Biochemistry and autoimmune response to the 2-oxoacid dehydrogenase complexes in primary biliary cirrhosis

Seminars in Liver Disease

Volumn 17, Issue 1, 1997, Pages 49-60

  Bassendine, Margaret F ^a   Jones, David E J ^a   Yeaman, Stephen J ^a  

^a NEWCASTLE UNIVERSITY   (United Kingdom)

Author keywords

autoantibody; autoimmunity; biliary; liver cirrhosis; pyruvate dehydrogenase complex; T lymphocyte

Indexed keywords

2 OXOACID DEHYDROGENASE; AUTOANTIGEN; DIHYDROLIPOAMIDE ACETYLTRANSFERASE; PYRUVATE DEHYDROGENASE;

AEROBIC METABOLISM; ANTIBODY SPECIFICITY; ARTICLE; AUTOIMMUNITY; BIOCHEMISTRY; COMPLEX FORMATION; ENZYME ACTIVITY; HUMAN; IMMUNE RESPONSE; IMMUNOTHERAPY; PRIMARY BILIARY CIRRHOSIS; PRIORITY JOURNAL; T LYMPHOCYTE ACTIVATION;

EID: 0030905186     PISSN: 02728087     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-2007-1007182     Document Type: Article

References (99)

1. Mitchison HC, Bassendine MF, Hendnck AM, et al: Positive antimitochondrial antibody but normal liver function tests: is this primary biliary cirrhosis? Hepatology 6.1279-84, 1986.
2. Perham RN: Interaction of protein domains in the assembly of 2-oxoacid dehydrogenases. In: Patel MS, Roche TE, Harris RA (eds): Alpha-keto acid dehydrogenase complexes. Basel, Birkhauser Verlag, 1996, pp 1-15.
3. Popov KM, Kedishvili NY, Zhao Y, et al: Primary structure of pyruvate dehydrogenase kinase establishes a new family of eukaryotic protein kinases. J Biol Chem 268:26602-6, 1993.
4. Popov KM, Kedishvili NY, Zhao Y, et al: Molecular cloning of the p45 subunit of pyruvate dehydrogenase kinase. J Biol Chem 269:29720-4, 1994.
5. Popov KM, Zhao Y, Shimomura Y, et al: Branched-chain α-ketoacid dehydrogenase kinase. J Biol Chem 267:13127-30, 1992.
6. Lawson JE, Nui X-D, Browning KS, et al: Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C. Biochemistry 32:8987-93, 1993.
7. De Marcucci OGL, Lindsay JG: Component X. An immunologically distinct polypeptide associated with mammalian pyruvate dehydrogenase multi-enzyme complex. Eur J Biochem 149:641-8, 1985.
8. Jilka JM, Rahmatullah M, Kazemi M, et al: Properties of a newly characterised protein of the bovine kidney pyruvate dehydrogenase complex. J Biol Chem 261:1858-67, 1986.
9. Behal RH, Browning KS, Hall TB, et al: Cloning and nucleotide sequence of the gene for protein X from Saccharomyces cerevisiae. Proc Natl Acad Sci 86:8732-6, 1989.
10. De Marcucci OGL, Gibb JM, Dick J, et al: Biosynthesis, import and processing of precursor polypeptides of mammalian mitochondrial pyruvate dehydrogenase complex. Biochem J 251: 817-23, 1988.
11. Patel M, Harris RA Mammalian α-keto acid dehydrogenase complexes: gene regulation and genetic defects. FASEB J 9:1164-72, 1995.
12. Fussey SPM, Guest JR, James OFW, et al: Identification and analysis of the major M2 autoantigens in primary biliary cirrhosis. Proc Natl Acad Sci 85:8654-8, 1988.
13. Brown RM, Dahl H-HM, Brown GK X-chromosome localization of the functional gene for the E1α subunit of the human pyruvate dehydrogenase complex. Genomics 4:174-81, 1989.
14. Danner DJ, Armstrong N, Heffelfinger SC, et al: Absence of branched-chain acyl-transferase as a cause of maple syrup urine disease. J Clin Invest 75:858-60, 1985.
15. Stephens PE, Darlison MG, Lewis HM, et al: The pyruvate dehydrogenase complex of Escherichia cou K12. Eur J Biochem 133:481-9, 1983.
16. Graham LD, Guest JR, Lewis HM, et al: The pyruvate dehydrogenase multi-enzyme complex of Escherichia coli: genetic reconstruction and functional analysis of the lipoyl domains. Phil Trans R Soc Lond A 317:391-404, 1986
17. Mattevi A, Obmolova G, Schulze E, et al: Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex. Science 255:1544-50, 1992.
18. Guest JR: Functional implications of structural homologies between chloramphenicol acetyltransferase and dihydrolipoamide acetyltransferase. FEMS Microbiol Lett 44:417-22, 1987.
19. Davis AL, Laue ED, Perham RN: Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex. J Mol Biol 229: 1037-48, 1993.
20. Green JDF, Laue ED, Perham RN, et al: Three-dimensional structure of a lipoyl domain from the dihydrolipoyl acetyltransferase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli. J Mol Biol 248:328-43, 1995.
21. Motokawa Y, Fujiwara K, Okamura-Ikeda K: Lipoylation of E2 component in alpha-keto acid dehydrogenase complexes. In: Patel MS, Roche TE, Harris RA (eds): Alpha-keto acid dehydrogenase complexes. Basel. Birkhauser Verlag, 1996, pp 119-30.
22. Maeng C-Y, Yazdi MA, Niu X-D, et al: Expression, purification and characterisation of the dihydrolipoamide dehydrogenase-binding protein of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae. Biochem 33:13801-7, 1994
23. r-50000 polypeptide of mammalian pyruvate dehydrogenase complex participates in the acetylation reactions. Eur J Biochem 158:587-94, 1986.
24. Sanderson SJ, Miller C, Lindsay JG: Stoichiometry, organisation and catalytic function of protein X of the pyruvate dehydrogenase complex from bovine heart. Eur J Biochem 236: 68-77, 1996.
25. Gershwin ME, Mackay IR, Sturgess A, Coppel RL: Identification and specificity of a cDNA encoding the 70 KDa mitochondrial antigen recognised in primary biliary cirrhosis. J Immunol 138:3525-31, 1987.
26. Coppel RL, McNeilage LJ, Surh CD, et al: Primary structure of the human M2 mitochondrial autoantigen of primary biliary cirrhosis. dihydrolipoamide acetyltransferase. Proc Natl Acad Sci USA 85:7317-21, 1988.
27. Yeaman SJ, Fussey SPM, Danner DJ, et al: Primary biliary cirrhosis: identification of two major M2 mitochondrial autoantigens. Lancet i: 1067-70, 1988.
28. Van de Water J, Gershwin ME, Leung P, Coppel R: The autoepitope of the 74 KD mitochondrial autoantigen of primary biliary cirrhosis corresponds to the functional site of dihydrolipoamide acetyltransferase J Exp Med 167:1791-9, 1988
29. Mutimer DJ, Fussey SPM, Yeaman SJ, et al: Frequency of IgG and IgM autoantibodies to four specific M2 mitochondrial autoantigens in primary biliary cirrhosis. Hepatology 10:403-7, 1989.
30. Van de Water J, Fregeau D, Davis P, et al: Autoantibodies of primary biliary cirrhosis recognise dihydrolipoamide acetyltransferase and inhibit enzyme function. J Immunol 141:2321-4, 1988.
31. Fussey SPM, Ali ST, Guest JR, et al: Reactivity of primary biliary cirrhosis sera with Escherichia coli dihydrolipoamide acetyltransferase (E2p). characterisation of the main immunogenic region. Proc Natl Acad Sci 87:3987-91, 1990.
32. Fussey SPM, Bassendine MF, James OFW, Yeaman SJ. Characterisation of the reactivity of autoantibodies in primary biliary cirrhosis. FEBS Lett 246:49-53, 1989.
33. Fraser CM, Gocayne JD, White O, et al: The minimal gene complement of Mycoplasma genitalium Science 270:397-403, 1995
34. Guan Y, Rawsthorne S, Scofield G, et al: Cloning and characterisation of a dihydrolipoamide acetyltransferase (E2) subunit of the pyruvate dehydiogenase complex from Arabidopsis thaliana. J Biol Chem 270:5412-17, 1995.
35. Lindenborn-Fotinos J, Baum H, Berg PA: Mitochondrial antibodies in primary biliary cirrhosis. species and non-species specific determinants of M2 antigens. Hepatology 5.763-9, 1985.
36. Fussey SPM, Lindsay JG, Fuller C, et al: Autoantibodies in primary biliary cirrhosis: analysis of reactivity against eukaryotic and prokaryotic 2-oxoacid dehydrogenase complexes. Hepatology 13:467-74, 1991.
37. Fussey SPM, West SM, Lindsay JG, et al: Clarification of the identity of the major M2 autoantigen in primary biliary cirrhosis. Clin Sci 80:451-5, 1991.
38. Teoh KL, Mackay IR, Rowley MJ, Fussey SPM: Enzyme inhibitory autoantibodies to pyruvate dehydrogenase complex in primary biliary cirrhosis differ for mammalian, yeast and bacterial enzymes: implications for molecular mimicry. Hepatology 19:1029-33, 1994.
39. Vilagut L, Vila J, Vinas O, et al: Cross-reactivity of anti-Mycobacterium gordonae antibodies with the major mitochondrial autoantigens in primary biliary cirrhosis. J Hepatol 21:673-7, 1994
40. Stemerowicz R, Hopf U, Moller B, et al: Are mitochondrial antibodies in primary biliary cirrhosis induced by R(rough)-mutants of enterobacteriaceae? Lancet ii 1166-9, 1988.
41. Heseltine L, Turner IB, Fussey SPM, et al: Primary biliary cirrhosis: quantitation of autoantibodies to purified mitochondrial enzymes and correlation with disease progression. Gastroenterology 99:1786-92, 1990.
42. Palmer JM, Bassendine MF, James OFW, Yeaman SJ: Human pyruvate dehydrogenase complex as an autoantigen in primary biliary cirrhosis. Clin Sci 85:289-93, 1993.
43. Fregeau DR, Davis PA, Danner DJ, et al: Antimitochondrial antibodies in primary biliary cirrhosis recognise dihydrolipoamide acyltransferase and inhibit enzyme function of the branched chain α-ketoacid dehydrogenase complex. J Immunol 142:3815-20, 1989.
44. Surh CD, Danner DJ, Ahmed A, et al: Reactivity of primary biliary cirrhosis sera with a human fetal liver cDNA clone of branched-chain α-keto acid dehydrogenase dihydrolipoamide acyltransferase. the 52 KDa mitochondrial autoantigen. Hepatology 9:63-68, 1989.
45. Fregeau DR, Prindiville T, Coppel RL, et al: Inhibition of α-ketoglutarate dehydrogenase activity by a distinct population of autoantibodies recognising dihydrolipoamide succinyltransferase in primary biliary cirrhosis. Hepatology 11:975-81, 1990.
46. Surh CD, Roche TE, Danner DJ, et al: Antimitochondrial autoantibodies in primary biliary cirrhosis recognise cross-reactive epitope(s) on protein X and dihydrolipoamide acetyltransferase of pyruvate dehydrogenase complex. Hepatology 10: 127-33, 1989.
47. Fussey SPM, Bassendine MF, Fittes D, et al: The E1α and β subunits of the pyruvate dehydrogenase complex are M2"d" and M2"e" autoantigens in primary biliary cirrhosis. Clin Sci 77:365-8, 1989.
48. Fregeau DR, Roche TE, Davis PA, et al: Primary biliary cirrhosis: inhibition of pyruvate dehydrogenase activity by autoantibodies specific for E1-α, a non-lipoic acid containing mitochondrial enzyme. J Immunol 144:1671-6, 1990.
49. Muno D, Kominami E, Ishii H, et al: Isolation of tryptic fragment of antigen from mitochondrial inner membrane proteins reacting with antimitochondrial antibody in sera of patients with primary biliary cirrhosis. Hepatology 11:16-23, 1990.
50. Tisch R, Yang XD, Singer SM, et al: Immune response to glutamic acid decarboxylase correlates with insulitis in non-obese diabetic mice. Nature 366:72-75, 1993.
51. Surh CD, Coppel R, Gershwin ME: Structural requirement for autoreactivity on human pyruvate dehydrogenase - E2, the major autoantigen of primary biliary cirrhosis. J Immunol 144:3367-74, 1990.
52. Leung PSC, Iwayan T, Coppel RL, Gershwin ME: Site directed mutagenesis of lysine within the immunodominant autoepitope of PDC-E2. Hepatology 12:1321-8, 1990
53. Tuaillon N, Andre C, Briand JP, et al: A lipoyl synthetic octade-capeptide of dihydrolipoamide acetyltransferase specifically recognised by anti-M2 autoantibodies in primary biliary cirrhosis. J Immunol 148:445-50, 1992.
54. Quinn J, Diamond AG, Masters AK, et al: Expression and lipoylation in Escherichia coli of the inner lipoyl domain of the E2 component of the human pyruvate dehydrogenase complex. Biochem J 289:81-85, 1993.
55. Quinn J, Diamond AG, Palmer JM, et al: Lipoylated and unlipoylated domains of human PDC-E2 as autoantigens in primary biliary cirrhosis: significance of lipoate attachment. Hepatology 18:1384-91, 1993.
56. Leung PSC, Chuang DT, Wynn RM, et al: Autoantibodies to BCOADC-E2 in patients with primary biliary cirrhosis recognise a conformational epitope. Hepatology 22:505-13, 1995.
57. Bjorkland A, Festin R, Mendel-Hartvig I, et al: Blood and liver infiltrating lymphocytes in primary biliary cirrhosis: Increase in activated T and natural killer cells and recruitment of primed memory T-cells. Hepatology 13:1106-11, 1991.
58. Leon MP, Spickett G, Jones DEJ, Bassendine MF: CD4+ T-cell subsets defined by isoforms of CD45 in primary biliary cirrhosis. Clin Exp Immunol 99:233-9, 1995.
59. Ballardini G, Mirakian R, Bianchi FB, et al: Aberrant expression of HLA-DR antigens on the bile duct epithelium in primary biliary cirrhosis' Relevance to pathogenesis. Lancet ii: 1009-13, 1984.
60. Floreani A, Bennett MK, Mitchison HC, et al: Progression of autoimmune damage in primary biliary cirrhosis: an immunohistochemical study. Autoimmunity 2 311-21, 1989.
61. Bloom S, Fleming K, Chapman R: Adhesion molecule expression in primary sclerosing cholangitis and primary biliary cirrhosis. Gut 36:604-9, 1995.
62. Leon MP, Kirby JA, Gibbs P, et al: Immunogenicity of biliary epithelial cells: study of the expression of B7 molecules. J Hepatol 22:591-5, 1995.
63. Champion BR, Page KR, Parish N, et al: Identification of a thyroxine-containing self-epitope of thyroglobulin which triggers thyroid autoreactive T-cells. J Exp Med 174:363-70, 1991.
64. Miyazaki I, Cheung RK, Gaedigk R, et al. T-cell activation and anergy to islet cell antigen in type 1 diabetes. J Immunol 154: 1461-9, 1995.
65. Sommer N, Harcourt GC, Willcox N, et al: Acetylcholine receptor reactive T lymphocytes from healthy subjects and myaesthenia gravis patients. Neurology 41:1270-6, 1991.
66. Jones DEJ, Palmer JM, Yeaman SJ, et al. T-cell responses to the components of pyruvate dehydrogenase complex in primary biliary cirrhosis. Hepatology 21:995-1002, 1995.
67. Lohr H, Fleischer B, Gerken G, et al: Autoreactive liver-infiltrating T-cells in primary biliary cirrhosis recognise inner mitochondrial epitopes and the pyruvate dehydrogenase complex. J Hepatol 18:322-7, 1993.
68. Van de Water J, Ansari A, Prindiville T, et al: Heterogeneity of autoreactive T cell clones specific for the E2 component of the pyruvate dehydrogenase complex in primary biliary cirrhosis. J Exp Med 181:723-733, 1995.
69. Van de Water J, Ansari AA, Surh CD, et al: Evidence for the targeting by 2-oxo-dehydrogenase enzymes in the T cell response of primary biliary cirrhosis. J Immunol 146:89-94, 1991.
70. Shimoda S, Nakamura M, Ishibashi H, et al: HLA DR4*0101-restricted immunodominant T-cell autoepitope of pyruvate dehydrogenase complex in primary biliary cirrhosis: evidence of molecular mimicry in human autoimmune disease. J Exp Med 181.1835-45, 1995.
71. Jones DEJ, Palmer JM, Yeaman SJ, et al: T-cell responses to human pyruvate dehydrogenase complex and its components in primary biliary cirrhosis. Gastroenterology 106:A912, 1994.
72. Russell GC, Guest JR. Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme. Biochim Biophys Acta 1076:225-32, 1991.
73. Paul WE, Seder RA: Lymphocyte responses and cytokines. Cell 76:241-51, 1994.
74. Kotzin BL, Karaturi S, Chou YK, et al: Preferential T-cell receptor β-chain variable gene use in myelin basic protein-reactive T cell clones from patients with multiple sclerosis. Proc Natl Acad Sci USA 88:9161-5, 1991.
75. Wilson KB, Quayle AJ, Suleyman S, et al: Heterogeneity of the TCR repertoire in synovial fluid T lymphocytes responding to BCG in a patient with early rheumatoid arthritis. Scand J Immunol 38:102-12, 1993.
76. Tsai SL, Lai MY, Chen DS: Analysis of rearranged T cell receptor (TCR) V beta transcripts in livers of primary biliary cirrhosis: preferential V beta usage suggests antigen-driven selection. Clin Exp Immunol 103.99-104, 1996.
77. Tandon N, Freeman M, Weetman AP: T cell responses to synthetic TSH receptor peptides in Graves' disease. Clin Exp Immunol 89:468-73, 1991.
78. Pette M, Fujita K, Whitaker JN, et al: Myelin basic protein specific T-lymphocyte lines from MS patients and healthy individuals. Neurology 40:1770-6, 1990.
79. Cohen IR: The cognitive paradigm and the immunological homunculus. Immunol Today 13:490-3, 1992.
80. Klein R, Wiebel M, Engelhart S, Berg PA: Sera from patients with tuberculosis recognise the M2a-epitope (E2 subunit of pyruvate dehydrogenase) specific for primary biliary cirrhosis. Clin Exp Immunol 92-308-16, 1993.
81. Gilburd H, Ziporen L, Zharhary D, et al: Antimitochondrial (pyruvate dehydrogenase) antibodies in leprosy. J Clin Immunol 14:14-19, 1994.
82. Liu GY, Fairchild PJ, Smith RM, et al: Low avidity recognition of self-antigen by T cells permits escape from central tolerance. Immunity 3:407-15, 1995.
83. Jones DEJ, Palmer JM, James OFW, et al: Characterisation of T-cell responses to dihydrolipoamide acetyltransferase in primary biliary cirrhosis. Clin Immunol and Immunopathol 76: S46, 1995.
84. Cha S, Leung PSC, Gershwin ME, et al: Combinatorial antibodies to dihydrolipoamide acetyltransferase, the major autoantigen in primary biliary cirrhosis. Proc Natl Acad Sci USA 90:2527-31, 1993.
85. Cha S, Leung PSC, Coppel RL, et al: Heterogeneity of combinatorial human autoantibodies against PDC-E2 and biliary epithelial cells in patients with primary biliary cirrhosis. Hepatology 20:574-83, 1994.
86. Van de Water J, Turchany J, Leung PSC, et al: Molecular mimicry in primary biliary cirrhosis: evidence for biliary epithelial expression of a molecule cross-reactive with pyruvate dehydrogenase complex. J Clin Invest 91:2653-64, 1993.
87. Tsuneyama K, Van de Water J, Nakanuma Y, et al: Human combinatorial autoantibodies and mouse monoclonal antibodies to PDC-E2 produce abnormal apical staining of salivary glands in patients with co-existent primary biliary cirrhosis and Sjögrens syndrome. Hepatology 20:893-8, 1994.
88. Joplin R, Johnson GD, Matthews JB, et al: Distribution of pyruvate dehydrogenase dihydrolipoamide acetyltransferase (PDC-E2) and another mitochondrial marker in salivary gland and biliary epithelium from patients with primary biliary cirrhosis. Hepatology 19:1375-80, 1994.
89. Epstein O, Thomas HC, Sherlock S: Primary biliary cirrhosis is a dry gland syndrome with features of chronic graft versus host disease. Lancet i: 1166-8, 1980.
90. Nakanuma Y, Tsuneyama K, Kono N, et al: Biliary epithelial cell expression of pyruvate dehydrogenase complex in primary biliary cirrhosis: an immunohistochemical and immunoelectron microscopic study. Hum Pathol 26:92-98, 1995
91. Joplin R, Wallace LL, Johnson GD, et al: Subcellular localization of pyruvate dehydrogenase dihydrolipoamide acetyltransferase in human intrahepatic biliary epithelial cells. J Pathol 176:381-90, 1995.
92. Tsuneyama K, Van de Water J, Leung P, et al. Abnormal expression of the E2 component of the pyruvate dehydrogenase complex on the luminal surface of biliary epithelium occurs before the major histocompatibility complex class II and BB1/B7 expression. Hepatology 21:1031-7, 1995.
93. Meuer SC, Moebius U, Manns M, et al Clonal analysis of human T lymphocytes infiltrating the liver in chronic active hepatitis B and primary biliary cirrhosis. Eur J Immunol 18:1447-52, 1988.
94. Krams SM, Van de Water J, Coppel RL, et al: Analysis of hepatic T lymphocytes and immunoglobulin deposits in patients with primary biliary cirrhosis. Hepatology 12:306-13, 1991.
95. Germain RN: MHC dependent antigen processing. Cell 76: f 287-99, 1994.
96. Chicz RM, Urban RG, Gorga JC, et al: Specificity and promiscuity among naturally processed peptides bound to HLA-DR alleles. J Exp Med 178:27-47, 1993.
97. Rontogianni D, Gerber H, Zimmermann A: Primary biliary cirrhosis (PBC): antigen-presenting cells differ in their distribution in early and late stage PBC and involve the ductal but not the ductular compartment. Histol Histopathol 9:211-20, 1994.
98. Matsuno K, Ezaki T, Kudo S, Uehara Y: A life stage of particleladen rat dendritic cells in vivo: their terminal division, active phagocytosis and translocation from the liver to the draining lymph. J Exp Med 183:1865-78, 1996.
99. Samson MF, Smilek DE: Reversal of acute experimental autoimmune encephalomyelitis and prevention of relapses by treatment with a myelin basic protein peptide analogue modified to form long-lived peptide-MHC complexes. J Immunol 155:2737-46, 1995.