메뉴 건너뛰기




Volumn 48, Issue 1, 2015, Pages 19-28

Glycated-H2A histone is better bound by serum anti-DNA autoantibodies in SLE patients: Glycated-histones as likely trigger for SLE?

Author keywords

AGEs; Anti DNA antibodies; Deoxyribose; Glycated histone; SLE

Indexed keywords

AUTOANTIBODY; DEOXYRIBOSE; DNA ANTIBODY; EPITOPE; HISTONE H2A; IMMUNOGLOBULIN G; ANTIBODIES, ANTINUCLEAR; ANTIGEN-ANTIBODY COMPLEX; CALF THYMUS DNA; DNA; HISTONES; PROTEIN BINDING;

EID: 84919784556     PISSN: 08916934     EISSN: 1607842X     Source Type: Journal    
DOI: 10.3109/08916934.2014.941059     Document Type: Article
Times cited : (19)

References (42)
  • 1
    • 84880369837 scopus 로고    scopus 로고
    • B cell encounters with apoptotic cells
    • Bekeredjian-Ding, I. 2013. B cell encounters with apoptotic cells. Autoimmunity. 46: 307-311.
    • (2013) Autoimmunity. , vol.46 , pp. 307-311
    • Bekeredjian-Ding, I.1
  • 2
    • 0029764927 scopus 로고    scopus 로고
    • Thrombosis and systemic lupus erythematosus: The Hopkins Lupus Cohort Perspective
    • Petri, M. 1996. Thrombosis and systemic lupus erythematosus: the Hopkins Lupus Cohort Perspective. Scand. J. Rheumatol. 25: 191-193.
    • (1996) Scand. J. Rheumatol. , vol.25 , pp. 191-193
    • Petri, M.1
  • 3
    • 0026566292 scopus 로고
    • Antibodies to histones in systemic lupus erythematosus and drug-induced lupus syndromes
    • Monestier, M., and B. L. Kotzin. 1992. Antibodies to histones in systemic lupus erythematosus and drug-induced lupus syndromes. Rheum. Dis. Clin. North Am. 18: 415-436.
    • (1992) Rheum. Dis. Clin. North Am. , vol.18 , pp. 415-436
    • Monestier, M.1    Kotzin, B.L.2
  • 4
    • 0018226902 scopus 로고
    • Serologic studies in patients with systemic lupus erythematosus and central nervous system dysfunction
    • Winfield, J. B., C. M. Brunner, and D. Koffler. 1978. Serologic studies in patients with systemic lupus erythematosus and central nervous system dysfunction. Arthritis Rheum. 21: 289-294.
    • (1978) Arthritis Rheum. , vol.21 , pp. 289-294
    • Winfield, J.B.1    Brunner, C.M.2    Koffler, D.3
  • 5
    • 0017087992 scopus 로고
    • Chromatin structure as probed by nucleosomes and proteases: Evidence for the central role of histones H3 and H4
    • Sollner-Webb, B., R. D. Camerini-Otero, and G. Falsenfeld. 1976. Chromatin structure as probed by nucleosomes and proteases: evidence for the central role of histones H3 and H4. Cell. 9: 179-193.
    • (1976) Cell. , vol.9 , pp. 179-193
    • Sollner-Webb, B.1    Camerini-Otero, R.D.2    Falsenfeld, G.3
  • 6
    • 84872184328 scopus 로고    scopus 로고
    • Autoimmunity to isomerized histone H2B in systemic lupus erythematosus
    • Doyle, H. A., D. W. Aswad, and M. J. Mamula. 2013. Autoimmunity to isomerized histone H2B in systemic lupus erythematosus. Autoimmunity. 46: 6-13.
    • (2013) Autoimmunity. , vol.46 , pp. 6-13
    • Doyle, H.A.1    Aswad, D.W.2    Mamula, M.J.3
  • 7
    • 84867922604 scopus 로고    scopus 로고
    • Apoptosis and NET formation in the pathogenesis of SLE
    • Bout, Y. M., D. F. G. J. Wolthuis, M. F. M. Dirkx, et al. 2012. Apoptosis and NET formation in the pathogenesis of SLE. Autoimmunity. 45: 597-601.
    • (2012) Autoimmunity. , vol.45 , pp. 597-601
    • Bout, Y.M.1    Wolthuis, D.F.G.J.2    Dirkx, M.F.M.3
  • 8
    • 34848886115 scopus 로고    scopus 로고
    • Accumulation of advanced glycation end products in patients with systemic lupus erythematosus
    • de Leeuw, K., R. Graff, R. De Vries, et al. 2007. Accumulation of advanced glycation end products in patients with systemic lupus erythematosus. Rheumatology. 46: 1551-1556.
    • (2007) Rheumatology. , vol.46 , pp. 1551-1556
    • De Leeuw, K.1    Graff, R.2    De Vries, R.3
  • 9
    • 67649695176 scopus 로고    scopus 로고
    • Involvement of toxic AGEs (TAGE) in the pathogenesis of diabetic vascular complications and Alzheimer's disease
    • Takeuchi, M., and S. Yamagishi. 2009. Involvement of toxic AGEs (TAGE) in the pathogenesis of diabetic vascular complications and Alzheimer's disease. J. Alzheimer's Dis. 16: 845-858.
    • (2009) J. Alzheimer's Dis. , vol.16 , pp. 845-858
    • Takeuchi, M.1    Yamagishi, S.2
  • 10
    • 0032563120 scopus 로고    scopus 로고
    • Role of the Maillard reaction in aging of tissue proteins. Advance glycation end product-dependent increase in imidazolium cross-links in human lens proteins
    • Frye, E. B., T. P. Degenhardt, S. R. Thorpe, and J. W. Baynes. 1998. Role of the Maillard reaction in aging of tissue proteins. Advance glycation end product-dependent increase in imidazolium cross-links in human lens proteins. J. Biol. Chem. 273: 18714-18719.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18714-18719
    • Frye, E.B.1    Degenhardt, T.P.2    Thorpe, S.R.3    Baynes, J.W.4
  • 11
    • 0344286498 scopus 로고    scopus 로고
    • Activation of receptor for advanced glycation end products: A mechanism for chronic vascular dysfunction in diabetic vasculo-pathy and atherosclerosis
    • Schmidt, A. M., S. D. Yan, J. L. Wautier, and D. Stern. 1999. Activation of receptor for advanced glycation end products: a mechanism for chronic vascular dysfunction in diabetic vasculo-pathy and atherosclerosis. Circ. Res. 84: 489-497.
    • (1999) Circ. Res. , vol.84 , pp. 489-497
    • Schmidt, A.M.1    Yan, S.D.2    Wautier, J.L.3    Stern, D.4
  • 12
    • 76249098959 scopus 로고    scopus 로고
    • 2-Deoxy-D-ribose induces cellular damage by increasing oxidative stress and protein glycation in a pancreatic beta-cell line
    • Koh, G., D. H. Lee, and J. T. Woo. 2010. 2-Deoxy-D-ribose induces cellular damage by increasing oxidative stress and protein glycation in a pancreatic beta-cell line. Metabolism. 59: 325-332.
    • (2010) Metabolism. , vol.59 , pp. 325-332
    • Koh, G.1    Lee, D.H.2    Woo, J.T.3
  • 13
    • 33645341711 scopus 로고    scopus 로고
    • Aging at the molecular level
    • S. I. S Tattaan, ed. Kluwer academic publishers, The Netherlands.
    • Zglinicki, T. V. 2003. Aging at the molecular level. In: Biology of aging and its modulation. S. I. S Tattaan, ed. Kluwer academic publishers, The Netherlands. p. 563-589.
    • (2003) Biology of Aging and Its Modulation , pp. 563-589
    • Zglinicki, T.V.1
  • 14
    • 17044365726 scopus 로고    scopus 로고
    • Nucleosome and chromatin fibre dynamics
    • Luger, K., and J. C. Hansen. 2005. Nucleosome and chromatin fibre dynamics. Curr. Opin. Struct. Biol. 15: 188-196.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 188-196
    • Luger, K.1    Hansen, J.C.2
  • 15
    • 0035313770 scopus 로고    scopus 로고
    • Higher-order structure of chromatin and chromosomes
    • Woodcock, C. L., and S. Dimitrov. 2001. Higher-order structure of chromatin and chromosomes. Curr. Opin. Gent. Dev. 11: 130-135.
    • (2001) Curr. Opin. Gent. Dev. , vol.11 , pp. 130-135
    • Woodcock, C.L.1    Dimitrov, S.2
  • 17
    • 0026482265 scopus 로고
    • Advanced glycosylation: Chemistry, biology, and implications for diabetes and aging
    • Bucala, R., and A. Cerami. 1992. Advanced glycosylation: chemistry, biology, and implications for diabetes and aging. Adv. Pharmacol. 23: 1-34.
    • (1992) Adv. Pharmacol. , vol.23 , pp. 1-34
    • Bucala, R.1    Cerami, A.2
  • 18
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
    • Chen, Y.H., J. T. Yang, and H. M. Martinez. 1972. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry. 11: 4120-4131.
    • (1972) Biochemistry. , vol.11 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.M.3
  • 19
    • 0027396024 scopus 로고
    • The effect of hydroxyl radical on the antigenicity of native DNA
    • Alam, K., A. Ali, and R. Ali. 1993. The effect of hydroxyl radical on the antigenicity of native DNA. FEBS Lett. 319: 66-70.
    • (1993) FEBS Lett. , vol.319 , pp. 66-70
    • Alam, K.1    Ali, A.2    Ali, R.3
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London). 227: 680-685.
    • (1970) Nature (London). , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0018200168 scopus 로고
    • Use of staphylococcal protein A as an immunological reagent
    • Goding, J. W. 1978. Use of staphylococcal protein A as an immunological reagent. J. Immunol. Methods. 20: 241-253.
    • (1978) J. Immunol. Methods. , vol.20 , pp. 241-253
    • Goding, J.W.1
  • 22
    • 1842858892 scopus 로고    scopus 로고
    • Evaluation of antibodies against oxygen free radical-modified DNA by ELISA
    • Ali, R., and K. Alam. 2002. Evaluation of antibodies against oxygen free radical-modified DNA by ELISA. Methods Mol. Biol. 186: 171-181.
    • (2002) Methods Mol. Biol. , vol.186 , pp. 171-181
    • Ali, R.1    Alam, K.2
  • 23
    • 34648834617 scopus 로고    scopus 로고
    • Immunogenicity of mitochondrial DNA modified by hydroxyl radical
    • Alam, K., Moinuddin, and S. Jabeen. 2007. Immunogenicity of mitochondrial DNA modified by hydroxyl radical. Cell. Immunol. 247: 12-17.
    • (2007) Cell. Immunol. , vol.247 , pp. 12-17
    • Moinuddin, A.K.1    Jabeen, S.2
  • 24
    • 34548033304 scopus 로고    scopus 로고
    • Catechol-estrogen modified DNA: A better antigen for cancer autoantibody
    • Khan, W. A., K. Alam, and Moinuddin. 2007. Catechol-estrogen modified DNA: a better antigen for cancer autoantibody. Arch. Biochem. Biophys. 465: 293-300.
    • (2007) Arch. Biochem. Biophys. , vol.465 , pp. 293-300
    • Khan, W.A.1    Alam, K.2    Moinuddin3
  • 25
    • 0024852380 scopus 로고
    • Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentose in the aging process
    • Sell, D. R., and V. M. Monnier. 1989. Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentose in the aging process. J. Biol. Chem. 264: 21597-21602.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21597-21602
    • Sell, D.R.1    Monnier, V.M.2
  • 26
    • 0023069259 scopus 로고
    • ADP-ribosylation of proteins. Enzymology and biological significance
    • Althaus, F. R., and C. Richter. 1987. ADP-ribosylation of proteins. Enzymology and biological significance. Mol. Biol. Biochem. Biophys. 37: 1-237.
    • (1987) Mol. Biol. Biochem. Biophys. , vol.37 , pp. 1-237
    • Althaus, F.R.1    Richter, C.2
  • 27
    • 0024560451 scopus 로고
    • Clinical significance of antibodies to histones in systemic lupus erythema-tosus
    • Kohda, S., Y. Kanayama, M. Okamura, et al. 1989. Clinical significance of antibodies to histones in systemic lupus erythema-tosus. J. Rheumatol. 16: 24-28.
    • (1989) J. Rheumatol. , vol.16 , pp. 24-28
    • Kohda, S.1    Kanayama, Y.2    Okamura, M.3
  • 28
    • 33645408299 scopus 로고    scopus 로고
    • Anti-histones antibodies in systemic lupus erythematosus, comparison of three assays: Elisa, dot blot and immunoblot
    • Ghedira, I., H. Landolsi, A. Mankai, et al. 2006. Anti-histones antibodies in systemic lupus erythematosus, comparison of three assays: Elisa, dot blot and immunoblot. Pathol. Biol. (Paris) 54: 148-154.
    • (2006) Pathol. Biol. (Paris) , vol.54 , pp. 148-154
    • Ghedira, I.1    Landolsi, H.2    Mankai, A.3
  • 29
    • 0034548214 scopus 로고    scopus 로고
    • Analysis of accumulated T-cell clonotypes in patients with systemic lupus erythematosus
    • Kato, T., M. Kurokawa, H. Sasakawa, et al. 2000. Analysis of accumulated T-cell clonotypes in patients with systemic lupus erythematosus. Arthritis Rheum. 43: 2712-2721.
    • (2000) Arthritis Rheum. , vol.43 , pp. 2712-2721
    • Kato, T.1    Kurokawa, M.2    Sasakawa, H.3
  • 30
    • 0035515222 scopus 로고    scopus 로고
    • Apoptosis in lupus pathogenesis
    • Greidinger, E. L. 2001. Apoptosis in lupus pathogenesis. Front. Biosci. 6: 1392-1402.
    • (2001) Front. Biosci. , vol.6 , pp. 1392-1402
    • Greidinger, E.L.1
  • 31
    • 84901070188 scopus 로고    scopus 로고
    • Autoantigens: Novel forms and presentation to the immune system
    • Doyle, H. A., M.-L. Yang, M. T. Raycroft, et al. 2014. Autoantigens: Novel forms and presentation to the immune system. Autoimmunity. 47: 220-233.
    • (2014) Autoimmunity. , vol.47 , pp. 220-233
    • Doyle, H.A.1    Yang, M.-L.2    Raycroft, M.T.3
  • 32
    • 84887171398 scopus 로고    scopus 로고
    • Oxidative stress in the pathology and treatment of systemic lupus erythematosus
    • Perl, A. 2013. Oxidative stress in the pathology and treatment of systemic lupus erythematosus. Nature Rev. Rheumat. 9: 674-686.
    • (2013) Nature Rev. Rheumat. , vol.9 , pp. 674-686
    • Perl, A.1
  • 34
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini, M., E. Giannoni, F. Chiti, et al. 2002. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature (London). 416: 507-511.
    • (2002) Nature (London). , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3
  • 35
    • 33846910013 scopus 로고    scopus 로고
    • Immunoglobulin glycation with fructose: A comparative study
    • Jairajpuri, D. S., S. Fatima, and M. Saleemuddin. 2007. Immunoglobulin glycation with fructose: a comparative study. Clin. Chim. Acta. 378: 86-92.
    • (2007) Clin. Chim. Acta. , vol.378 , pp. 86-92
    • Jairajpuri, D.S.1    Fatima, S.2    Saleemuddin, M.3
  • 36
    • 0030835612 scopus 로고    scopus 로고
    • Role of protein-bound carbonyl groups in the formation of advanced glycation end products
    • Liggins, J., and A. J. Furth. 1997. Role of protein-bound carbonyl groups in the formation of advanced glycation end products. Biochim. Biophy. Acta. 1361: 123-130.
    • (1997) Biochim. Biophy. Acta. , vol.1361 , pp. 123-130
    • Liggins, J.1    Furth, A.J.2
  • 37
    • 0027233741 scopus 로고
    • Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus
    • McCance, D. R., D. G. Dyer, J. A. Dunn, et al. 1993. Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus. J. Clin. Invest. 91: 2470-2478.
    • (1993) J. Clin. Invest. , vol.91 , pp. 2470-2478
    • McCance, D.R.1    Dyer, D.G.2    Dunn, J.A.3
  • 38
    • 0028360017 scopus 로고
    • Identification and characterization of membrane cofactor protein (CD46) in the human kidneys
    • Nakanishi, I., A. Moutabarrik, T. Hara, et al. 1994. Identification and characterization of membrane cofactor protein (CD46) in the human kidneys. Eur. J. Immunol. 24: 1529-1535.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 1529-1535
    • Nakanishi, I.1    Moutabarrik, A.2    Hara, T.3
  • 39
    • 2642642114 scopus 로고    scopus 로고
    • Secondary structure analysis of individual transmembrane segments of the nicotinic acetylcholine receptor by circular dichroism and Fourier transform infrared spectroscopy
    • Corbin, J., N. Methot, H. H. Wang, et al. 1998. Secondary structure analysis of individual transmembrane segments of the nicotinic acetylcholine receptor by circular dichroism and Fourier transform infrared spectroscopy. J. Biol. Chem. 273: 771-777.
    • (1998) J. Biol. Chem. , vol.273 , pp. 771-777
    • Corbin, J.1    Methot, N.2    Wang, H.H.3
  • 40
    • 84861373395 scopus 로고    scopus 로고
    • Structural and immunological characterization of amadori-rich human serum albumin: Role in diabetes mellitus
    • Arif, B., J. M. Ashraf, and Moinuddin, et al. 2012. Structural and immunological characterization of amadori-rich human serum albumin: Role in diabetes mellitus. Arch. Biochem. Biophys. 522: 17-25.
    • (2012) Arch. Biochem. Biophys. , vol.522 , pp. 17-25
    • Arif, B.1    Ashraf, J.M.2    Moinuddin3
  • 41
    • 84891843122 scopus 로고    scopus 로고
    • Studies on peroxynitrite-modified H1 histone: Implications in systemic lupus erythematosus
    • Khan, M. A., K. Dixit, and Moinuddin, et al. 2014. Studies on peroxynitrite-modified H1 histone: implications in systemic lupus erythematosus. Biochimie. 97: 104-113.
    • (2014) Biochimie. , vol.97 , pp. 104-113
    • Khan, M.A.1    Dixit, K.2    Moinuddin3
  • 42
    • 0018177342 scopus 로고
    • Antibodies to histones in drug-induced and idiopathic lupus erythematosus
    • Fritzler, M. J., and E. M. Tan. 1978. Antibodies to histones in drug-induced and idiopathic lupus erythematosus. J. Clin. Invest. 62: 560-567.
    • (1978) J. Clin. Invest. , vol.62 , pp. 560-567
    • Fritzler, M.J.1    Tan, E.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.