메뉴 건너뛰기




Volumn 98, Issue 2, 2013, Pages 496-501

Novel insights into fatty acid oxidation, amino acid metabolism, and insulin secretion fromstudying patients with loss of function mutations in 3-hydroxyacyl-CoA dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

3 HYDROXYACYL COENZYME A DEHYDROGENASE; AMINO ACID; DIAZOXIDE; FATTY ACID; GLUTAMATE DEHYDROGENASE; INSULIN;

EID: 84873657887     PISSN: 0021972X     EISSN: 19457197     Source Type: Journal    
DOI: 10.1210/jc.2012-3134     Document Type: Review
Times cited : (19)

References (28)
  • 1
    • 0842287450 scopus 로고    scopus 로고
    • Mitochondrial β-oxidation
    • Bartlett K, Eaton S. Mitochondrial β-oxidation. Eur J Biochem. 2004;271(3):462-469.
    • (2004) Eur J Biochem. , vol.271 , Issue.3 , pp. 462-469
    • Bartlett, K.1    Eaton, S.2
  • 4
    • 77957554125 scopus 로고    scopus 로고
    • Pathophysiology of fatty acid oxidation disorders
    • Bennett MJ. Pathophysiology of fatty acid oxidation disorders. J Inherit Metab Dis. 2010;33(5):533-537.
    • (2010) J Inherit Metab Dis. , vol.33 , Issue.5 , pp. 533-537
    • Bennett, M.J.1
  • 5
    • 0015919670 scopus 로고
    • L-3-hydroxyacyl coenzyme A dehydrogenase from pig heart muscle. I. Purification and properties
    • Noyes BE, Bradshaw RA. L-3-Hydroxyacyl coenzyme A dehydrogenase from pig heart muscle. I. Purification and properties. J Biol Chem. 1973;248(9):3052- 3059.
    • (1973) J Biol Chem. , vol.248 , Issue.9 , pp. 3052-3059
    • Noyes, B.E.1    Bradshaw, R.A.2
  • 6
    • 0024382885 scopus 로고
    • Assay of L-3-hydroxyacyl-coenzyme A dehydrogenase with substrates of different chain lengths
    • He XY, Yang SY, Schulz H. Assay of L-3-hydroxyacyl-coenzyme A dehydrogenase with substrates of different chain lengths. Anal Biochem. 1989;180(1):105-109.
    • (1989) Anal Biochem. , vol.180 , Issue.1 , pp. 105-109
    • He, X.Y.1    Yang, S.Y.2    Schulz, H.3
  • 8
    • 0017746899 scopus 로고
    • Hydroxyacyl CoA dehydrogenase, an enzyme important in fat metabolism in different cell types in the islets of Langerhans
    • Agren A, Borg K, Brolin SE, Carlman J, Lundqvist G. Hydroxyacyl CoA dehydrogenase, an enzyme important in fat metabolism in different cell types in the islets of Langerhans. Diabetes Metab. 1977; 3(3):169-172.
    • (1977) Diabetes Metab. , vol.3 , Issue.3 , pp. 169-172
    • Agren, A.1    Borg, K.2    Brolin, S.E.3    Carlman, J.4    Lundqvist, G.5
  • 9
    • 34547095291 scopus 로고    scopus 로고
    • Specificity in β cell expression of L-3-hydroxyacyl-CoA dehydrogenase, short chain, and potential role in down-regulating insulin release
    • Martens GA, Vervoort A, Van de CM, et al. Specificity in β cell expression of L-3-hydroxyacyl-CoA dehydrogenase, short chain, and potential role in down-regulating insulin release. J Biol Chem. 2007;282(29):21134-21144.
    • (2007) J Biol Chem. , vol.282 , Issue.29 , pp. 21134-21144
    • Martens, G.A.1    Vervoort, A.2    Van De, C.M.3
  • 11
    • 0035394988 scopus 로고    scopus 로고
    • Tissue-specific deletion of Foxa2 in pancreatic β cells results in hyperinsulinemic hypoglycemia
    • Sund NJ, Vatamaniuk MZ, Casey M, et al. Tissue-specific deletion of Foxa2 in pancreatic β cells results in hyperinsulinemic hypoglycemia. Genes Dev. 2001;15(13):1706-1715.
    • (2001) Genes Dev. , vol.15 , Issue.13 , pp. 1706-1715
    • Sund, N.J.1    Vatamaniuk, M.Z.2    Casey, M.3
  • 12
    • 0034902277 scopus 로고    scopus 로고
    • Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of β-oxidation in insulin secretion
    • Clayton PT, Eaton S, Aynsley-Green A, et al. Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of β-oxidation in insulin secretion. J Clin Invest. 2001;108(3):457-465.
    • (2001) J Clin Invest. , vol.108 , Issue.3 , pp. 457-465
    • Clayton, P.T.1    Eaton, S.2    Aynsley-Green, A.3
  • 13
    • 0347990591 scopus 로고    scopus 로고
    • Familial hyperinsulinemic hypoglycemia caused by a defect in the SCHAD enzyme of mitochondrial fatty acid oxidation
    • Molven A, Matre GE, Duran M, et al. Familial hyperinsulinemic hypoglycemia caused by a defect in the SCHAD enzyme of mitochondrial fatty acid oxidation. Diabetes. 2004;53(1):221-227.
    • (2004) Diabetes. , vol.53 , Issue.1 , pp. 221-227
    • Molven, A.1    Matre, G.E.2    Duran, M.3
  • 14
    • 20944434799 scopus 로고    scopus 로고
    • Hyperinsulinism of infancy associated with a novel splice site mutation in the SCHAD gene
    • Hussain K, Clayton PT, Krywawych S, et al. Hyperinsulinism of infancy associated with a novel splice site mutation in the SCHAD gene. J Pediatr. 2005;146(5):706-708.
    • (2005) J Pediatr. , vol.146 , Issue.5 , pp. 706-708
    • Hussain, K.1    Clayton, P.T.2    Krywawych, S.3
  • 15
    • 67650221414 scopus 로고    scopus 로고
    • 3-Hydroxyacyl-coenzyme A dehydrogenase deficiency and hyperinsulinemic hypoglycemia: Characterization of a novel mutation and severe dietary protein sensitivity
    • Kapoor RR, James C, Flanagan SE, Ellard S, Eaton S, Hussain K. 3-Hydroxyacyl-coenzyme A dehydrogenase deficiency and hyperinsulinemic hypoglycemia: characterization of a novel mutation and severe dietary protein sensitivity. J Clin Endocrinol Metab. 2009; 94(7):2221-2225.
    • (2009) J Clin Endocrinol Metab. , vol.94 , Issue.7 , pp. 2221-2225
    • Kapoor, R.R.1    James, C.2    Flanagan, S.E.3    Ellard, S.4    Eaton, S.5    Hussain, K.6
  • 16
    • 66149153000 scopus 로고    scopus 로고
    • Identification of a diffuse form of hyperinsulinemic hypoglycemia by 18-fluoro-L-3,4 dihydroxyphenylalanine positron emission tomography/CT in a patient carrying a novel mutation of the HADH gene
    • Di CS, Gessi A, Pepe G, et al. Identification of a diffuse form of hyperinsulinemic hypoglycemia by 18-fluoro-L-3,4 dihydroxyphenylalanine positron emission tomography/CT in a patient carrying a novel mutation of the HADH gene. Eur J Endocrinol. 2009; 160(6):1019-1023.
    • (2009) Eur J Endocrinol. , vol.160 , Issue.6 , pp. 1019-1023
    • Di, C.S.1    Gessi, A.2    Pepe, G.3
  • 17
    • 79959771790 scopus 로고    scopus 로고
    • Short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: The clinical relevance of an early diagnosis and report of four new cases
    • Martins E, Cardoso ML, Rodrigues E, et al. Short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: the clinical relevance of an early diagnosis and report of four new cases. J Inherit Metab Dis. 2011;34(3):835-842.
    • (2011) J Inherit Metab Dis. , vol.34 , Issue.3 , pp. 835-842
    • Martins, E.1    Cardoso, M.L.2    Rodrigues, E.3
  • 18
    • 0346788907 scopus 로고    scopus 로고
    • Short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency associated with hyperinsulinism: A novel glucose-fatty acid cycle?
    • Eaton S, Chatziandreou I, Krywawych S, Pen S, Clayton PT, Hussain K. Short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency associated with hyperinsulinism: a novel glucose-fatty acid cycle? Biochem Soc Trans. 2003;31(Pt 6):1137-1139.
    • (2003) Biochem Soc Trans. , vol.31 , Issue.PART 6 , pp. 1137-1139
    • Eaton, S.1    Chatziandreou, I.2    Krywawych, S.3    Pen, S.4    Clayton, P.T.5    Hussain, K.6
  • 20
    • 0023695196 scopus 로고
    • Regulation of insulin release by factors that also modify glutamate dehydrogenase
    • Fahien LA, MacDonald MJ, Kmiotek EH, Mertz RJ, Fahien CM. Regulation of insulin release by factors that also modify glutamate dehydrogenase. J Biol Chem. 1988;263(27):13610-13614.
    • (1988) J Biol Chem. , vol.263 , Issue.27 , pp. 13610-13614
    • Fahien, L.A.1    MacDonald, M.J.2    Kmiotek, E.H.3    Mertz, R.J.4    Fahien, C.M.5
  • 21
    • 33745955624 scopus 로고    scopus 로고
    • Protein-sensitive hypoglycemia without leucine sensitivity in hyperinsulinism caused by K(ATP) channel mutations
    • Fourtner SH, Stanley CA, Kelly A. Protein-sensitive hypoglycemia without leucine sensitivity in hyperinsulinism caused by K(ATP) channel mutations. J Pediatr. 2006;149(1):47-52.
    • (2006) J Pediatr. , vol.149 , Issue.1 , pp. 47-52
    • Fourtner, S.H.1    Stanley, C.A.2    Kelly, A.3
  • 22
    • 77957760755 scopus 로고    scopus 로고
    • Mechanism of hyperinsulinism in short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency involves activation of glutamate dehydrogenase
    • Li C, Chen P, Palladino A, et al. Mechanism of hyperinsulinism in short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency involves activation of glutamate dehydrogenase. J Biol Chem. 2010;285(41): 31806-31818.
    • (2010) J Biol Chem. , vol.285 , Issue.41 , pp. 31806-31818
    • Li, C.1    Chen, P.2    Palladino, A.3
  • 23
    • 84860809004 scopus 로고    scopus 로고
    • Leucine-sensitive hyperinsulinaemic hypoglycaemia in patients with loss of function mutations in 3-hydroxyacyl-CoA dehydrogenase
    • Heslegrave AJ, Kapoor RR, Eaton S, et al. Leucine-sensitive hyperinsulinaemic hypoglycaemia in patients with loss of function mutations in 3-hydroxyacyl-CoA dehydrogenase. Orphanet J Rare Dis. 2012;7(1):25.
    • (2012) Orphanet J Rare Dis. , vol.7 , Issue.1 , pp. 25
    • Heslegrave, A.J.1    Kapoor, R.R.2    Eaton, S.3
  • 24
    • 39149123797 scopus 로고    scopus 로고
    • Role of short-chain hydroxyacyl CoA dehydrogenases in SCHAD deficiency
    • Filling C, Keller B, Hirschberg D, et al. Role of short-chain hydroxyacyl CoA dehydrogenases in SCHAD deficiency. Biochem Biophys Res Commun. 2008;368(1):6-11.
    • (2008) Biochem Biophys Res Commun. , vol.368 , Issue.1 , pp. 6-11
    • Filling, C.1    Keller, B.2    Hirschberg, D.3
  • 25
    • 77952626170 scopus 로고    scopus 로고
    • Systemic activation of glutamate dehydrogenase increases renal ammoniagenesis: Implications for the hyperinsulinism/hyperammonemia syndrome
    • Treberg JR, Clow KA, Greene KA, Brosnan ME, Brosnan JT. Systemic activation of glutamate dehydrogenase increases renal ammoniagenesis: implications for the hyperinsulinism/hyperammonemia syndrome. Am J Physiol Endocrinol Metab. 2010;298(6):E1219-E1225.
    • (2010) Am J Physiol Endocrinol Metab , vol.298 , Issue.6
    • Treberg, J.R.1    Clow, K.A.2    Greene, K.A.3    Brosnan, M.E.4    Brosnan, J.T.5
  • 26
    • 80052271742 scopus 로고    scopus 로고
    • The structure and allosteric regulation of glutamate dehydrogenase
    • Li M, Li C, Allen A, Stanley CA, Smith TJ. The structure and allosteric regulation of glutamate dehydrogenase. Neurochem Int. 2011;59(4):445-455.
    • (2011) Neurochem Int. , vol.59 , Issue.4 , pp. 445-455
    • Li, M.1    Li, C.2    Allen, A.3    Stanley, C.A.4    Smith, T.J.5
  • 27
    • 84857804808 scopus 로고    scopus 로고
    • The structure and allosteric regulation of mammalian glutamate dehydrogenase
    • Li M, Li C, Allen A, Stanley CA, Smith TJ. The structure and allosteric regulation of mammalian glutamate dehydrogenase. Arch Biochem Biophys. 2012;519(2):69-80.
    • (2012) Arch Biochem Biophys. , vol.519 , Issue.2 , pp. 69-80
    • Li, M.1    Li, C.2    Allen, A.3    Stanley, C.A.4    Smith, T.J.5
  • 28
    • 84859506954 scopus 로고    scopus 로고
    • Short-chain 3-hydroxyacyl-coenzyme A dehydrogenase associates with a protein super-complex integrating multiple metabolic pathways
    • Narayan SB, Master SR, Sireci AN, et al. Short-chain 3-hydroxyacyl- coenzyme A dehydrogenase associates with a protein super-complex integrating multiple metabolic pathways. PLoS One. 2012; 7(4):e35048.
    • (2012) PLoS One. , vol.7 , Issue.4
    • Narayan, S.B.1    Master, S.R.2    Sireci, A.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.