Identification of a new functional splice variant of the enzyme methionine sulphoxide reductase A (MSRA) expressed in rat vascular smooth muscle cells

References

• Hsieh CC, Yen MH, Yen CH, Lau YT. Oxidized low-density lipoprotein induces apoptosis via generation of reactive oxygen species in vascular smooth muscle cells. Cardiovasc Res 2001; 49: 135–145
   PubMed Web of Science ®Google Scholar
• Lee JY, Jung GY, Heo HJ, Yun MR, Park JY, Bae SS, Hong KW, Lee WS, Kim CD. 4-Hydroxynonenal induces vascular smooth muscle cell apoptosis through mitochondrial generation of reactive oxygen species. Toxicol Lett 2006; 166: 212–221
   PubMed Web of Science ®Google Scholar
• Li PF, Dietz R, von Harsdorf R. Reactive oxygen species induce apoptosis of vascular smooth muscle cell. FEBS Lett 1997; 404: 249–252
   PubMedGoogle Scholar
• Li PF, Dietz R, von Harsdorf R. Differential effect of hydrogen peroxide and superoxide anion on apoptosis and proliferation of vascular smooth muscle cells. Circulation 1997; 96: 3602–3609
   PubMed Web of Science ®Google Scholar
• Lassegue B, Clempus RE. Vascular NAD(P)H oxidases: specific features, expression, and regulation. Am J Physiol Regul Integr Comp Physiol 2003; 285: R277–R297
   PubMed Web of Science ®Google Scholar
• Kashiwakura Y, Watanabe M, Kusumi N, Sumiyoshi K, Nasu Y, Yamada H, Sawamura T, Kumon H, Takei K, Daida H. Dynamin-2 regulates oxidized low-density lipoprotein-induced apoptosis of vascular smooth muscle cell. Circulation 2004; 110: 3329–3334
   PubMedGoogle Scholar
• Rajagopalan S, Meng XP, Ramasamy S, Harrison DG, Galis ZS. Reactive oxygen species produced by macrophage-derived foam cells regulate the activity of vascular matrix metalloproteinases in vitro. Implications for atherosclerotic plaque stability. J Clin Invest 1996; 98: 2572–2579
   PubMed Web of Science ®Google Scholar
• Moon SK, Thompson LJ, Madamanchi N, Ballinger S, Papaconstantinou J, Horaist C, Runge MS, Patterson C. Aging, oxidative responses, and proliferative capacity in cultured mouse aortic smooth muscle cells. Am J Physiol Heart Circ Physiol 2001; 280: H2779–2788
   PubMed Web of Science ®Google Scholar
• Paravicini TM, Touyz RM. Redox signaling in hypertension. Cardiovasc Res 2006; 71: 247–258
   PubMed Web of Science ®Google Scholar
• Stoneman VE, Bennett MR. Role of apoptosis in atherosclerosis and its therapeutic implications. Clin Sci 2004; 107: 343–354
   PubMed Web of Science ®Google Scholar
• Yu BP, Chung HY. Oxidative stress and vascular aging. Diabetes Res Clin Pract 2001; 54: 73–80
   PubMed Web of Science ®Google Scholar
• Huang W, Escribano J, Sarfarazi M, Coca-Prados M. Identification, expression and chromosome localization of a human gene encoding a novel protein with similarity to the pilB family of transcriptional factors (pilin) and to bacterial peptide methionine sulfoxide reductases. Gene 1999; 233: 233–240
   PubMed Web of Science ®Google Scholar
• Jung S, Hansel A, Kasperczyk H, Hoshi T, Heinemann SH. Activity, tissue distribution and site-directed mutagenesis of a human peptide methionine sulfoxide reductase of type B: hCBS1. FEBS Lett 2002; 527: 91–94
   PubMed Web of Science ®Google Scholar
• Hansel A, Jung S, Hoshi T, Heinemann SH. A second human methionine sulfoxide reductase (hMSRB2) reducing methionine-R-sulfoxide displays a tissue expression pattern distinct from hMSRB1. Redox Rep 2003; 8: 384–388
   PubMed Web of Science ®Google Scholar
• Moskovitz J, Weissbach H, Brot N. Cloning and expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins. Proc Natl Acad Sci USA 1996; 93: 2095–2099
   PubMedGoogle Scholar
• Petropoulos I, Mary J, Perichon M, Friguet B. Rat peptide methionine sulphoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging. Biochem J 2001; 355: 819–825
   PubMedGoogle Scholar
• Hansel A, Heinemann SH, Hoshi T. Heterogeneity and function of mammalian MSRs: enzymes for repair, protection and regulation. Biochim Biophys Acta 2005; 1703: 239–247
   PubMed Web of Science ®Google Scholar
• Kim HY, Gladyshev VN. Alternative first exon splicing regulates subcellular distribution of methionine sulfoxide reductases. BMC Mol Biol 2006; 7: 11
   PubMedGoogle Scholar
• Lee JW, Gordiyenko NV, Marchetti M, Tserentsoodol N, Sagher D, Alam S, Weissbach H, Kantorow M, Rodriguez IR. Gene structure, localization and role in oxidative stress of methionine sulfoxide reductase A (MSRA) in the monkey retina. Exp Eye Res 2006; 82: 816–827
   PubMedGoogle Scholar
• Vougier S, Mary J, Friguet B. Subcellular localization of methionine sulphoxide reductase A (MsrA): evidence for mitochondrial and cytosolic isoforms in rat liver cells. Biochem J 2003; 373: 531–537
   PubMed Web of Science ®Google Scholar
• Kim HY, Gladyshev VN. Role of structural and functional elements of mouse methionine-S-sulfoxide reductase in its subcellular distribution. Biochemistry 2005; 44: 8059–8067
   PubMed Web of Science ®Google Scholar
• Lowther WT, Brot N, Weissbach H, Honek JF, Matthews BW. Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase. Proc Natl Acad Sci USA 2000; 97: 6463–6468
   PubMed Web of Science ®Google Scholar
• Tete-Favier F, Cobessi D, Boschi-Muller S, Azza S, Branlant G, Aubry A. Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 A resolution. Structure 2000; 8: 1167–1178
   PubMedGoogle Scholar
• Moskovitz J, Flescher E, Berlett BS, Azare J, Poston JM, Stadtman ER. Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress. Proc Natl Acad Sci USA 1998; 95: 14071–14075
   PubMed Web of Science ®Google Scholar
• Jung B, Lee EH, Chung WS, Lee SJ, Shin SH, Joo SH, Kim SK, Lee JH. Increased viability of PC12 cells exposed to amyloid-beta peptide by transduction with human TAT-methionine sulfoxide reductase. Neuroreport 2003; 14: 2349–2353
   PubMedGoogle Scholar
• Yermolaieva O, Xu R, Schinstock C, Brot N, Weissbach H, Heinemann SH, Hoshi T. Methionine sulfoxide reductase A protects neuronal cells against brief hypoxia/reoxygenation. Proc Natl Acad Sci USA 2004; 101: 1159–1164
   PubMed Web of Science ®Google Scholar
• Kantorow M, Hawse JR, Cowell TL, Benhamed S, Pizarro GO, Reddy VN, Hejtmancik JF. Methionine sulfoxide reductase A is important for lens cell viability and resistance to oxidative stress. Proc Natl Acad Sci USA 2004; 101: 9654–9659
   PubMed Web of Science ®Google Scholar
• Picot CR, Petropoulos I, Perichon M, Moreau M, Nizard C, Friguet B. Overexpression of MsrA protects WI-38 SV40 human fibroblasts against H2O2-mediated oxidative stress. Free Radic Biol Med 2005; 39: 1332–1341
   PubMed Web of Science ®Google Scholar
• Ruan H, Tang XD, Chen ML, Joiner ML, Sun G, Brot N, Weissbach H, Heinemann SH, Iverson L, Wu CF, Hoshi T. High-quality life extension by the enzyme peptide methionine sulfoxide reductase. Proc Natl Acad Sci USA 2002; 99: 2748–2753
   PubMed Web of Science ®Google Scholar
• Marchetti MA, Pizarro GO, Sagher D, Deamicis C, Brot N, Hejtmancik JF, Weissbach H, Kantorow M. Methionine sulfoxide reductases B1, B2, and B3 are present in the human lens and confer oxidative stress resistance to lens cells. Invest Ophthalmol Vis Sci 2005; 46: 2107–2112
   PubMedGoogle Scholar
• Koc A, Gasch AP, Rutherford JC, Kim HY, Gladyshev VN. Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and -independent components of aging. Proc Natl Acad Sci USA 2004; 101: 7999–8004
   PubMed Web of Science ®Google Scholar
• Moskovitz J, Bar-Noy S, Williams WM, Requena J, Berlett BS, Stadtman ER. Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals. Proc Natl Acad Sci USA 2001; 98: 12920–12925
   PubMed Web of Science ®Google Scholar
• Gabbita SP, Aksenov MY, Lovell MA, Markesbery WR. Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain. J Neurochem 1999; 73: 1660–1666
   PubMed Web of Science ®Google Scholar
• Kimes BW, Brandt BL. Characterization of two putative smooth muscle cell lines from rat thoracic aorta. Exp Cell Res 1976; 98: 349–366
   PubMedGoogle Scholar
• Hansel A, Kuschel L, Hehl S, Lemke C, Agricola HJ, Hoshi T, Heinemann SH. Mitochondrial targeting of the human peptide methionine sulfoxide reductase (MSRA), an enzyme involved in the repair of oxidized proteins. FASEB J 2002; 16: 911–913
   PubMedGoogle Scholar
• Gasteiger E, Hoogland C, Gattiker A, Duvaud S, Wilkins MR, Appel RD, Bairoch A. Protein identification and analysis tools on the ExPASy server. The proteomics protocols handbook, WJM Totowa. Humana Press, New York 2005; 571–607
   Google Scholar
• Irani K. Oxidant signaling in vascular cell growth, death, and survival: a review of the roles of reactive oxygen species in smooth muscle and endothelial cell mitogenic and apoptotic signaling. Circ Res 2000; 87: 179–183
   PubMed Web of Science ®Google Scholar
• Martinet W, De Meyer GRY, Herman AG, Kockx MM. Reactive oxygen species induce RNA damage in human atherosclerosis. Eur J Clin Invest 2004; 34: 323–327
   PubMed Web of Science ®Google Scholar
• Daou GB, Srivastava AK. Reactive oxygen species mediate Endothelin-1-induced activation of ERK1/2, PKB, and Pyk2 signaling, as well as protein synthesis, in vascular smooth muscle cells. Free Radic Biol Med 2004; 37: 208–215
   PubMedGoogle Scholar
• Kalyankrishna S, Parmentier JH, Malik KU. Arachidonic acid-derived oxidation products initiate apoptosis in vascular smooth muscle cells. Prostaglandins Other Lipid Mediat 2002; 70: 13–29
   PubMedGoogle Scholar
• Cao Z, Li Y. Chemical induction of cellular antioxidants affords marked protection against oxidative injury in vascular smooth muscle cells. Biochem Biophys Res Commun 2002; 292: 50–57
   PubMed Web of Science ®Google Scholar
• Yan SK, Chang T, Wang H, Wu L, Wang R, Meng QH. Effects of hydrogen sulfide on homocysteine-induced oxidative stress in vascular smooth muscle cells. Biochem Biophys Res Commun 2006; 351: 485–491
   PubMed Web of Science ®Google Scholar
• Schallreuter KU, Rubsam K, Chavan B, Zothner C, Gillbro JM, Spencer JD, Wood JM. Functioning methionine sulfoxide reductases A and B are present in human epidermal melanocytes in the cytosol and in the nucleus. Biochem Biophys Res Commun 2006; 342: 145–152
   PubMed Web of Science ®Google Scholar
• Picot CR, Perichon M, Lundberg KC, Friguet B, Szweda LI, Petropoulos I. Alterations in mitochondrial and cytosolic methionine sulfoxide reductase activity during cardiac ischemia and reperfusion. Exp Gerontol 2006; 41: 663–667
   PubMedGoogle Scholar
• Kim HY, Gladyshev VN. Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases. Mol Biol Cell 2004; 15: 1055–1064
   PubMed Web of Science ®Google Scholar
• Kryukov GV, Kumar RA, Koc A, Sun Z, Gladyshev VN. Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase. Proc Natl Acad Sci USA 2002; 99: 4245–4250
   PubMed Web of Science ®Google Scholar
• Boschi-Muller S, Azza S, Branlant G. E. coli methionine sulfoxide reductase with a truncated N terminus or C terminus, or both, retains the ability to reduce methionine sulfoxide. Protein Sci 2001; 10: 2272–2279
   PubMedGoogle Scholar