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Erschienen in: Clinical Reviews in Allergy & Immunology 1/2012

01.02.2012

Autoimmune Diseases and Polyamines

verfasst von: Wesley H. Brooks

Erschienen in: Clinical Reviews in Allergy & Immunology | Ausgabe 1/2012

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Abstract

Genetics and environmental factors have important roles in autoimmune diseases but neither has given us sufficient understanding of these mysterious diseases. Therefore, we are now looking closer at epigenetics, an interface between genetics and environmental factors. Epigenetics can be defined as reversible heritable changes to chromatin that can alter gene expression without altering the gene’s DNA sequence. Methylation of DNA and histones are primary means of epigenetic control. By adding methyl groups to DNA and histones, it can limit accessibility of the underlying gene thereby altering the amount of gene expression. The methyl group is derived from an essential molecule in the cell, S-adenosylmethionine (SAM). However, a group of small molecules called polyamines also require SAM for their synthesis. Polyamines are essential for many cellular functions and polyamine activity is increased in many autoimmune diseases. Presented here is the “polyamine hypothesis” in which increased polyamine synthesis competes with cellular methylation (epigenetic control) for SAM. It is proposed that increased polyamine activity can cause disruption of cellular methylation, which can lead to abnormal expression of previously sequestered genes and disruption of other methylation-dependent cellular processes.
Literatur
1.
Zurück zum Zitat Renaudineau Y, Youinou P (2011) Epigenetics and autoimmunity, with special emphasis on DNA methylation. Keio J Medicine 60:10–16 Renaudineau Y, Youinou P (2011) Epigenetics and autoimmunity, with special emphasis on DNA methylation. Keio J Medicine 60:10–16
2.
Zurück zum Zitat Cornacchia E, Golbus J, Maybaum J, Strahler J, Hanash S, Richardson B (1988) Hydralazine and procainamide inhibit T cell DNA methylation and induce autoreactivity. J Immunol 140:2197–2200PubMed Cornacchia E, Golbus J, Maybaum J, Strahler J, Hanash S, Richardson B (1988) Hydralazine and procainamide inhibit T cell DNA methylation and induce autoreactivity. J Immunol 140:2197–2200PubMed
3.
Zurück zum Zitat Javierre BM, Fernandez AF, Richter J et al (2010) Changes in the pattern of DNA methylation associate with twin discordance in systemic lupus erythematosus. Genome Res 20:170–179PubMed Javierre BM, Fernandez AF, Richter J et al (2010) Changes in the pattern of DNA methylation associate with twin discordance in systemic lupus erythematosus. Genome Res 20:170–179PubMed
4.
Zurück zum Zitat Seiler N (1999) Polyamines and the immune system. In: Bardócz, White (eds) Polyamines in health and nutrition. Kluwer Academic, Norwell Seiler N (1999) Polyamines and the immune system. In: Bardócz, White (eds) Polyamines in health and nutrition. Kluwer Academic, Norwell
5.
Zurück zum Zitat Brooks WH (2010) X chromosome inactivation and autoimmunity. Clinic Rev Allergy Immunol 39:20–29 Brooks WH (2010) X chromosome inactivation and autoimmunity. Clinic Rev Allergy Immunol 39:20–29
6.
Zurück zum Zitat Brooks WH (2005) Autoimmune disorders result from loss of epigenetic control following chromosome damage. Med Hypotheses 64:590–598PubMed Brooks WH (2005) Autoimmune disorders result from loss of epigenetic control following chromosome damage. Med Hypotheses 64:590–598PubMed
7.
Zurück zum Zitat Thomas T, Thomas TJ (2001) Polyamines in cell growth and cell death: molecular mechanisms and therapeutic applications. Cell Mol Life Sci 58:244–258PubMed Thomas T, Thomas TJ (2001) Polyamines in cell growth and cell death: molecular mechanisms and therapeutic applications. Cell Mol Life Sci 58:244–258PubMed
8.
Zurück zum Zitat Canellakis ES, Kyriakidis DA, Rinehart CA, Huang SC, Panagiotidis C, Wong WF (1985) Regulation of polyamine biosynthesis by antizyme and some recent developments relating the induction of polyamine biosynthesis to cell growth. Biosci Rep 5:189–204PubMed Canellakis ES, Kyriakidis DA, Rinehart CA, Huang SC, Panagiotidis C, Wong WF (1985) Regulation of polyamine biosynthesis by antizyme and some recent developments relating the induction of polyamine biosynthesis to cell growth. Biosci Rep 5:189–204PubMed
9.
Zurück zum Zitat Bale S, Lopez MM, Makhatadze GI, Fang Q, Pegg AE, Ealick SE (2008) Structural basis for putrescine activation of human S-adenosylmethionine decarboxylase. Biochemistry 47:13404–13417PubMed Bale S, Lopez MM, Makhatadze GI, Fang Q, Pegg AE, Ealick SE (2008) Structural basis for putrescine activation of human S-adenosylmethionine decarboxylase. Biochemistry 47:13404–13417PubMed
10.
Zurück zum Zitat Pegg AE (2008) Spermidine/spermine-N1-acetyltransferase: a key metabolic regulator. Am J Physiol Endocrinol Metab 294:E995–E1010PubMed Pegg AE (2008) Spermidine/spermine-N1-acetyltransferase: a key metabolic regulator. Am J Physiol Endocrinol Metab 294:E995–E1010PubMed
11.
Zurück zum Zitat Furumitsu Y, Yukioka K, Yukioka M et al (2000) Interleukin-1beta induces elevation of spermidine/spermine N1-acetyltransferase activity and an increase in the amount of putrescine in synovial adherent cells from patients with rheumatoid arthritis. J Rheumatol 27:1352–1357PubMed Furumitsu Y, Yukioka K, Yukioka M et al (2000) Interleukin-1beta induces elevation of spermidine/spermine N1-acetyltransferase activity and an increase in the amount of putrescine in synovial adherent cells from patients with rheumatoid arthritis. J Rheumatol 27:1352–1357PubMed
12.
Zurück zum Zitat Furumitsu Y, Yukioka K, Kojima A et al (1993) Levels of urinary polyamines in patients with rheumatoid arthritis. J Rheumatol 20:1661–1665PubMed Furumitsu Y, Yukioka K, Kojima A et al (1993) Levels of urinary polyamines in patients with rheumatoid arthritis. J Rheumatol 20:1661–1665PubMed
13.
Zurück zum Zitat Ferrante A, Storer RJ, Cleland LJ (1990) Polyamine oxidase activity in rheumatoid arthritis synovial fluid. Clin Exp Immunol 80:373–375PubMed Ferrante A, Storer RJ, Cleland LJ (1990) Polyamine oxidase activity in rheumatoid arthritis synovial fluid. Clin Exp Immunol 80:373–375PubMed
14.
Zurück zum Zitat Igarashi K, Kashiwagi K (2010) Modulation of cellular function by polyamines. Int J Biochem Cell Biol 42:39–51PubMed Igarashi K, Kashiwagi K (2010) Modulation of cellular function by polyamines. Int J Biochem Cell Biol 42:39–51PubMed
15.
Zurück zum Zitat Shin M, Nakamuta H, Oda-Ueda N, Larsson LI, Fujiwara K (2008) Immunocytochemical demonstration of polyamines in nucleoli and nuclei. Histochem Cell Biol 129:659–665PubMed Shin M, Nakamuta H, Oda-Ueda N, Larsson LI, Fujiwara K (2008) Immunocytochemical demonstration of polyamines in nucleoli and nuclei. Histochem Cell Biol 129:659–665PubMed
16.
Zurück zum Zitat Haddox MK, Russell DH (1981) Differential conjugation of polyamines to calf nuclear and nucleolar proteins. J Cell Physiol 109:447–452PubMed Haddox MK, Russell DH (1981) Differential conjugation of polyamines to calf nuclear and nucleolar proteins. J Cell Physiol 109:447–452PubMed
17.
Zurück zum Zitat Whelly SM (1991) Role of polyamine in the regulation of RNA synthesis in uterine nucleoli. J Steroid Biochem Mol Biol 39:161–167PubMed Whelly SM (1991) Role of polyamine in the regulation of RNA synthesis in uterine nucleoli. J Steroid Biochem Mol Biol 39:161–167PubMed
18.
Zurück zum Zitat Bachrach U (2005) Naturally occurring polyamines: interaction with macromolecules. Curr Protein Pept Sci 6:559–566PubMed Bachrach U (2005) Naturally occurring polyamines: interaction with macromolecules. Curr Protein Pept Sci 6:559–566PubMed
19.
Zurück zum Zitat Moinard C, Cynober L, de Bandt JP (2005) Polyamines: metabolism and implications in human diseases. Clin Nutr 24:184–197PubMed Moinard C, Cynober L, de Bandt JP (2005) Polyamines: metabolism and implications in human diseases. Clin Nutr 24:184–197PubMed
20.
Zurück zum Zitat Morgan DM (1999) Polyamines. An overview. Mol Biotechnol 11:229–250PubMed Morgan DM (1999) Polyamines. An overview. Mol Biotechnol 11:229–250PubMed
21.
Zurück zum Zitat Matthews HR (1993) My favourite molecule: polyamines, chromatin structure and transcription. BioEssays 15:561–566PubMed Matthews HR (1993) My favourite molecule: polyamines, chromatin structure and transcription. BioEssays 15:561–566PubMed
22.
Zurück zum Zitat Newton GL, Aguilera JA, Ward JF, Fahey RC (1996) Polyamine-induced compaction and aggregation of DNA: a major factor in radioprotection of chromatin under physiological conditions. Radiation Res 145:776–780PubMed Newton GL, Aguilera JA, Ward JF, Fahey RC (1996) Polyamine-induced compaction and aggregation of DNA: a major factor in radioprotection of chromatin under physiological conditions. Radiation Res 145:776–780PubMed
23.
Zurück zum Zitat Thomas TJ, Thomas T (1994) Polyamine-induced Z-DNA conformation in plasmids containing (dA-dC)n. (dG-dT)n inserts and increased binding of lupus autoantibodies to the Z-DNA form of plasmids. Biochem J 298:485–491PubMed Thomas TJ, Thomas T (1994) Polyamine-induced Z-DNA conformation in plasmids containing (dA-dC)n. (dG-dT)n inserts and increased binding of lupus autoantibodies to the Z-DNA form of plasmids. Biochem J 298:485–491PubMed
24.
Zurück zum Zitat Hobbs CA, Gilmour SK (2000) High levels of intracellular polyamines promote histone acetyltransferase activity resulting in chromatin hyperacetylation. J Cell Biochem 77:345–360PubMed Hobbs CA, Gilmour SK (2000) High levels of intracellular polyamines promote histone acetyltransferase activity resulting in chromatin hyperacetylation. J Cell Biochem 77:345–360PubMed
25.
Zurück zum Zitat Morgan JE, Blankenship JW, Matthews HR (1987) Polyamines and acetylpolyamines increase the stability and alter the conformation of nucleosome core particles. Biochemistry 26:3643–3649PubMed Morgan JE, Blankenship JW, Matthews HR (1987) Polyamines and acetylpolyamines increase the stability and alter the conformation of nucleosome core particles. Biochemistry 26:3643–3649PubMed
26.
Zurück zum Zitat Wallon UM, O’Brien TG (2005) Polyamines modulate carcinogen-induced mutagenesis in vivo. Environ Mol Mutagen 45:62–69PubMed Wallon UM, O’Brien TG (2005) Polyamines modulate carcinogen-induced mutagenesis in vivo. Environ Mol Mutagen 45:62–69PubMed
27.
Zurück zum Zitat Alm K, Oredsson S (2009) Cells and polyamines do it cyclically. Essays Biochem 46:63–76PubMed Alm K, Oredsson S (2009) Cells and polyamines do it cyclically. Essays Biochem 46:63–76PubMed
28.
Zurück zum Zitat Park MH (2006) The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF5A). J Biochem 139:161–169PubMed Park MH (2006) The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF5A). J Biochem 139:161–169PubMed
29.
Zurück zum Zitat Sakai TT, Cohen SS (1976) Effects of polyamines on the structure and reactivity of tRNA. Prob Nucleic Acid Res Mol Biol 17:15–42 Sakai TT, Cohen SS (1976) Effects of polyamines on the structure and reactivity of tRNA. Prob Nucleic Acid Res Mol Biol 17:15–42
30.
Zurück zum Zitat Loftfield RB, Eigner EA, Pastuszyn A (1981) The role of spermine in preventing misacylation by phenylalanyl-tRNA synthetase. J Biol Chem 256:6729–6735PubMed Loftfield RB, Eigner EA, Pastuszyn A (1981) The role of spermine in preventing misacylation by phenylalanyl-tRNA synthetase. J Biol Chem 256:6729–6735PubMed
31.
Zurück zum Zitat Lüthi D, Günzel D, McGuigan JAS (1999) Mg-ATP binding: its modification by spermine, the relevance to cytosolic Mg2+ buffering, changes in the intracellular ionized Mg2+ concentration and the estimation of Mg2+ by 31P-NMR. Exp Physiol 84:231–252PubMed Lüthi D, Günzel D, McGuigan JAS (1999) Mg-ATP binding: its modification by spermine, the relevance to cytosolic Mg2+ buffering, changes in the intracellular ionized Mg2+ concentration and the estimation of Mg2+ by 31P-NMR. Exp Physiol 84:231–252PubMed
32.
Zurück zum Zitat Facchiano F, Facchiano A, Facchiano AM (2006) The role of transglutaminase-2 and its substrates in human diseases. Front Biosci 11:1758–1773PubMed Facchiano F, Facchiano A, Facchiano AM (2006) The role of transglutaminase-2 and its substrates in human diseases. Front Biosci 11:1758–1773PubMed
33.
Zurück zum Zitat Jeitner TM, Pinto JT, Krasnikov BF, Horswill M, Cooper AJL (2009) Transglutaminases and neurodegeneration. J Neurochem 109:160–166PubMed Jeitner TM, Pinto JT, Krasnikov BF, Horswill M, Cooper AJL (2009) Transglutaminases and neurodegeneration. J Neurochem 109:160–166PubMed
34.
Zurück zum Zitat Yuan Q, Ray RM, Viar MJ, Johnson LR (2001) Polyamine regulation of ornithine decarboxylase and its antizyme in intestinal epithelial cells Am. J Physiol Gastrointest Liver Physiol 280:G130–G138 Yuan Q, Ray RM, Viar MJ, Johnson LR (2001) Polyamine regulation of ornithine decarboxylase and its antizyme in intestinal epithelial cells Am. J Physiol Gastrointest Liver Physiol 280:G130–G138
35.
Zurück zum Zitat Thomas T, Thomas TJ (1993) Structural specificity of polyamines in modulating the binding of estrogen receptor to potential Z-DNA forming sequences. J Recept Res 13:1115–1133PubMed Thomas T, Thomas TJ (1993) Structural specificity of polyamines in modulating the binding of estrogen receptor to potential Z-DNA forming sequences. J Recept Res 13:1115–1133PubMed
36.
Zurück zum Zitat Maeda Y, Rachez C, Hawel L et al (2002) Polyamines modulate the interaction between nuclear receptors and vitamin D receptor-interacting protein 205. Mol Endocrinol 16:1502–1510PubMed Maeda Y, Rachez C, Hawel L et al (2002) Polyamines modulate the interaction between nuclear receptors and vitamin D receptor-interacting protein 205. Mol Endocrinol 16:1502–1510PubMed
37.
Zurück zum Zitat Williams K, Romano C, Dichter MA, Molinoff PB (1991) Modulation of the NMDA receptor by polyamines. Life Sci 48:469–498PubMed Williams K, Romano C, Dichter MA, Molinoff PB (1991) Modulation of the NMDA receptor by polyamines. Life Sci 48:469–498PubMed
38.
Zurück zum Zitat Schuber F (1989) Influence of polyamines on membrane functions. Biochem J 260:1–10PubMed Schuber F (1989) Influence of polyamines on membrane functions. Biochem J 260:1–10PubMed
39.
Zurück zum Zitat Williams K (1997) Modulation and block of ion channels: a new biology of polyamines. Cell Signal 9:1–13PubMed Williams K (1997) Modulation and block of ion channels: a new biology of polyamines. Cell Signal 9:1–13PubMed
40.
Zurück zum Zitat Scott RH, Sutton KG, Dolphin AC (1993) Interactions of polyamines with neuronal ion channels. Trends Neurosci 16:153–160PubMed Scott RH, Sutton KG, Dolphin AC (1993) Interactions of polyamines with neuronal ion channels. Trends Neurosci 16:153–160PubMed
41.
Zurück zum Zitat Ahern GP, Wang X, Miyares RL (2006) Polyamines are potent ligands for the capasicin receptor TRPV1. J Biol Chem 281:8991–8995PubMed Ahern GP, Wang X, Miyares RL (2006) Polyamines are potent ligands for the capasicin receptor TRPV1. J Biol Chem 281:8991–8995PubMed
42.
Zurück zum Zitat Schindler M, Koppel DE, Sheetz MP (1980) Modulation of membrane protein lateral mobility by polyphosphates and polyamines. Proc Natl Acad Sci USA 77:1457–1461PubMed Schindler M, Koppel DE, Sheetz MP (1980) Modulation of membrane protein lateral mobility by polyphosphates and polyamines. Proc Natl Acad Sci USA 77:1457–1461PubMed
43.
Zurück zum Zitat Poduslo JF, Curran GL (1996) Polyamine modification increases the permeability of proteins at the blood–nerve and blood–brain barriers. J Neurochem 66:1599–1609PubMed Poduslo JF, Curran GL (1996) Polyamine modification increases the permeability of proteins at the blood–nerve and blood–brain barriers. J Neurochem 66:1599–1609PubMed
44.
Zurück zum Zitat Law CL, Wong PCL, Fong WF (1984) Effects of polyamines on the uptake of neurotransmitters by rat brain synaptosomes. J Neurochem 42:870–872PubMed Law CL, Wong PCL, Fong WF (1984) Effects of polyamines on the uptake of neurotransmitters by rat brain synaptosomes. J Neurochem 42:870–872PubMed
45.
Zurück zum Zitat Giorgi PP (1978) Spermidine: a constituent of the myelin sheath? Neurosci Lett 10:335–340PubMed Giorgi PP (1978) Spermidine: a constituent of the myelin sheath? Neurosci Lett 10:335–340PubMed
46.
Zurück zum Zitat Ha HC, Sirisoma NS, Kuppusamy P, Zweier JL, Woster PM, Casero RA (1998) The natural polyamine spermine functions directly as a free radical scavenger. Proc Natl Acad Sci USA 95:11140–11145PubMed Ha HC, Sirisoma NS, Kuppusamy P, Zweier JL, Woster PM, Casero RA (1998) The natural polyamine spermine functions directly as a free radical scavenger. Proc Natl Acad Sci USA 95:11140–11145PubMed
47.
Zurück zum Zitat Seiler N, Raul F (2005) Polyamines and apoptosis. J Cell Mol Med 9:623–642PubMed Seiler N, Raul F (2005) Polyamines and apoptosis. J Cell Mol Med 9:623–642PubMed
48.
Zurück zum Zitat Pérez-Cano FJ, Franch A, Castellote C, Castell M (2003) Immunomodulatory action of spermine and spermidine on NR8383 macrophage line in various culture conditions. Cell Immunol 226:86–94PubMed Pérez-Cano FJ, Franch A, Castellote C, Castell M (2003) Immunomodulatory action of spermine and spermidine on NR8383 macrophage line in various culture conditions. Cell Immunol 226:86–94PubMed
49.
Zurück zum Zitat Sjöholm A (1993) Role of polyamines in the regulation of proliferation and hormone production by insulin-secreting cells. Am J Physiol Cell Physiol 264:C501–C518 Sjöholm A (1993) Role of polyamines in the regulation of proliferation and hormone production by insulin-secreting cells. Am J Physiol Cell Physiol 264:C501–C518
50.
Zurück zum Zitat Sakata K, Kashiwagi K, Sharmin S, Ueda S, Igarashi K (2003) Acrolein produced from polyamines as one of the uraemic toxins. Biochem Soc Trans 31:371–374PubMed Sakata K, Kashiwagi K, Sharmin S, Ueda S, Igarashi K (2003) Acrolein produced from polyamines as one of the uraemic toxins. Biochem Soc Trans 31:371–374PubMed
51.
Zurück zum Zitat Flescher E, Bowlin TL, Ballester A, Houk R, Talal N (1989) Increased polyamines may downregulate interleukin 2 production in rheumatoid arthritis. J Clin Invest 83:1356–1362PubMed Flescher E, Bowlin TL, Ballester A, Houk R, Talal N (1989) Increased polyamines may downregulate interleukin 2 production in rheumatoid arthritis. J Clin Invest 83:1356–1362PubMed
52.
Zurück zum Zitat Yukioka K, Wakitani S, Yukioka M, Furumitsu Y, Shichikawa K, Ochi T, Goto H, Matsui-Yuasa I, Otani S, Nishizawa Y et al (1992) Polyamine levels in synovial tissues and synovial fluids of patients with rheumatoid arthritis. J Rheumatol 19:689–692PubMed Yukioka K, Wakitani S, Yukioka M, Furumitsu Y, Shichikawa K, Ochi T, Goto H, Matsui-Yuasa I, Otani S, Nishizawa Y et al (1992) Polyamine levels in synovial tissues and synovial fluids of patients with rheumatoid arthritis. J Rheumatol 19:689–692PubMed
53.
Zurück zum Zitat Thomas TJ, Meryhew NL, Messner RP (2005) Enhanced binding of lupus sera to the polyamine-induced left-handed Z-DNA for of polynucleotides. Arthritis Rheum 33:356–365 Thomas TJ, Meryhew NL, Messner RP (2005) Enhanced binding of lupus sera to the polyamine-induced left-handed Z-DNA for of polynucleotides. Arthritis Rheum 33:356–365
54.
Zurück zum Zitat Moinuddin AA (1996) SLE autoantibodies recognize spermine induced Z-conformation of native calf thymus DNA. Biochem Mol Biol Int 40:787–797 Moinuddin AA (1996) SLE autoantibodies recognize spermine induced Z-conformation of native calf thymus DNA. Biochem Mol Biol Int 40:787–797
55.
Zurück zum Zitat Puri H, Campbell RA, Puri A et al (1978) Serum-free polyamines in children with systemic lupus erythematosus. Adv Polyamine Res 2:359–367 Puri H, Campbell RA, Puri A et al (1978) Serum-free polyamines in children with systemic lupus erythematosus. Adv Polyamine Res 2:359–367
56.
Zurück zum Zitat Thomas TJ, Gunnia UB, Thomas T (1992) Reversal of the abnormal development of T cell subpopulations in the thymus of autoimmune MRL-lpr/lpr mice by a polyamine biosynthesis inhibitor. Autoimmunity 13:275–283PubMed Thomas TJ, Gunnia UB, Thomas T (1992) Reversal of the abnormal development of T cell subpopulations in the thymus of autoimmune MRL-lpr/lpr mice by a polyamine biosynthesis inhibitor. Autoimmunity 13:275–283PubMed
57.
Zurück zum Zitat McCann PP, Pegg AE (1992) Ornithine decarboxylase as an enzyme target for therapy. Pharmacol Therapeutics 54:195–215 McCann PP, Pegg AE (1992) Ornithine decarboxylase as an enzyme target for therapy. Pharmacol Therapeutics 54:195–215
58.
Zurück zum Zitat Higashi K, Yoshida M, Igarashi A, Ito K, Wada Y, Murakami S, Kobayashi D, Nakano M, Sohda M, Nakajima T, Narita I, Toida T, Kashiwagi K, Igarashi K (2009) Intense correlation between protein-conjugated acrolein and primary Sjögren’s syndrome. Clinica Chimica Acta 411:359–363 Higashi K, Yoshida M, Igarashi A, Ito K, Wada Y, Murakami S, Kobayashi D, Nakano M, Sohda M, Nakajima T, Narita I, Toida T, Kashiwagi K, Igarashi K (2009) Intense correlation between protein-conjugated acrolein and primary Sjögren’s syndrome. Clinica Chimica Acta 411:359–363
59.
Zurück zum Zitat Woods PL (2006) Neurodegeneration and aldehyde load: from concept to therapeutics. J Psychiatry Neurosci 31:296–297 Woods PL (2006) Neurodegeneration and aldehyde load: from concept to therapeutics. J Psychiatry Neurosci 31:296–297
60.
Zurück zum Zitat Soulet D, Rivest S (2003) Polyamines play critical role in the control of the innate immune response in the mouse central nervous system. J Cell Biol 162:257–268PubMed Soulet D, Rivest S (2003) Polyamines play critical role in the control of the innate immune response in the mouse central nervous system. J Cell Biol 162:257–268PubMed
61.
Zurück zum Zitat Moreno B, Fernandez-Diez B, Di Penta A, Villoslada P (2010) Preclinical studies of methylthioadenosine for the treatment of multiple sclerosis. Mult Scler 16:1102–1108PubMed Moreno B, Fernandez-Diez B, Di Penta A, Villoslada P (2010) Preclinical studies of methylthioadenosine for the treatment of multiple sclerosis. Mult Scler 16:1102–1108PubMed
62.
Zurück zum Zitat Moreno B, Hevia H, Santamaria M, Sepulcre J, Munoz J, Garcia-Trevijano ER, Berasain C, Corrales FJ, Avila MA, Villoslada P (2006) Methylthioadenosine reverses brain autoimmune disease. Annals Neurol 60:323–334 Moreno B, Hevia H, Santamaria M, Sepulcre J, Munoz J, Garcia-Trevijano ER, Berasain C, Corrales FJ, Avila MA, Villoslada P (2006) Methylthioadenosine reverses brain autoimmune disease. Annals Neurol 60:323–334
63.
Zurück zum Zitat McNaught KSP, Brown GC (1998) Nitric oxide causes glutamate release from brain synaptosomes. J Neurochem 70:1541–1546PubMed McNaught KSP, Brown GC (1998) Nitric oxide causes glutamate release from brain synaptosomes. J Neurochem 70:1541–1546PubMed
64.
Zurück zum Zitat Russell DH, Meier H (1975) Alterations in the accumulation patterns of polyamines in brains of myelin-deficient mice. J Neurobiol 6:267–275PubMed Russell DH, Meier H (1975) Alterations in the accumulation patterns of polyamines in brains of myelin-deficient mice. J Neurobiol 6:267–275PubMed
65.
Zurück zum Zitat Koenig H, Goldstone AD, Lu CY (1989) Blood–brain barrier breakdown in cold-injured brain is linked to a biphase stimulation of ornithine decarboxylase activity and polyamine synthesis: both are coordinately inhibited by verapamil, dexamethasone, and aspirin. J Neurochem 52:101–109PubMed Koenig H, Goldstone AD, Lu CY (1989) Blood–brain barrier breakdown in cold-injured brain is linked to a biphase stimulation of ornithine decarboxylase activity and polyamine synthesis: both are coordinately inhibited by verapamil, dexamethasone, and aspirin. J Neurochem 52:101–109PubMed
66.
Zurück zum Zitat Satriano J, Vallon V (2006) Primary kidney growth and its consequences at the onset of diabetes mellitus. Amino Acids 31:1–9PubMed Satriano J, Vallon V (2006) Primary kidney growth and its consequences at the onset of diabetes mellitus. Amino Acids 31:1–9PubMed
67.
Zurück zum Zitat Bjelakovic G, Beninati S, Bjelakovic B, Sokolovic D, Jevtovic T, Stojanovic L, Rossi S, Tabolacci C, Kocić G, Pavlovic D, Saranac LJ, Zivic S (2010) Does polyamine oxidase activity influences the oxidative metabolism of children who suffer of diabetes mellitus? Mol Cell Biochem 341:79–85PubMed Bjelakovic G, Beninati S, Bjelakovic B, Sokolovic D, Jevtovic T, Stojanovic L, Rossi S, Tabolacci C, Kocić G, Pavlovic D, Saranac LJ, Zivic S (2010) Does polyamine oxidase activity influences the oxidative metabolism of children who suffer of diabetes mellitus? Mol Cell Biochem 341:79–85PubMed
68.
Zurück zum Zitat Pirinen E, Kuulasmaa T, Pietilä M et al (2007) Enhanced polyamine catabolism alters homeostatic control of white adipose tissue mass, energy expenditure, and glucose metabolism. Mol Cell Biol 27:4953–4967PubMed Pirinen E, Kuulasmaa T, Pietilä M et al (2007) Enhanced polyamine catabolism alters homeostatic control of white adipose tissue mass, energy expenditure, and glucose metabolism. Mol Cell Biol 27:4953–4967PubMed
69.
Zurück zum Zitat Seghieri G, Anichini R, Ciuti M, Gironi A, Bennardini F, Franconi F (1997) Raised erythrocyte polyamine levels in non-insulin-dependent diabetes mellitus with great vessel disease and albuminuria. Diabetes Res Clin Prac 37:15–20 Seghieri G, Anichini R, Ciuti M, Gironi A, Bennardini F, Franconi F (1997) Raised erythrocyte polyamine levels in non-insulin-dependent diabetes mellitus with great vessel disease and albuminuria. Diabetes Res Clin Prac 37:15–20
70.
Zurück zum Zitat Matsushita K, Fukumoto M, Kobayashi T, Kobayashi M, Ishizaki E, Minami M, Katsumura K, Liao SD, Wu DM, Zhang T, Puro DG (2010) Diabetes-induced inhibition of voltage-dependent calcium channels in the retinal microvasculature: role of spermine. Invest Ophthalmol Vis Sci 51:5979–5990PubMed Matsushita K, Fukumoto M, Kobayashi T, Kobayashi M, Ishizaki E, Minami M, Katsumura K, Liao SD, Wu DM, Zhang T, Puro DG (2010) Diabetes-induced inhibition of voltage-dependent calcium channels in the retinal microvasculature: role of spermine. Invest Ophthalmol Vis Sci 51:5979–5990PubMed
71.
Zurück zum Zitat Szathmary I, Selmect L, Szobor A, Molnar J (1994) Altered polyamine levels in skeletal muscle of patients with myasthenia gravis. Clin Neuropathol 13:181–184PubMed Szathmary I, Selmect L, Szobor A, Molnar J (1994) Altered polyamine levels in skeletal muscle of patients with myasthenia gravis. Clin Neuropathol 13:181–184PubMed
72.
Zurück zum Zitat Invernizzi P, Pasini S, Selmi C, Gershwin ME, Podda M (2009) Female predominance and X chromosome defects in autoimmune disease. J Autoimmunity 33:12–16 Invernizzi P, Pasini S, Selmi C, Gershwin ME, Podda M (2009) Female predominance and X chromosome defects in autoimmune disease. J Autoimmunity 33:12–16
73.
Zurück zum Zitat Lu Q, Wu A, Tesmer L, Ray D, Yousif N, Richardson B (2007) Demethylation of CD40LG on the inactive X in T cells from women with lupus. J Immunol 179:6352–6358PubMed Lu Q, Wu A, Tesmer L, Ray D, Yousif N, Richardson B (2007) Demethylation of CD40LG on the inactive X in T cells from women with lupus. J Immunol 179:6352–6358PubMed
74.
Zurück zum Zitat Cordoba-Guijarro S, Feal C, Dauden E et al (2000) Lupus erythematosus-like lesions in a carrier of X-linked chronic granulomatous disease. J Eur Acad Dermatol Venereol 14:409PubMed Cordoba-Guijarro S, Feal C, Dauden E et al (2000) Lupus erythematosus-like lesions in a carrier of X-linked chronic granulomatous disease. J Eur Acad Dermatol Venereol 14:409PubMed
75.
Zurück zum Zitat Ortiz-Romero P, Corell-Almuzara A, Lopez-Estebaranz J et al (1997) Lupus like lesions in a patient with X-linked chronic granulomatous disease and recombinant X chromosome. Dermatology 195:280–283PubMed Ortiz-Romero P, Corell-Almuzara A, Lopez-Estebaranz J et al (1997) Lupus like lesions in a patient with X-linked chronic granulomatous disease and recombinant X chromosome. Dermatology 195:280–283PubMed
76.
Zurück zum Zitat Chagnon P, Schneider R, Hébert J et al (2006) Identification and characterization of an Xp22.33;Yp11.2 translocation causing a triplication of several genes of the pseudoautosomal region 1 in an XX male patient with severe systemic lupus erythematosus. Arthritis Rheum 54:1270–1278PubMed Chagnon P, Schneider R, Hébert J et al (2006) Identification and characterization of an Xp22.33;Yp11.2 translocation causing a triplication of several genes of the pseudoautosomal region 1 in an XX male patient with severe systemic lupus erythematosus. Arthritis Rheum 54:1270–1278PubMed
77.
Zurück zum Zitat Kalantry S (2011) Recent advances in X-chromosome inactivation. J Cell Physiol 226:1714–1718PubMed Kalantry S (2011) Recent advances in X-chromosome inactivation. J Cell Physiol 226:1714–1718PubMed
78.
Zurück zum Zitat Zhang LF, Huynh KD, Lee JT (2007) Perinucleolar targeting of the inactive X during S phase: evidence for a role in the maintenance of silencing. Cell 129:693–706PubMed Zhang LF, Huynh KD, Lee JT (2007) Perinucleolar targeting of the inactive X during S phase: evidence for a role in the maintenance of silencing. Cell 129:693–706PubMed
79.
Zurück zum Zitat Carrel L, Willard HF (2005) X-inactivation profile reveals extensive variability in X-linked gene expression in females. Nature 434:400–404PubMed Carrel L, Willard HF (2005) X-inactivation profile reveals extensive variability in X-linked gene expression in females. Nature 434:400–404PubMed
80.
Zurück zum Zitat Sharp A, Robinson D, Jacobs P (2000) Age- and tissue-specific variation of X chromosome inactivation ratios in normal women. Hum Genet 107:343–349PubMed Sharp A, Robinson D, Jacobs P (2000) Age- and tissue-specific variation of X chromosome inactivation ratios in normal women. Hum Genet 107:343–349PubMed
81.
Zurück zum Zitat Carrel L, Park C, Tyekucheva S, Dunn J, Chiaromonte F, Makova KD (2006) Genomic environment predicts expression patterns on the human inactive X chromosome. PLoS Genetics 2:e151PubMed Carrel L, Park C, Tyekucheva S, Dunn J, Chiaromonte F, Makova KD (2006) Genomic environment predicts expression patterns on the human inactive X chromosome. PLoS Genetics 2:e151PubMed
82.
Zurück zum Zitat Brooks WH, Le Dantec C, Pers JO, Youinou P, Renaudineau Y (2010) Epigenetics and autoimmunity’. J Autoimmunity 34:j207–j219 Brooks WH, Le Dantec C, Pers JO, Youinou P, Renaudineau Y (2010) Epigenetics and autoimmunity’. J Autoimmunity 34:j207–j219
83.
Zurück zum Zitat Toussirot E, Roudier J (2008) Epstein–Barr virus in autoimmune diseases. Best Pract Res Clin Rheumatol 22:883–896PubMed Toussirot E, Roudier J (2008) Epstein–Barr virus in autoimmune diseases. Best Pract Res Clin Rheumatol 22:883–896PubMed
84.
Zurück zum Zitat Bajaj BG, Murakami M, Cai Q, Verma SC, Lan K, Robertson ES (2008) Epstein–Barr virus nuclear antigen 3C interacts with and enhances the stability of the c-Myc oncoprotein. J Virology 82:4082–4090PubMed Bajaj BG, Murakami M, Cai Q, Verma SC, Lan K, Robertson ES (2008) Epstein–Barr virus nuclear antigen 3C interacts with and enhances the stability of the c-Myc oncoprotein. J Virology 82:4082–4090PubMed
85.
Zurück zum Zitat Bello-Fernandez C, Packham G, Cleveland JL (1993) The ornithine decarboxylase gene is a transcriptional target of c-Myc. Proc Natl Acad Sci USA 90:7804–7808PubMed Bello-Fernandez C, Packham G, Cleveland JL (1993) The ornithine decarboxylase gene is a transcriptional target of c-Myc. Proc Natl Acad Sci USA 90:7804–7808PubMed
86.
Zurück zum Zitat Maraia RJ (2001) La protein and the trafficking of nascent RNA polymerase III transcripts. J Cell Biol 153:F13–F18PubMed Maraia RJ (2001) La protein and the trafficking of nascent RNA polymerase III transcripts. J Cell Biol 153:F13–F18PubMed
87.
Zurück zum Zitat Matera AG, Frey MR, Margelot K, Wolin SL (1995) A perinucleolar compartment contains several RNA polymerase III transcripts as well as the polypyrimidine tract-binding protein, hnRNP I. J Cell Biol 129:1181–1193PubMed Matera AG, Frey MR, Margelot K, Wolin SL (1995) A perinucleolar compartment contains several RNA polymerase III transcripts as well as the polypyrimidine tract-binding protein, hnRNP I. J Cell Biol 129:1181–1193PubMed
88.
Zurück zum Zitat Häsler J, Strub K (2006) Alu elements as regulators of gene expression. Nuc Acids Res 34:5491–5497 Häsler J, Strub K (2006) Alu elements as regulators of gene expression. Nuc Acids Res 34:5491–5497
89.
Zurück zum Zitat Price AL, Eskin E, Pevzner PA (2004) Whole-genome analysis of Alu repeat elements reveals complex evolutionary history. Genome Res 14:2245–2252PubMed Price AL, Eskin E, Pevzner PA (2004) Whole-genome analysis of Alu repeat elements reveals complex evolutionary history. Genome Res 14:2245–2252PubMed
90.
Zurück zum Zitat Ross MT, Graham DV, Coffey AJ et al (2005) The DNA sequence of the human X chromosome. Nature 434:325–337PubMed Ross MT, Graham DV, Coffey AJ et al (2005) The DNA sequence of the human X chromosome. Nature 434:325–337PubMed
91.
Zurück zum Zitat Haeusler RA, Engelke DR (2006) Spatial organization of transcription by RNA polymerase III. Nuc Acids Res 34:4826–4836 Haeusler RA, Engelke DR (2006) Spatial organization of transcription by RNA polymerase III. Nuc Acids Res 34:4826–4836
92.
Zurück zum Zitat Huang S, Deerinck TJ, Ellisman MH, Spector DL (1998) The perinucleolar compartment and transcription. J Cell Biol 143:35–47PubMed Huang S, Deerinck TJ, Ellisman MH, Spector DL (1998) The perinucleolar compartment and transcription. J Cell Biol 143:35–47PubMed
93.
Zurück zum Zitat Kole R, Fresco LD, Keene JD, Cohen PL, Eisenberg RA, Andrews PG (1985) Alu RNA-protein complexes formed in vitro react with a novel lupus autoantibody. J Biol Chem 260:11781–11786PubMed Kole R, Fresco LD, Keene JD, Cohen PL, Eisenberg RA, Andrews PG (1985) Alu RNA-protein complexes formed in vitro react with a novel lupus autoantibody. J Biol Chem 260:11781–11786PubMed
94.
Zurück zum Zitat Lyon MF (2000) LINE-1 elements and X chromosome inactivation: a function for “junk” DNA? Proc Natl Acad Sci USA 97:6248–6249PubMed Lyon MF (2000) LINE-1 elements and X chromosome inactivation: a function for “junk” DNA? Proc Natl Acad Sci USA 97:6248–6249PubMed
95.
Zurück zum Zitat Chow JC, Ciaudo C, Fazzari MJ, Mise N, Servant N, Glass JL, Attreed M, Avner P, Wutz A, Barillot E, Greally JM, Voinnet O, Heard E (2010) LINE-1 activity in facultative heterochromatin formation during X chromosome inactivation. Cell 141:956–969PubMed Chow JC, Ciaudo C, Fazzari MJ, Mise N, Servant N, Glass JL, Attreed M, Avner P, Wutz A, Barillot E, Greally JM, Voinnet O, Heard E (2010) LINE-1 activity in facultative heterochromatin formation during X chromosome inactivation. Cell 141:956–969PubMed
96.
Zurück zum Zitat Sassaman DM, Dombroski BA, Moran JV et al (1997) Many human L1 elements are capable of retrotransposition. Nat Genet 16:37–43PubMed Sassaman DM, Dombroski BA, Moran JV et al (1997) Many human L1 elements are capable of retrotransposition. Nat Genet 16:37–43PubMed
97.
Zurück zum Zitat Garcia-Perez JL, Doucet AJ, Bucheton A, Moran JV, Gilbert N (2007) Distinct mechanisms for trans-mediated mobilization of cellular RNAs by the LINE-1 reverse transcriptase. Genome Res 17:602–611PubMed Garcia-Perez JL, Doucet AJ, Bucheton A, Moran JV, Gilbert N (2007) Distinct mechanisms for trans-mediated mobilization of cellular RNAs by the LINE-1 reverse transcriptase. Genome Res 17:602–611PubMed
98.
Zurück zum Zitat Dewannieux M, Esnault C, Heidmann T (2003) LINE-mediated retrotransposition of marked Alu sequences. Nature Genet 35:41–48PubMed Dewannieux M, Esnault C, Heidmann T (2003) LINE-mediated retrotransposition of marked Alu sequences. Nature Genet 35:41–48PubMed
99.
Zurück zum Zitat Balada E, Ordi-Ros J, Vilardell-Tarrés M (2009) Molecular mechanisms mediated by human endogenous retroviruses (HERVs) in autoimmunity. Rev Med Virol 19:273–286PubMed Balada E, Ordi-Ros J, Vilardell-Tarrés M (2009) Molecular mechanisms mediated by human endogenous retroviruses (HERVs) in autoimmunity. Rev Med Virol 19:273–286PubMed
100.
Zurück zum Zitat Nalabothula N, Indig FE, Carrier F (2010) The nucleolus takes control of protein trafficking under cellular stress. Mol Cell Pharmacol 2:203–212PubMed Nalabothula N, Indig FE, Carrier F (2010) The nucleolus takes control of protein trafficking under cellular stress. Mol Cell Pharmacol 2:203–212PubMed
101.
Zurück zum Zitat Li JZ, Steinman CR (1989) Plasma DNA in systemic lupus erythematosus: characterization of cloned base sequences. Arthritis Rheum 32:726–733PubMed Li JZ, Steinman CR (1989) Plasma DNA in systemic lupus erythematosus: characterization of cloned base sequences. Arthritis Rheum 32:726–733PubMed
102.
Zurück zum Zitat Tsuchiya T, Saegusa Y, Taira T, Mimori T, Iguchi-Ariga SMM, Ariga H (1998) Ku antigen binds to Alu family DNA. J Biochem 123:120–127PubMed Tsuchiya T, Saegusa Y, Taira T, Mimori T, Iguchi-Ariga SMM, Ariga H (1998) Ku antigen binds to Alu family DNA. J Biochem 123:120–127PubMed
103.
Zurück zum Zitat Marshak-Rothstein A (2006) Toll-like receptors in systemic autoimmune disease. Nature Rev Immunol 6:823–835 Marshak-Rothstein A (2006) Toll-like receptors in systemic autoimmune disease. Nature Rev Immunol 6:823–835
104.
Zurück zum Zitat Brooks WH (2002) Autoimmune diseases may result from inappropriate RNA polymerase III transcription. Arthritis Rheum 46:1412–1413PubMed Brooks WH (2002) Autoimmune diseases may result from inappropriate RNA polymerase III transcription. Arthritis Rheum 46:1412–1413PubMed
105.
Zurück zum Zitat Ricardson AL, Wang ZC, De Nicolo A, Lu X, Brown M, Miron A, Liao X, Iglehart JD, Livingston DM, Ganesan S (2006) X chromosomal abnormalities in basal-like human breast cancer. Cancer Cell 9:121–132 Ricardson AL, Wang ZC, De Nicolo A, Lu X, Brown M, Miron A, Liao X, Iglehart JD, Livingston DM, Ganesan S (2006) X chromosomal abnormalities in basal-like human breast cancer. Cancer Cell 9:121–132
106.
Zurück zum Zitat Nakopoulou L, Panayotopoulou EG, Giannopoulou I, Tsirmpa I, Katsarou S, Mylona E, Alexandrou P, Keramopoulos A (2007) Extra copies of chromosomes 16 and X in invasive breast carcinomas are related to aggressive phenotype and poor prognosis. J Clin Pathol 60:808–815PubMed Nakopoulou L, Panayotopoulou EG, Giannopoulou I, Tsirmpa I, Katsarou S, Mylona E, Alexandrou P, Keramopoulos A (2007) Extra copies of chromosomes 16 and X in invasive breast carcinomas are related to aggressive phenotype and poor prognosis. J Clin Pathol 60:808–815PubMed
107.
Zurück zum Zitat Weichenrieder O, Wild K, Strub K, Cusack S (2000) Structure and assembly of the Alu domain of the mammalian signal recognition particle. Nature 408:167–173PubMed Weichenrieder O, Wild K, Strub K, Cusack S (2000) Structure and assembly of the Alu domain of the mammalian signal recognition particle. Nature 408:167–173PubMed
108.
Zurück zum Zitat Batey RT, Rambo RP, Lucast L, Rha B, Doudna JA (2000) Crystal structure of the ribonucleoprotein core of the signal recognition particle. Science 287:1232–1239PubMed Batey RT, Rambo RP, Lucast L, Rha B, Doudna JA (2000) Crystal structure of the ribonucleoprotein core of the signal recognition particle. Science 287:1232–1239PubMed
109.
Zurück zum Zitat Jacobson MR, Pederson T (1998) Localization of signal recognition particle RNA in the nucleolus of mammalian cells. Proc Natl Acad Sci USA 95:7981–7986PubMed Jacobson MR, Pederson T (1998) Localization of signal recognition particle RNA in the nucleolus of mammalian cells. Proc Natl Acad Sci USA 95:7981–7986PubMed
110.
Zurück zum Zitat Strub K, Walter P (1990) Assembly of the Alu domain of the signal recognition particle (SRP): dimerization of the two protein components is required for efficient binding to SRP RNA. Mol Cell Biol 10:777–784PubMed Strub K, Walter P (1990) Assembly of the Alu domain of the signal recognition particle (SRP): dimerization of the two protein components is required for efficient binding to SRP RNA. Mol Cell Biol 10:777–784PubMed
111.
Zurück zum Zitat Strub K, Moss J, Walter P (1991) Binding sites of the 9- and 14-kilodalton heterodimeric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolution. Mol Cell Biol 11:3949–3959PubMed Strub K, Moss J, Walter P (1991) Binding sites of the 9- and 14-kilodalton heterodimeric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolution. Mol Cell Biol 11:3949–3959PubMed
112.
Zurück zum Zitat Siegel V, Waiter P (1986) Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact. Nature 320:81–84PubMed Siegel V, Waiter P (1986) Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact. Nature 320:81–84PubMed
113.
Zurück zum Zitat Tolbert WD, Ekstrom JL, Mathews II, Secrist JA 3rd, Kapoor P, Pegg AE, Ealick SE (2001) The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase. Biochemistry 40:9484–9494PubMed Tolbert WD, Ekstrom JL, Mathews II, Secrist JA 3rd, Kapoor P, Pegg AE, Ealick SE (2001) The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase. Biochemistry 40:9484–9494PubMed
Metadaten
Titel
Autoimmune Diseases and Polyamines
verfasst von
Wesley H. Brooks
Publikationsdatum
01.02.2012
Verlag
Humana Press Inc
Erschienen in
Clinical Reviews in Allergy & Immunology / Ausgabe 1/2012
Print ISSN: 1080-0549
Elektronische ISSN: 1559-0267
DOI
https://doi.org/10.1007/s12016-011-8290-y

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