Table of Contents Author Guidelines Submit a Manuscript
Scientifica
Volume 2016, Article ID 9828672, 14 pages
http://dx.doi.org/10.1155/2016/9828672
Review Article

Human Metabolic Enzymes Deficiency: A Genetic Mutation Based Approach

1Department of Pharmaceutical Sciences, Babasaheb Bhimrao Ambedkar University, Raebareli Road, Vidyavihar, Lucknow 226025, India
2Department of Pharmaceutical Technology, Jadavpur University, Kolkata 700032, India
3Dr. Reddy’s Laboratories Limited, Bachupally, Hyderabad, Telangana 502325, India

Received 1 December 2015; Revised 21 January 2016; Accepted 31 January 2016

Academic Editor: Gary Lopaschuk

Copyright © 2016 Swati Chaturvedi et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. A. E. Vasdekis and G. Stephanopoulos, “Review of methods to probe single cell metabolism and bioenergetics,” Metabolic Engineering, vol. 27, pp. 115–135, 2015. View at Publisher · View at Google Scholar · View at Scopus
  2. S. Chanprasert and F. Scaglia, “Adult liver disorders caused by inborn errors of metabolism: review and update,” Molecular Genetics and Metabolism, vol. 114, no. 1, pp. 1–10, 2015. View at Publisher · View at Google Scholar · View at Scopus
  3. S. Sharma, P. Kumar, R. Agarwal, M. Kabra, A. Deorari, and V. Paul, “Approach to inborn errors of metabolism presenting in the neonate,” Indian Journal of Pediatrics, vol. 75, no. 3, pp. 271–276, 2010. View at Google Scholar
  4. B. A. Barshop, “Metabolic disease,” Genetics, vol. 3, pp. 37–46, 2003. View at Google Scholar
  5. National Institutes of Health, “NINDS, handout on lipid storage diseases fact sheet,” NIH Publication 05-2628, 2005. View at Google Scholar
  6. Metabolic Backgrounder: The Ross Metabolic Formula System for Meeting Special Nutrition Needs, Ross Products Division, Columbus, Ohio, USA, 2007.
  7. B. Wilcken, “An introduction to nutritional treatment in Inborn errors of metabolism—different disorders, different approaches,” The Southeast Asian Journal of Tropical medicine and Public Health, vol. 34, pp. 198–201, 2003. View at Google Scholar · View at Scopus
  8. K. M. Hendricks and C. Duggan, Manual of Pediatric Nutrition, BC Decker, 4th edition, 2005.
  9. S. Banka, R. Wynn, H. Byers, P. D. Arkwright, and W. G. Newman, “G6PC3 mutations cause non-syndromic severe congenital neutropenia,” Molecular Genetics and Metabolism, vol. 108, no. 2, pp. 138–141, 2013. View at Publisher · View at Google Scholar · View at Scopus
  10. K.-J. Lei, H. Chen, C.-J. Pan et al., “Glucose-6-phosphatase dependent substrate transport in the glycogen storage disease type-1a mouse,” Nature Genetics, vol. 13, no. 2, pp. 203–209, 1996. View at Publisher · View at Google Scholar · View at Scopus
  11. E. V. Schaftingen, “Fructose 2,6-bisphosphate,” Advances in Enzymology and Related areas of Molecular Biology, vol. 59, pp. 315–395, 1987. View at Google Scholar · View at Scopus
  12. J. Ashmore, A. B. Hastings, F. B. Nesbett, and A. E. Renold, “Studies on carbohydrate metabolism in rat liver slices. VI. Hormonal factors influencing glucose-6- phosphatise,” The Journal of Biological Chemistry, vol. 218, pp. 77–88, 1956. View at Google Scholar
  13. G. Wirthensohn and W. G. Guder, “Renal substrate metabolism,” Physiological Reviews, vol. 66, no. 2, pp. 469–497, 1986. View at Google Scholar · View at Scopus
  14. F. Rajas, N. Bruni, S. Montano, C. Zitoun, and G. Mithieux, “The glucose-6 phosphatase gene is expressed in human and rat small intestine: regulation of expression in fasted and diabetic rats,” Gastroenterology, vol. 117, no. 1, pp. 132–139, 1999. View at Publisher · View at Google Scholar · View at Scopus
  15. D. Azzout-Marniche, C. Gaudichon, C. Blouet et al., “Liver glyconeogenesis: a pathway to cope with postprandial amino acid excess in high-protein fed rats?” The American Journal of Physiology—Regulatory Integrative and Comparative Physiology, vol. 292, no. 4, pp. R1400–R1407, 2007. View at Publisher · View at Google Scholar · View at Scopus
  16. A. Benedetti, R. Fulceri, M. Ferro, and M. Comporti, “On a possible role for glucose-6-phosphatase in the regulation of liver cell cytosolic calcium concentration,” Trends in Biochemical Sciences, vol. 11, no. 7, pp. 284–285, 1986. View at Publisher · View at Google Scholar · View at Scopus
  17. K. Boztug, P. S. Rosenberg, M. Dorda et al., “Extended spectrum of human glucose-6-phosphatase catalytic subunit 3 deficiency: novel genotypes and phenotypic variability in severe congenital neutropenia,” Journal of Pediatrics, vol. 160, no. 4, pp. 679.e2–683.e2, 2012. View at Publisher · View at Google Scholar · View at Scopus
  18. J. C. Hutton and R. M. O'Brien, “Glucose-6-phosphatase catalytic subunit gene family,” The Journal of Biological Chemistry, vol. 284, no. 43, pp. 29241–29245, 2009. View at Publisher · View at Google Scholar · View at Scopus
  19. J. Yang Chou and B. C. Mansfield, “Molecular genetics of type 1 glycogen storage diseases,” Trends in Endocrinology and Metabolism, vol. 10, no. 3, pp. 104–113, 1999. View at Publisher · View at Google Scholar · View at Scopus
  20. R. Froissart, M. Piraud, A. M. Boudjemline et al., “Glucose-6-phosphatase deficiency,” Orphanet Journal of Rare Diseases, vol. 6, article 27, 2011. View at Publisher · View at Google Scholar · View at Scopus
  21. P. Marcolongo, R. Fulceri, A. Gamberucci, I. Czegle, G. Banhegyi, and A. Benedetti, “Multiple roles of glucose-6-phosphatases in pathophysiology: state of the art and future trends,” Biochimica et Biophysica Acta (BBA)—General Subjects, vol. 1830, no. 3, pp. 2608–2618, 2013. View at Publisher · View at Google Scholar · View at Scopus
  22. Y. T. Chen, “Glycogen storage diseases,” in The Metabolic Bases of Inherited Disease, pp. 1521–1551, McGraw-Hill, New York, NY, USA, 8th edition, 2000. View at Google Scholar
  23. Y. T. Chen and J. L. Van Hove, “Renal involvement in type I glycogen storage disease,” Advances in nephrology from the Necker Hospital, vol. 24, pp. 357–365, 1995. View at Google Scholar
  24. S. Efendic, S. Karlander, and M. Vranic, “Mild type II diabetes markedly increases glucose cycling in the postabsorptive state and during glucose infusion irrespective of obesity,” The Journal of Clinical Investigation, vol. 81, no. 6, pp. 1953–1961, 1988. View at Publisher · View at Google Scholar · View at Scopus
  25. Y. T. Chen and A. Burchell, The Metabolic Basis of Inherited Disease, McGraw-Hill, New York, NY, USA, 7th edition, 1995.
  26. J. Y. Chou, H. S. Jun, and B. C. Mansfield, “Glycogen storage disease type I and G6Pase-β deficiency: etiology and therapy,” Nature Reviews Endocrinology, vol. 6, no. 12, pp. 676–688, 2010. View at Publisher · View at Google Scholar · View at Scopus
  27. P. S. Kishnani, E. Faulkner, S. VanCamp et al., “Canine model and genomic structural organization of glycogen storage disease type Ia (GSD Ia),” Veterinary Pathology, vol. 38, no. 1, pp. 83–91, 2001. View at Publisher · View at Google Scholar · View at Scopus
  28. A. Zingone, H. Hiraiwa, C.-J. Pan et al., “Correction of glycogen storage disease type 1a in a mouse model by gene therapy,” The Journal of Biological Chemistry, vol. 275, no. 2, pp. 828–832, 2000. View at Publisher · View at Google Scholar · View at Scopus
  29. D. D. Koeberl, B. Sun, A. Bird, Y. T. Chen, K. Oka, and L. Chan, “Efficacy of helper-dependent adenovirus vector-mediated gene therapy in murine glycogen storage disease type Ia,” Molecular Therapy, vol. 15, no. 7, pp. 1253–1258, 2007. View at Publisher · View at Google Scholar · View at Scopus
  30. G. Visser, J.-P. Rake, J. Fernandes et al., “Neutropenia, neutrophil dysfunction, and inflammatory bowel disease in glycogen storage disease type Ib: results of the European study on glycogen storage disease type I,” Journal of Pediatrics, vol. 137, no. 2, pp. 187–191, 2000. View at Publisher · View at Google Scholar · View at Scopus
  31. B. K. Dieckgraefe, J. R. Korzenik, A. Husain, and L. Dieruf, “Association of glycogen storage disease 1b and Crohn disease: results of a North American survey,” European Journal of Pediatrics, vol. 161, no. 1, pp. S88–S92, 2002. View at Publisher · View at Google Scholar · View at Scopus
  32. H. L. Greene, F. B. Stifel, and R. H. Herman, “‘Ketotic hypoglycemia’ due to hepatic fructose-1,6-diphosphatase deficiency: treatment with folic acid,” The American Journal of Diseases of Children, vol. 124, no. 3, pp. 415–418, 1972. View at Google Scholar
  33. D. D. Koeberl, P. S. Kishnani, D. Bali, and Y.-T. Chen, “Emerging therapies for glycogen storage disease type I,” Trends in Endocrinology and Metabolism, vol. 20, no. 5, pp. 252–258, 2009. View at Publisher · View at Google Scholar · View at Scopus
  34. D. H. J. Martens, J. P. Rake, G. Navis, V. Fidler, C. M. L. Van Dael, and G. P. A. Smit, “Renal function in glycogen storage disease type I, natural course, and renopreservative effects of ACE inhibition,” Clinical Journal of the American Society of Nephrology, vol. 4, no. 11, pp. 1741–1746, 2009. View at Publisher · View at Google Scholar · View at Scopus
  35. D. Matern, T. E. Starzl, W. Arnaout et al., “Liver transplantation for glycogen storage disease types I, III, and IV,” European Journal of Pediatrics, vol. 158, supplement 2, pp. S43–S48, 1999. View at Publisher · View at Google Scholar · View at Scopus
  36. L. Fatvre, D. Houssin, J. Valayer, J. Brouard, M. Hadchouel, and O. Bernard, “Long-term outcome of liver transplantation in patients with glycogen storage disease type Ia,” Journal of Inherited Metabolic Disease, vol. 22, no. 6, pp. 723–732, 1999. View at Publisher · View at Google Scholar · View at Scopus
  37. M. K. Davis and D. A. Weinstein, “Liver transplantation in children with glycogen storage disease: controversies and evaluation of the risk/benefit of this procedure,” Pediatric Transplantation, vol. 12, no. 2, pp. 137–145, 2008. View at Publisher · View at Google Scholar · View at Scopus
  38. S. K. Reddy, S. L. Austin, M. Spencer-Manzon et al., “Liver transplantation for glycogen storage disease type Ia,” Journal of Hepatology, vol. 51, no. 3, pp. 483–490, 2009. View at Publisher · View at Google Scholar · View at Scopus
  39. P. Labrune, “Glycogen storage disease type I: indications for liver and/or kidney transplantation,” European Journal of Pediatrics, Supplement, vol. 161, no. 1, pp. S53–S55, 2002. View at Publisher · View at Google Scholar · View at Scopus
  40. S. Heng, K. M. Harris, and E. R. Kantrowitz, “Designing inhibitors against fructose 1,6-bisphosphatase: exploring natural products for novel inhibitor scaffolds,” European Journal of Medicinal Chemistry, vol. 45, no. 4, pp. 1478–1484, 2010. View at Publisher · View at Google Scholar · View at Scopus
  41. P. D. V. Poelje, S. C. Potter, and M. D. Erion, “Fructose-1, 6-bisphosphatase inhibitors for reducing excessive endogenous glucose production in type 2 diabetes,” in Diabetes—Perspectives in Drug Therapy, vol. 203 of Handbook of Experimental Pharmacology, pp. 279–301, Springer, Berlin, Germany, 2011. View at Publisher · View at Google Scholar
  42. M. R. El-Maghrabi, A. J. Lange, W. Jiang et al., “Human fructose-1,6-bisphosphatase gene (FBP1): exon-intron organization, localization to chromosome bands 9q22.2-q22.3, and mutation screening in subjects with fructose-1,6-bisphosphatase deficiency,” Genomics, vol. 27, no. 3, pp. 520–525, 1995. View at Publisher · View at Google Scholar · View at Scopus
  43. S. Moon, J.-H. Kim, J.-H. Han et al., “Novel compound heterozygous mutations in the fructose-1,6-bisphosphatase gene cause hypoglycemia and lactic acidosis,” Metabolism: Clinical and Experimental, vol. 60, no. 1, pp. 107–113, 2011. View at Publisher · View at Google Scholar · View at Scopus
  44. A. A. M. Morris, S. Deshpande, M. P. Ward-Platt et al., “Impaired ketogenesis in fructose-1,6-bisphosphatase deficiency: a pitfall in the investigation of hypoglycaemia,” Journal of Inherited Metabolic Disease, vol. 18, no. 1, pp. 28–32, 1995. View at Publisher · View at Google Scholar · View at Scopus
  45. Y. Kikawa, M. Inuzuka, B. Y. Jin et al., “Identification of genetic mutations in Japanese patients with fructose-1,6-bisphosphatase deficiency,” The American Journal of Human Genetics, vol. 61, no. 4, pp. 852–861, 1997. View at Publisher · View at Google Scholar · View at Scopus
  46. M. Faiyaz-Ul-Haque, M. Al-Owain, F. Al-Dayel et al., “Novel FBP1 gene mutations in Arab patients with fructose-1,6-bisphosphatase deficiency,” European Journal of Pediatrics, vol. 168, no. 12, pp. 1467–1471, 2009. View at Publisher · View at Google Scholar · View at Scopus
  47. T. Matsuura, Y. Chinen, R. Arashiro et al., “Two newly identified genomic mutations in a Japanese female patient with fructose-1,6-bisphosphatase (FBPase) deficiency,” Molecular Genetics and Metabolism, vol. 76, no. 3, pp. 207–210, 2002. View at Publisher · View at Google Scholar · View at Scopus
  48. B. Herzog, U. Wendel, A. A. M. Morris, and K. Eschrich, “Novel mutations in patients with fructose-1,6-bisphosphatase deficiency,” Journal of Inherited Metabolic Disease, vol. 22, no. 2, pp. 132–138, 1999. View at Publisher · View at Google Scholar · View at Scopus
  49. P. Prahl, E. Christensen, L. Hansen, and H. B. Mortensen, “Fructose 1,6-bisphosphatase deficiency as a cause of recessive serious hypoglycaemia,” Ugeskrift for Læger, vol. 168, no. 46, pp. 4014–4015, 2006. View at Google Scholar · View at Scopus
  50. L. Baker and A. I. Winegrad, “Fasting hypoglycaemia and metabolic acidosis associated with deficiency of hepatic fructose-1, 6-diphosphatase activity,” The Lancet, vol. 296, no. 7662, pp. 13–16, 1970. View at Publisher · View at Google Scholar · View at Scopus
  51. A. J. M. Janssen and F. J. M. Trijbels, “A new radiochemical assay for fructose-1,6-diphosphatase in human leucocytes,” Clinica Chimica Acta, vol. 119, no. 1-2, pp. 143–148, 1982. View at Publisher · View at Google Scholar · View at Scopus
  52. S. B. Melancon, A. K. Khachadurian, H. L. Nadler, and B. I. Brown, “Metabolic and biochemical studies in fructose 1, 6-diphosphatase deficiency,” The Journal of Pediatrics, vol. 82, no. 4, pp. 650–657, 1973. View at Publisher · View at Google Scholar · View at Scopus
  53. D. H. Solomon, M. C. Raynal, G. A. Tejwani, and Y. E. Cayre, “Activation of the fructose 1,6-bisphosphatase gene by 1,25-dihydroxyvitamin D3 during monocytic differentiation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 85, no. 18, pp. 6904–6908, 1988. View at Google Scholar
  54. D. Alexander, M. Assaf, A. Khudr, I. Haddad, and A. Barakat, “Fructose-1,6-diphosphatase deficiency: diagnosis using leukocytes and detection of heterozygotes with radiochemical and spectrophotometric methods,” Journal of Inherited Metabolic Disease, vol. 8, no. 4, pp. 174–177, 1985. View at Publisher · View at Google Scholar · View at Scopus
  55. A. B. Burlina, M. Poletto, Y. S. Shin, and F. Zacchello, “Clinical and biochemical observations on three cases of fructose-1, 6-diphosphatase deficiency,” Journal of Inherited Metabolic Disease, vol. 13, no. 3, pp. 263–266, 1990. View at Publisher · View at Google Scholar · View at Scopus
  56. Y. Kikawa, T. Takano, A. Nakai et al., “Monocytes, not lymphocytes, show increased fructose-1,6-diphosphatase activity during culture,” Journal of Inherited Metabolic Disease, vol. 16, no. 5, pp. 913–914, 1993. View at Publisher · View at Google Scholar · View at Scopus
  57. “Disorders of fructose metabolism,” in Metabolic and Molecular Bases of Inherited Disease, B. Steinmann, R. Gitzelmann, G. Van den Berghe, C. R. Scriver, A. L. Beaudet, and W. S. D. V. Sly, Eds., pp. 1489–1520, McGraw-Hill, New York, NY, USA, 2001.
  58. P. D. van Poelje, Q. Dang, and M. D. Erion, “Fructose-1,6-bisphosphatase as a therapeutic target for type 2 diabetes,” Drug Discovery Today: Therapeutic Strategies, vol. 4, no. 2, pp. 103–109, 2007. View at Publisher · View at Google Scholar · View at Scopus
  59. M. D. Erion, P. D. Van Poelje, Q. Dang et al., “MB06322 (CS-917): a potent and selective inhibitor of fructose 1,6-bisphosphatase for controlling gluconeogenesis in type 2 diabetes,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 22, pp. 7970–7975, 2005. View at Publisher · View at Google Scholar · View at Scopus
  60. P. D. van Poelje, S. C. Potter, V. C. Chandramouli, B. R. Landau, Q. Dang, and M. D. Erion, “Inhibition of fructose 1,6-bisphosphatase reduces excessive endogenous glucose production and attenuates hyperglycemia in Zucker diabetic fatty rats,” Diabetes, vol. 55, no. 6, pp. 1747–1754, 2006. View at Publisher · View at Google Scholar · View at Scopus
  61. R. Stark and R. G. Kibbey, “The mitochondrial isoform of phosphoenolpyruvate carboxykinase (PEPCK-M) and glucose homeostasis: has it been overlooked?” Biochimica et Biophysica Acta (BBA)—General Subjects, vol. 1840, no. 4, pp. 1313–1330, 2014. View at Publisher · View at Google Scholar · View at Scopus
  62. S. Modaressi, K. Brechtel, B. Christ, and K. Jungermann, “Human mitochondrial phosphoenolpyruvate carboxykinase 2 gene. Structure, chromosomal localization and tissue-specific expression,” Biochemical Journal, vol. 333, no. 2, pp. 359–366, 1998. View at Publisher · View at Google Scholar · View at Scopus
  63. L. Reshef, R. W. Hanson, and F. J. Ballard, “A possible physiological role for glyceroneogenesis in rat adipose tissue,” The Journal of Biological Chemistry, vol. 245, no. 22, pp. 5979–5984, 1970. View at Google Scholar · View at Scopus
  64. S. C. Kalhan, S. Mahajan, E. Burkett, L. Reshef, and R. W. Hanson, “Glyceroneogenesis and the source of glycerol for hepatic triacylglycerol synthesis in humans,” The Journal of Biological Chemistry, vol. 276, no. 16, pp. 12928–12931, 2001. View at Publisher · View at Google Scholar · View at Scopus
  65. P. Hakimi, M. T. Johnson, J. Yang et al., “Phosphoenolpyruvate carboxykinase and the critical role of cataplerosis in the control of hepatic metabolism,” Nutrition and Metabolism, vol. 2, article 33, 2005. View at Publisher · View at Google Scholar · View at Scopus
  66. C.-W. Hsieh, C. Huang, I. Bederman et al., “Function of phosphoenolpyruvate carboxykinase in mammary gland epithelial cells,” Journal of Lipid Research, vol. 52, no. 7, pp. 1352–1362, 2011. View at Publisher · View at Google Scholar · View at Scopus
  67. R. K. Ball, R. R. Friis, C. A. Schoenenberger, W. Doppler, and B. Groner, “Prolactin regulation of beta-casein gene expression and of a cytosolic 120-kd protein in a cloned mouse mammary epithelial cell line,” The EMBO Journal, vol. 7, no. 7, pp. 2089–2095, 1988. View at Google Scholar · View at Scopus
  68. R. W. Hanson, “Thematic minireview series: a perspective on the biology of phosphoenolpyruvate carboxykinase 55 years after its discovery,” The Journal of Biological Chemistry, vol. 284, no. 40, pp. 27021–27023, 2009. View at Publisher · View at Google Scholar · View at Scopus
  69. M. Adeva-Andany, M. López-Ojén, R. Funcasta-Calderón et al., “Comprehensive review on lactate metabolism in human health,” Mitochondrion, vol. 17, pp. 76–100, 2014. View at Publisher · View at Google Scholar · View at Scopus
  70. S. Chandran, F. Yap, and K. Hussain, “Genetic disorders leading to hypoglycaemia,” Journal of Genetic Syndromes & Gene Therapy, vol. 4, article 192, 2013. View at Publisher · View at Google Scholar
  71. B. H. Robinson, N. MacKay, K. Chun, and M. Ling, “Disorders of pyruvate carboxylase and the pyruvate dehydrogenase complex,” Journal of Inherited Metabolic Disease, vol. 19, no. 4, pp. 452–462, 1996. View at Publisher · View at Google Scholar · View at Scopus
  72. R. E. Frye and P. J. Benke, “Pyruvate Dehydrogenase Complex Deficiency,” 2014, http://emedicine.medscape.com/article/948360-overview.
  73. B. H. Robinson, K. Chun, N. Mackay, G. Otulakowski, R. Petrova-Benedict, and H. Willard, “Isolated and combined deficiencies of the alpha-keto acid dehydrogenase complexes,” Annals of the New York Academy of Sciences, vol. 573, pp. 337–346, 1989. View at Publisher · View at Google Scholar · View at Scopus
  74. G. K. Brown, R. M. Brown, R. D. Scholem, D. M. Kirby, and H.-H. M. Dahl, “The clinical and biochemical spectrum of human pyruvate dehydrogenase complex deficiency,” Annals of the New York Academy of Sciences, vol. 573, pp. 360–368, 1989. View at Publisher · View at Google Scholar · View at Scopus
  75. M. S. Patel and T. E. Roche, “Molecular biology and biochemistry of pyruvate dehydrogenase complexes,” The FASEB Journal, vol. 4, no. 14, pp. 3224–3233, 1990. View at Google Scholar · View at Scopus
  76. B. H. Robinson, N. MacKay, K. Chun, and M. Ling, “Disorders of pyruvate carboxylase and the pyruvate dehydrogenase complex,” Journal of Inherited Metabolic Disease, vol. 19, no. 4, pp. 452–462, 1996. View at Publisher · View at Google Scholar · View at Scopus
  77. D. S. Kerr, I. D. Wexler, A. Tripatara, and M. S. Patel, “Defects of the human pyruvate dehydrogenase complex,” in Alpha Keto Acid Dehydrogenase Complexes, M. S. Patel, T. Roche, and R. A. Harris, Eds., pp. 249–270, Birkhäuser, Basel, Switzerland, 1996. View at Google Scholar
  78. L. J. Otero, R. M. Brown, and G. K. Brown, “Arginine 302 mutations in the pyruvate dehydrogenase E1α subunit gene: identification of further patients and in vitro demonstration of pathogenicity,” Human Mutation, vol. 12, no. 2, pp. 114–121, 1998. View at Google Scholar
  79. J. Steller, J. J. Gargus, L. H. Gibbs, A. N. Hasso, and V. E. Kimonis, “Mild phenotype in a male with pyruvate dehydrogenase complex deficiency associated with novel hemizygous in-frame duplication of the e1α subunit gene (PDHA1),” Neuropediatrics, vol. 45, no. 1, pp. 56–60, 2014. View at Publisher · View at Google Scholar · View at Scopus
  80. J. Fernandes, J. M. Saudubray, G. V. D. Berghe, and J. H. Walter, Inborn Metabolic Diseases: Diagnosis and Treatment, Springer Medizin, Heidelberg, Germany, 2006.
  81. K. P. Patel, T. W. O'Brien, S. H. Subramony, J. Shuster, and P. W. Stacpoole, “The spectrum of pyruvate dehydrogenase complex deficiency: clinical, biochemical and genetic features in 371 patients,” Molecular Genetics and Metabolism, vol. 105, no. 1, pp. 34–43, 2012. View at Publisher · View at Google Scholar · View at Scopus
  82. G. K. Brown, L. J. Otero, M. LeGris, and R. M. Brown, “Pyruvate dehydrogenase deficiency,” Journal of Medical Genetics, vol. 31, no. 11, pp. 875–879, 1994. View at Publisher · View at Google Scholar · View at Scopus
  83. C. Bardella, P. J. Pollard, and I. Tomlinson, “SDH mutations in cancer,” Biochimica et Biophysica Acta—Bioenergetics, vol. 1807, no. 11, pp. 1432–1443, 2011. View at Publisher · View at Google Scholar · View at Scopus
  84. P. Heutink, A. G. L. van der Mey, L. A. Sandkuijl et al., “A gene subject to genomic imprinting and responsible for hereditary paragangliomas maps to chromosome 11q23-qter,” Human Molecular Genetics, vol. 1, no. 1, pp. 7–10, 1992. View at Publisher · View at Google Scholar · View at Scopus
  85. B. E. Baysal, J. E. Farr, W. S. Rubinstein et al., “Fine mapping of an imprinted gene for familial nonchromaffin paragangliomas, on chromosome 11q23,” American Journal of Human Genetics, vol. 60, no. 1, pp. 121–132, 1997. View at Google Scholar · View at Scopus
  86. T. Bourgeron, D. Chretien, J. Poggi-Bach et al., “Mutation of the fumarase gene in two siblings with progressive encephalopathy and fumarase deficiency,” The Journal of Clinical Investigation, vol. 93, no. 6, pp. 2514–2518, 1994. View at Publisher · View at Google Scholar · View at Scopus
  87. B. E. Baysal, J. E. Willett-Brozick, E. C. Lawrence et al., “Prevalence of SDHB, SDHC, and SDHD germline mutations in clinic patients with head and neck paragangliomas,” Journal of Medical Genetics, vol. 39, no. 3, pp. 178–183, 2002. View at Publisher · View at Google Scholar · View at Scopus
  88. P. J. Pollard, N. C. Wortham, and I. P. M. Tomlinson, “The TCA cycle and tumorigenesis: the examples of fumarate hydratase and succinate dehydrogenase,” Annals of Medicine, vol. 35, no. 8, pp. 632–639, 2003. View at Google Scholar · View at Scopus
  89. N. Burnichon, J.-J. Brière, R. Libé et al., “SDHA is a tumor suppressor gene causing paraganglioma,” Human Molecular Genetics, vol. 19, no. 15, pp. 3011–3020, 2010. View at Publisher · View at Google Scholar · View at Scopus
  90. H.-X. Hao, O. Khalimonchuk, M. Schraders et al., “SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma,” Science, vol. 325, no. 5944, pp. 1139–1142, 2009. View at Publisher · View at Google Scholar · View at Scopus
  91. S. Rahman, R. B. Blok, H.-H. M. Dahl et al., “Leigh syndrome: clinical features and biochemical and DNA abnormalities,” Annals of Neurology, vol. 39, no. 3, pp. 343–351, 1996. View at Publisher · View at Google Scholar · View at Scopus
  92. M. H. Rivner, M. Shamsnia, T. R. Swift et al., “Kearns-Sayre syndrome and complex II deficiency,” Neurology, vol. 39, no. 5, pp. 693–696, 1989. View at Publisher · View at Google Scholar · View at Scopus
  93. M. Deschauer, Z. Gizatullina, A. Schulze et al., “Molecular and biochemical investigations in fumarase deficiency,” Molecular Genetics and Metabolism, vol. 88, no. 2, pp. 146–152, 2006. View at Publisher · View at Google Scholar · View at Scopus
  94. T. Suzuki, M. Sato, T. Yoshida, and S. Tuboi, “Rat liver mitochondrial and cytosolic fumarases with identical amino acid sequences are encoded from a single gene,” The Journal of Biological Chemistry, vol. 264, no. 5, pp. 2581–2586, 1989. View at Google Scholar · View at Scopus
  95. C. Ottolenghi, L. Hubert, Y. Allanore et al., “Clinical and biochemical heterogeneity associated with fumarase deficiency,” Human Mutation, vol. 32, no. 9, pp. 1046–1052, 2011. View at Publisher · View at Google Scholar · View at Scopus
  96. E. M. Coughlin, E. Christensen, P. L. Kunz et al., “Molecular analysis and prenatal diagnosis of human fumarase deficiency,” Molecular Genetics and Metabolism, vol. 63, no. 4, pp. 254–262, 1998. View at Publisher · View at Google Scholar · View at Scopus
  97. J. Loeffen, R. Smeets, T. Voit, G. Hoffmann, and J. Smeitink, “Fumarase deficiency presenting with periventricular cysts,” Journal of Inherited Metabolic Disease, vol. 28, no. 5, pp. 799–800, 2005. View at Publisher · View at Google Scholar · View at Scopus
  98. N. A. Alam, A. J. Rowan, N. C. Wortham et al., “Genetic and functional analyses of FH mutations in multiple cutaneous and uterine leiomyomatosis, hereditary leiomyomatosis and renal cancer, and fumarate hydratase deficiency,” Human Molecular Genetics, vol. 12, no. 11, pp. 1241–1252, 2003. View at Publisher · View at Google Scholar · View at Scopus
  99. A. M. Remes, S. A. Filppula, H. Rantala et al., “A novel mutation of the fumarase gene in a family with autosomal recessive fumarase deficiency,” Journal of Molecular Medicine, vol. 82, no. 8, pp. 550–554, 2004. View at Publisher · View at Google Scholar · View at Scopus
  100. J. Zeman, J. Krijt, L. Stratilová et al., “Abnormalities in succinylpurines in fumarase deficiency: possible role in pathogenesis of CNS impairment,” Journal of Inherited Metabolic Disease, vol. 23, no. 4, pp. 371–374, 2000. View at Publisher · View at Google Scholar · View at Scopus
  101. I. P. M. Tomlinson, N. A. Alam, A. J. Rowan et al., “Germline mutations in FH predispose to dominantly inherited uterine fibroids, skin leiomyomata and papillary renal cell cancer the multiple leiomyoma consortium,” Nature Genetics, vol. 30, no. 4, pp. 406–410, 2002. View at Publisher · View at Google Scholar · View at Scopus
  102. P. Rustin and A. Rötig, “Inborn errors of complex II—unusual human mitochondrial diseases,” Biochimica et Biophysica Acta (BBA)—Bioenergetics, vol. 1553, no. 1-2, pp. 117–122, 2002. View at Publisher · View at Google Scholar · View at Scopus
  103. J. R. Toro, M. L. Nickerson, M.-H. Wei et al., “Mutations in the fumarate hydratase gene cause hereditary leiomyomatosis and renal cell cancer in families in North America,” The American Journal of Human Genetics, vol. 73, no. 1, pp. 95–106, 2003. View at Publisher · View at Google Scholar · View at Scopus
  104. E. Beutler, “G6PD deficiency,” Blood, vol. 84, no. 11, pp. 3613–3636, 1994. View at Google Scholar · View at Scopus
  105. P. J. Mason, J. M. Bautista, and F. Gilsanz, “G6PD deficiency: the genotype-phenotype association,” Blood Reviews, vol. 21, no. 5, pp. 267–283, 2007. View at Publisher · View at Google Scholar · View at Scopus
  106. L. Luzzatto, T. J. Vulliamy, and A. Mehta, “Glucose 6-phosphate dehydrogenase deficiency,” in The Metabolic and Molecular Bases of Inherited Disease, pp. 4517–4553, McGraw Hill, 2001. View at Google Scholar
  107. J. E. Frank, “Diagnosis and management of G6PD deficiency,” American Family Physician, vol. 72, no. 7, pp. 1277–1282, 2005. View at Google Scholar · View at Scopus
  108. C. J. Sutherland, N. Tanomsing, D. Nolder et al., “Two non recombining sympatric forms of the human malaria parasite Plasmodium ovale occur globally,” The Journal of Infectious Diseases, vol. 201, no. 10, pp. 1544–1550, 2010. View at Publisher · View at Google Scholar
  109. M. R. N. Daloii, Z. Hajebrahimi, and L. Najafi, “Molecular identification of the most prevalent mutation of glucose-6-phosphate dehydrogenase gene in deficient patients in Gilan province,” Journal of Sciences, Islamic Republic of Iran, vol. 14, pp. 327–331, 2003. View at Google Scholar
  110. A. Dallol, H. Banni, M. A. Gari et al., “Five novel glucose-6-phosphate dehydrogenase deficiency haplotypes correlating with disease severity,” Journal of Translational Medicine, vol. 10, article 199, 2012. View at Publisher · View at Google Scholar · View at Scopus
  111. N. Laouini, A. Bibi, H. Ammar et al., “Glucose-6-phosphate dehydrogenase deficiency in Tunisia: molecular data and phenotype-genotype association,” Molecular Biology Reports, vol. 40, no. 2, pp. 851–856, 2013. View at Publisher · View at Google Scholar · View at Scopus
  112. M. Cappellini and G. Fiorelli, “Glucose-6-phosphate dehydrogenase deficiency,” The Lancet, vol. 371, no. 9606, pp. 64–74, 2008. View at Publisher · View at Google Scholar · View at Scopus
  113. M. M. C. Wamelink, E. A. Struys, and C. Jakobs, “The biochemistry, metabolism and inherited defects of the pentose phosphate pathway: a review,” Journal of Inherited Metabolic Disease, vol. 31, no. 6, pp. 703–717, 2008. View at Publisher · View at Google Scholar · View at Scopus
  114. J. H. J. Huck, N. M. Verhoeven, E. A. Struys, G. S. Salomons, C. Jakobs, and M. S. Van Der Knaap, “Ribose-5-phosphate isomerase deficiency: new inborn error in the pentose phosphate pathway associated with a slowly progressive leukoencephalopathy,” American Journal of Human Genetics, vol. 74, no. 4, pp. 745–751, 2004. View at Publisher · View at Google Scholar · View at Scopus
  115. M. M. Wamelink, E. A. Struys, G. S. Salomons, D. Fowler, C. Jakobs, and P. T. Clayton, “Transaldolase deficiency in a two-year-old boy with cirrhosis,” Molecular Genetics and Metabolism, vol. 94, no. 2, pp. 255–258, 2008. View at Publisher · View at Google Scholar · View at Scopus
  116. S. Thorell, P. Gergely Jr., K. Banki, A. Perl, and G. Schneider, “The three-dimensional structure of human transaldolase,” FEBS Letters, vol. 475, no. 3, pp. 205–208, 2000. View at Publisher · View at Google Scholar · View at Scopus
  117. C. W. Fung, S. Siu, C. Mak et al., “A rare cause of hepatosplenomegaly-transaldolase deficiency,” Journal of Inherited Metabolic Disease, vol. 30, supplement 1, article 62, 2007. View at Google Scholar
  118. V. Valayannopoulos, N. M. Verhoeven, K. Mention et al., “Transaldolase deficiency: a new cause of hydrops fetalis and neonatal multi-organ disease,” Journal of Pediatrics, vol. 149, no. 5, pp. 713–717, 2006. View at Publisher · View at Google Scholar · View at Scopus
  119. N. M. Verhoeven, M. Wallot, J. H. J. Huck et al., “A newborn with severe liver failure, cardiomyopathy and transaldolase deficiency,” Journal of Inherited Metabolic Disease, vol. 28, no. 2, pp. 169–179, 2005. View at Publisher · View at Google Scholar · View at Scopus
  120. E. Schmidt, J.-M. Nuoffer, J. Häberle et al., “Identification of novel mutations of the human N-acetylglutamate synthase gene and their functional investigation by expression studies,” Biochimica et Biophysica Acta (BBA)—Molecular Basis of Disease, vol. 1740, no. 1, pp. 54–59, 2005. View at Publisher · View at Google Scholar · View at Scopus
  121. C. Bachmann, S. Krähenbühl, J. P. Colombo, G. Schubiger, K. H. Jaggi, and O. Tönz, “N-acetylglutamate synthetase deficiency: a disorder of ammonia detoxication,” The New England Journal of Medicine, vol. 304, no. 9, pp. 543–345, 1981. View at Google Scholar · View at Scopus
  122. A. J. Meijer, C. Lof, I. C. Ramos, and A. J. Verhoeven, “Control of ureogenesis,” European Journal of Biochemistry, vol. 148, no. 1, pp. 189–196, 1985. View at Publisher · View at Google Scholar · View at Scopus
  123. N. A. Mew and L. Caldovic, “N-acetylglutamate synthase deficiency: an insight into the genetics, epidemiology, pathophysiology, and treatment,” The Application of Clinical Genetics, vol. 4, pp. 127–135, 2011. View at Google Scholar
  124. L. Caldovic, H. Morizono, M. G. Panglao et al., “Late onset N-acetylglutamate synthase deficiency caused by hypomorphic alleles,” Human Mutation, vol. 25, no. 3, pp. 293–298, 2005. View at Publisher · View at Google Scholar · View at Scopus
  125. C. Bachmann, M. Brandis, E. Weissenbarth-Riedel, R. Burghard, and J. P. Colombo, “Nacetylglutamate synthetase deficiency, a second patient,” Journal of Inherited Metabolic Disease, vol. 11, pp. 191–193, 1988. View at Google Scholar
  126. L. Caldovic, H. Morizono, M. G. Panglao, S. F. Cheng, S. Packman, and M. Tuchman, “Null mutations in the N-acetylglutamate synthase gene associated with acute neonatal disease and hyperammonemia,” Human Genetics, vol. 112, no. 4, pp. 364–368, 2003. View at Google Scholar · View at Scopus
  127. L. Caldovic, N. Ah Mew, D. Shi, H. Morizono, M. Yudkoff, and M. Tuchman, “N-acetylglutamate synthase: structure, function and defects,” Molecular Genetics and Metabolism, vol. 100, supplement, pp. S13–S19, 2010. View at Publisher · View at Google Scholar · View at Scopus
  128. M. Heckmann, B. Wermuth, J. Häberle, H. G. Koch, L. Gortner, and J. G. Kreuder, “Misleading diagnosis of partial N-acetylglutamate synthase deficiency based on enzyme measurement corrected by mutation analysis,” Acta Paediatrica, vol. 94, no. 1, pp. 121–124, 2005. View at Publisher · View at Google Scholar · View at Scopus
  129. W.-L. Hwu, Y.-H. Chien, N. L. Tang, L.-K. Law, C.-Y. Lin, and N.-C. Lee, “Deficiency of the carnitine transporter (OCTN2) with partial N-acetylglutamate synthase (NAGS) deficiency,” Journal of Inherited Metabolic Disease, vol. 30, no. 5, article 816, 2007. View at Publisher · View at Google Scholar · View at Scopus
  130. J. Häberle, E. Schmidt, S. Pauli et al., “Mutation analysis in patients with N-acetylglutamate synthase deficiency,” Human Mutation, vol. 21, no. 6, pp. 593–597, 2003. View at Publisher · View at Google Scholar · View at Scopus
  131. L. Caldovic, N. A. Mew, D. Shi, H. Morizono, M. Yudkoff, and M. Tuchman, “N-acetylglutamate synthase: structure, function and defects,” Molecular Genetics and Metabolism, vol. 100, pp. S13–S19, 2010. View at Publisher · View at Google Scholar · View at Scopus
  132. G. M. Enns, S. A. Berry, G. T. Berry, W. J. Rhead, S. W. Brusilow, and A. Hamosh, “Survival after treatment with phenylacetate and benzoate for urea-cycle disorders,” The New England Journal of Medicine, vol. 356, no. 22, pp. 2282–2292, 2007. View at Publisher · View at Google Scholar · View at Scopus
  133. S. Banka, R. Wynn, and W. G. Newman, “Variability of bone marrow morphology in G6PC3 mutations: is there a genotype-phenotype correlation or age-dependent relationship?” American Journal of Hematology, vol. 86, no. 2, pp. 235–237, 2011. View at Publisher · View at Google Scholar · View at Scopus
  134. A. Dursun, R. K. Ozgul, A. Soydas et al., “Familial pulmonary arterial hypertension, leucopenia, and atrial septal defect: a probable new familial syndrome with multisystem involvement,” Clinical Dysmorphology, vol. 18, no. 1, pp. 19–23, 2009. View at Publisher · View at Google Scholar · View at Scopus
  135. M. Germeshausen, C. Zeidler, M. Stuhrmann, M. Lanciotti, M. Ballmaier, and K. Welte, “Digenic mutations in severe congenital neutropenia,” Haematologica, vol. 95, no. 7, pp. 1207–1210, 2010. View at Publisher · View at Google Scholar · View at Scopus
  136. C. Aytekin, M. Germeshausen, N. Tuygun, F. Dogu, and A. Ikinciogullari, “A novel G6PC3 gene mutation in a patient with severe congenital neutropenia,” Journal of Pediatric Hematology/Oncology, vol. 35, no. 2, pp. e81–e83, 2013. View at Publisher · View at Google Scholar · View at Scopus
  137. K. Boztug, G. Appaswamy, A. Ashikov et al., “A syndrome with congenital neutropenia and mutations in G6PC3,” The New England Journal of Medicine, vol. 360, no. 1, pp. 32–43, 2009. View at Publisher · View at Google Scholar · View at Scopus
  138. B. N. Smith, C. Evans, A. Ali et al., “Phenotypic heterogeneity and evidence of a founder effect associated with G6PC3 mutations in patients with severe congenital neutropenia,” British Journal of Haematology, vol. 158, no. 1, pp. 146–149, 2012. View at Publisher · View at Google Scholar · View at Scopus
  139. K. Boztug, P. S. Rosenberg, M. Dorda et al., “Extended spectrum of human glucose-6-phosphatase catalytic subunit 3 deficiency: novel genotypes and phenotypic variability in severe congenital neutropenia,” Journal of Pediatrics, vol. 160, no. 4, pp. 679–e2, 2012. View at Publisher · View at Google Scholar · View at Scopus
  140. B. Hayee, A. Antonopoulos, E. J. Murphy et al., “G6PC3 mutations are associated with a major defect of glycosylation: a novel mechanism for neutrophil dysfunction,” Glycobiology, vol. 21, no. 7, pp. 914–924, 2011. View at Publisher · View at Google Scholar · View at Scopus
  141. D. H. McDermott, S. S. De Ravin, H. S. Jun et al., “Severe congenital neutropenia resulting from G6PC3 deficiency with increased neutrophil CXCR4 expression and myelokathexis,” Blood, vol. 116, no. 15, pp. 2793–2802, 2010. View at Publisher · View at Google Scholar · View at Scopus
  142. J. Xia, A. A. Bolyard, E. Rodger et al., “Prevalence of mutations in ELANE, GFI1, HAX1, SBDS, WAS and G6PC3 in patients with severe congenital neutropenia,” British Journal of Haematology, vol. 147, no. 4, pp. 535–542, 2009. View at Publisher · View at Google Scholar · View at Scopus
  143. M. Graille, P. Meyer, N. Leulliot et al., “Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archaeal and bacterial enzymes,” Biochimie, vol. 87, no. 8, pp. 763–769, 2005. View at Publisher · View at Google Scholar · View at Scopus
  144. L. Amar, J. Bertherat, E. Baudin et al., “Genetic testing in pheochromocytoma or functional paraganglioma,” Journal of Clinical Oncology, vol. 23, no. 34, pp. 8812–8818, 2005. View at Publisher · View at Google Scholar · View at Scopus
  145. F. Schiavi, C. C. Boedeker, B. Bausch et al., “Predictors and prevalence of paraganglioma syndrome associated with mutations of the SDHC gene,” The Journal of the American Medical Association, vol. 294, no. 16, pp. 2057–2063, 2005. View at Publisher · View at Google Scholar
  146. M. Town, J. M. Bautista, P. J. Mason, and L. Luzzatto, “Both mutations in G6PD A—are necessary to produce the G6PD deficient phenotype,” Human Molecular Genetics, vol. 1, no. 3, pp. 171–174, 1992. View at Publisher · View at Google Scholar · View at Scopus
  147. S. Despoisses, L. Noel, A. Choiset et al., “Regional mapping of FH to band 1q42.1 by gene dosage studies,” Cytogenetics and Cell Genetics, vol. 37, pp. 450–451, 1984. View at Google Scholar
  148. C. Barnerias, J.-M. Saudubray, G. Touati et al., “Pyruvate dehydrogenase complex deficiency: four neurological phenotypes with differing pathogenesis,” Developmental Medicine and Child Neurology, vol. 52, no. 2, pp. e1–e9, 2010. View at Publisher · View at Google Scholar · View at Scopus
  149. W. Lissens, L. De Meirleir, S. Seneca et al., “Mutations in the X-linked pyruvate dehydrogenase (E1) alpha subunit gene (PDHA1) in patients with a pyruvate dehydrogenase complex deficiency,” Human Mutation, vol. 15, pp. 209–219, 2000. View at Publisher · View at Google Scholar
  150. O. Elpeleg, A. Shaag, E. Ben-Shalom, T. Schmid, and C. Bachmann, “N-acetylglutamate synthase deficiency and the treatment of hyperammonemic encephalopathy,” Annals of Neurology, vol. 52, no. 6, pp. 845–849, 2002. View at Publisher · View at Google Scholar · View at Scopus