Proteomic analysis for protein carbonyl as an indicator of oxidative damage in senescence-accelerated mice

References

• Takeda T, Hosokawa M, Takeshita S, Irino M, Matsushita T, Tomita Y, Yamashira K, Hamamoto H, Shimizu K, Ishii M, Yamamuro T. A new murine model of accelerated senescence. Mech Ageing 1981; 17: 83–194
   Google Scholar
• Hosokawa M, Ueno M. Aging of blood–brain barrier and neuronal cells of eye and ear in SAM mice. Neurobiol Aging 1999; 20: 117–123
   PubMedGoogle Scholar
• Butterfield DA, Howard JB, Yatin S, Allen LK, Carney MJ. Free radical oxidation of brain proteins in accelerated senescence and its modulation by N-tertbutyl-a-phenylnitrone. Proc Natl Acad Sci 1997; 94: 674–678
   PubMed Web of Science ®Google Scholar
• Kurokawa T, Asada S, Nishitani S, Hazeki O. Age-related changes in manganese superoxide dismutase activity in the cerebral cortex of senescence-accelerated prone and resistant mouse. Neurosci Lett 2001; 298: 135–138
   PubMedGoogle Scholar
• Getchell VT, Peng X, Stromberg JA, Chan CK, Green CP, Subhedar KN, Shah SD, Mattson PM, Getchell LM. Age-related trends in gene expression in the chemosensorynasal mucosae of senescence-accelerated mice. Ageing Res Rev 2003; 2: 211–243
   PubMedGoogle Scholar
• Hosokawa M. A higher oxidative status accelerates senescence and aggravates age-dependent disorders in SAMP strains of mice. Mech Ageing 2002; 123: 1553–1561
   PubMed Web of Science ®Google Scholar
• Yasui F, Ishibashi M, Matsugo S, Kojo S, Oomura Y, Sasaki K. Brain lipid hydroperoxide level increases in senescence-accelerated mice at an early age. Neurosci Lett 2003; 350: 66–68
   PubMed Web of Science ®Google Scholar
• Takeda T, Hosokawa M, Higuchi K. Senescence-accelerated mouse (SAM): A novel murine model of accelerated senescence. J Am Geriatr Soc 1991; 39: 911–919
   PubMed Web of Science ®Google Scholar
• Cho MY, Bae HS, Choi KB, Cho YS, Song WC, Yoo KJ, Paik KY. Differential expression of the liver proteome in senescence accelerated mice. Proteomics 2003; 3: 1883–1894
   PubMed Web of Science ®Google Scholar
• Butterfield DA, Koppal T, Howard B, Subramaniam R, Hensley K, Yatin S, Allen K, Aksenov M, Aksenov M, Caeney J. Structural and functional changes in proteins induced by free radical-mediated oxidative stress and protective action of the antioxidants N-tert-butyl-alpha-phenylnitrone and vitamin E. Ann NY Acad Sci 1998; 854: 448–462
   PubMedGoogle Scholar
• Berlett SB, Stadtman RE. Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 1997; 272: 20313–20316
   PubMed Web of Science ®Google Scholar
• Castegna A, Aksenov M, Aksenova M, Thongboonkerd V, Klein BJ, Pierce MW, Booze R, Markesbery RW, Butterfield DA. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part 1: Creatine kinase BB, glutamine synthase, and ubiquitin carboxyl-terminal hydrolase L-1. Free Radic Biol Med 2002; 33: 562–574
   PubMed Web of Science ®Google Scholar
• Levine RL, Garland D, Oliver CN, Amici A, Climent I, Lenz AG, Ahn BW, Shaltiel S, Stadtman ER. Determination of carbonyl content in oxidatively modified proteins. Methods Enzymol 1990; 186: 464–478
   PubMed Web of Science ®Google Scholar
• Kang HJ, Kim MS. DNA cleavage by hydroxyl radicals generated in the Cu,Zn-superoxide dismutase and hydrogen peroxide system. Mol Cells 1997; 7: 777–782
   PubMedGoogle Scholar
• Park JW, Choi CH, Kim MS, Chung MH. Oxidative status on senescenceaccelerated mice. J Gerontol A Biol Sci 1996; 51: B337–B345
   PubMed Web of Science ®Google Scholar
• Kawanishi S, Hiraku Y, Oikawa S. Mechanism of guanine-specific DNA damage by oxidative stress and its role in carcinogenesis and aging. Mutat Res 2001; 488: 65–76
   PubMed Web of Science ®Google Scholar
• Ookawara T, Kawamura N, Kitagawa Y, Taniguchi N. Site-specific and random fragmentation of Cu,Zn-superoxide dismutase by glycation reaction. Implication of reactive oxygen species. J Biol Chem 1992; 267: 18505–18510
   PubMed Web of Science ®Google Scholar
• Sato K, Akaike T, Kohno M, Ando M, Maeda H. Hydroxyl radical production by H2O2 plus Cu,Zn-superoxide dismutase reflects the activity of free copper released from the oxidatively damaged enzyme. J Biol Chem 1992; 267: 25371–25377
   PubMed Web of Science ®Google Scholar
• Kaufman JR. Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls. Genes 1999; 13: 1211–1233
   Google Scholar
• Yoshida H, Haze K, Yanagi K, Yura T, Mori K. Identification of the cis-acting endoplasmic reticulum stress response element resposible for transcriptinal induction of mammalian glucouse-regulated proteins. J Biol Chem 1998; 273: 33741–33749
   PubMed Web of Science ®Google Scholar
• Roy B, Lee SA. The mammalian endoplasmic reticulum stress response element consists of an evolutionarily conserved tripartite structure and interacts with a novel stress-inducible complex. Nucleic Acids Res 1999; 27: 1437–1443
   PubMed Web of Science ®Google Scholar
• Lappi KA, Lensink FM, Alanen IH, Salo HEK, Lobell M, Juffer HA, Ruddock WL. A conserved arginine plays a role in the catalytic cycle of the protein disulfide Isomerases. J Mol Biol 2004; 335: 283–295
   PubMed Web of Science ®Google Scholar
• Chang PW, Tsui SK, Liew C, Lee CC, Waye MM, Fung KP. Isolation, characterization, and chromosomal mapping of a novel cDNA clone encoding human selenium binding protein. J Cell Biochem 1997; 64: 217–224
   PubMedGoogle Scholar
• Rabek PJ, Boylston, III HK, Papaconstantinou J. Carbonylation of ER chaperone proteins in aged mouse liver. Biochem Biophys Res Commun 2003; 305: 566–572
   PubMed Web of Science ®Google Scholar
• Stefani M, Dobson MC. Protein aggregation and aggregate toxity: New insights into protein folding, misfolding diseases and biological evolution. J Mol Med 2003; 81: 678–699
   PubMed Web of Science ®Google Scholar
• Rakhit R, Cunningham P, Furtos-Matei A, Dahan S, Qi FX, Crow PJ, Casham RN, Kondejewski HL, Chakrabartty A. Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic leteral sclerosis. J Biol Chem 2002; 277: 47551–47556
   PubMed Web of Science ®Google Scholar
• Cohen EF, Kelly WJ. Therapeutic approaches to protein-misfolding diseases. Nature 2003; 426: 905–909
   PubMed Web of Science ®Google Scholar
• Ojika K, Mitake S, Tohdoh N, Appel HS, Otsuka Y, Katada E, Matsukawa N. Hippocampal cholinergic neurostimulating peptides (HCNP). Prog Neurobiol 2000; 60: 37–83
   PubMedGoogle Scholar
• Levey IA. Muscarinic acetylcholine receptor expression in memory circuits: Implications for treatment of Alzheimer disease. Proc Natl Acad Sci 1996; 93: 13541–13546
   PubMed Web of Science ®Google Scholar
• Ojika K, Mitake S, Kayama T, Taiji M. Two different molecules, NGF and free-HCNP, stimulate cholinergic activity in septal nuculei in vitro in a different manner. Brain Res Dev Brain Res 1994; 79: 1–9
   PubMedGoogle Scholar
• Ojika K, Appel HS. Neurotrophic effects of hippocampal extracts on medial septal nucleus in vitro. Proc Natl Acad Sci 1984; 81: 2567–2571
   PubMedGoogle Scholar
• Whitehouse PJ, Price DL, Struble RG, Clark AW, Coyle JT, Delon MR. Alzheimer's disease and senile dementia: Loss of neurons in the basal forebrain. Science 1982; 215: 1237–1239
   PubMed Web of Science ®Google Scholar
• Avila AM, Corrales JF, Ruiz F, Sánchez-Góngra E, Mingorance J, Carretero VM, Mato MJ. Specific interaction of methionine adenosyltransferase with free radicals. Biofactor 1998; 8: 27–32
   PubMed Web of Science ®Google Scholar
• Trolin GC, Löfberg C, Trolin G, Orelamd L, Brain. ATP:L-methionine S-adenosyltransferase (MAT) S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH): Regional distribution and age-related changes. Eur Neuropsychopharmacol 1994; 4: 469–477
   PubMed Web of Science ®Google Scholar
• Beynon RJ, Veggerby C, Payne CE, Robertson DL, Gaskell SJ, Humphries RE, Hurst JL. Polymorphism in major urinary proteins: Molecular heterogeneity in a wild mouse population. J Chem Ecol 2002; 28: 1429–1446
   PubMedGoogle Scholar
• Friedman V, Wagner J, Danner DB. Isolation and identification of aging-related cDNAs in the mouse. Mech Ageing Dev 1990; 52: 27–43
   PubMedGoogle Scholar