol. 91 2001 258 264
    • (2001) J. Appl. Physiol. , vol.91 , pp. 258-264
    • Norman, B.1    Sabina, R.L.2    Jansson, E.3
  • 35
    • 84857687439 scopus 로고    scopus 로고
    • AMPK functions as an adenylate charge-regulated protein kinase
    • J.S. Oakhill, J.W. Scott, and B.E. Kemp AMPK functions as an adenylate charge-regulated protein kinase Trends Endocrinol. Metab. 23 2012 125 132
    • (2012) Trends Endocrinol. Metab. , vol.23 , pp. 125-132
    • Oakhill, J.S.1    Scott, J.W.2    Kemp, B.E.3
  • 37
    • 78650931836 scopus 로고    scopus 로고
    • Metformin activates AMP kinase through inhibition of AMP deaminase
    • J. Ouyang, R.A. Parakhia, and R.S. Ochs Metformin activates AMP kinase through inhibition of AMP deaminase J. Biol. Chem. 286 2011 1 11
    • (2011) J. Biol. Chem. , vol.286 , pp. 1-11
    • Ouyang, J.1    Parakhia, R.A.2    Ochs, R.S.3
  • 40
    • 0019130655 scopus 로고
    • Disruption of the purine nucleotide cycle. A potential explanation for muscle dysfunction in myoadenylate deaminase deficiency
    • R.L. Sabina, J.L. Swain, B.M. Patten, T. Ashizawa, W.E. O'Brien, and E.W. Holmes Disruption of the purine nucleotide cycle. A potential explanation for muscle dysfunction in myoadenylate deaminase deficiency J. Clin. Invest. 66 1980 1419 1423
    • (1980) J. Clin. Invest. , vol.66 , pp. 1419-1423
    • Sabina, R.L.1    Swain, J.L.2    Patten, B.M.3    Ashizawa, T.4    O'Brien, W.E.5    Holmes, E.W.6
  • 42
    • 79953211917 scopus 로고    scopus 로고
    • Nutrient starvation elicits an acute autophagic response mediated by Ulk1 dephosphorylation and its subsequent dissociation from AMPK
    • L. Shang, S. Chen, F. Du, S. Li, L. Zhao, and X. Wang Nutrient starvation elicits an acute autophagic response mediated by Ulk1 dephosphorylation and its subsequent dissociation from AMPK Proc. Natl. Acad. Sci. USA 108 2011 4788 4793
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 4788-4793
    • Shang, L.1    Chen, S.2    Du, F.3    Li, S.4    Zhao, L.5    Wang, X.6
  • 44
    • 0032923739 scopus 로고    scopus 로고
    • Generalized lacZ expression with the ROSA26 Cre reporter strain
    • P. Soriano Generalized lacZ expression with the ROSA26 Cre reporter strain Nat. Genet. 21 1999 70 71
    • (1999) Nat. Genet. , vol.21 , pp. 70-71
    • Soriano, P.1
  • 47
    • 0033003760 scopus 로고    scopus 로고
    • A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays
    • J.H. Zhang, T.D. Chung, and K.R. Oldenburg A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays J. Biomol. Screen. 4 1999 67 73
    • (1999) J. Biomol. Screen. , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 48
    • 65349177200 scopus 로고    scopus 로고
    • AMPK: An emerging drug target for diabetes and the metabolic syndrome
    • B.B. Zhang, G. Zhou, and C. Li AMPK: an emerging drug target for diabetes and the metabolic syndrome Cell Metab. 9 2009 407 416
    • (2009) Cell Metab. , vol.9 , pp. 407-416
    • Zhang, B.B.1    Zhou, G.2    Li, C.3
  • 49
    • 79551507263 scopus 로고    scopus 로고
    • AMPK-dependent phosphorylation of ULK1 induces autophagy
    • M. Zhao, and D.J. Klionsky AMPK-dependent phosphorylation of ULK1 induces autophagy Cell Metab. 13 2011 119 120
    • (2011) Cell Metab. , vol.13 , pp. 119-120
    • Zhao, M.1    Klionsky, D.J.2
  • 50
    • 63849224233 scopus 로고    scopus 로고
    • AMPK activators - Potential therapeutics for metabolic and other diseases
    • G. Zhou, I.K. Sebhat, and B.B. Zhang AMPK activators - potential therapeutics for metabolic and other diseases Acta Physiol. (Oxf.) 196 2009 175 190
    • (2009) Acta Physiol. (Oxf.) , vol.196 , pp. 175-190
    • Zhou, G.1    Sebhat, I.K.2    Zhang, B.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.