메뉴 건너뛰기




Volumn 35, Issue 4, 2010, Pages 548-558

Nicotine reduces the cytotoxic effect of glycated proteins on microglial cells

Author keywords

Alzheimer's disease; Glycation; Microglial cells; Nicotine; Secondary structure

Indexed keywords

ADVANCED GLYCATION END PRODUCT RECEPTOR; BOVINE SERUM ALBUMIN; CONGO RED; GLUCOSE; GLYCOSYLATED PROTEIN; LIPOCORTIN 5; NICOTINE; NITRIC OXIDE; PROPIDIUM IODIDE; REACTIVE OXYGEN METABOLITE; THIOFLAVINE;

EID: 77953539682     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11064-009-0095-5     Document Type: Article
Times cited : (17)

References (50)
  • 1
    • 42449109476 scopus 로고    scopus 로고
    • Mechanisms of disease: Advanced glycation end products and their receptor in inflammation and diabetes complications
    • Yan SF, Ramasamy R, Schmidt AM (2008) Mechanisms of disease: advanced glycation end products and their receptor in inflammation and diabetes complications. Nat Clin Pract Endocrinol Metab 4:285-293
    • (2008) Nat Clin Pract Endocrinol Metab , vol.4 , pp. 285-293
    • Yan, S.F.1    Ramasamy, R.2    Schmidt, A.M.3
  • 2
    • 44449179863 scopus 로고    scopus 로고
    • Possible involvement of advanced glycation end-products, AGEs, in the pathogenesis of Alzheimer's disease
    • Takeuchi M, Yamagishi S (2008) Possible involvement of advanced glycation end-products, AGEs, in the pathogenesis of Alzheimer's disease. Curr Pharm Des 14:973-978
    • (2008) Curr Pharm Des , vol.14 , pp. 973-978
    • Takeuchi, M.1    Yamagishi, S.2
  • 3
    • 44449172015 scopus 로고    scopus 로고
    • Role of advanced glycation end products in diabetic neuropathy
    • Sugimoto K, Yasujima M, Yagihashi S (2008) Role of advanced glycation end products in diabetic neuropathy. Curr Pharm Des 14:953-961
    • (2008) Curr Pharm Des , vol.14 , pp. 953-961
    • Sugimoto, K.1    Yasujima, M.2    Yagihashi, S.3
  • 4
    • 0344925061 scopus 로고    scopus 로고
    • Advanced glycation end product ligands for the receptor for advanced glycation endproducts: Biochemical characterization and formation kinetics
    • Valencia JV, Weldon SC, Quinn D et al (2004) Advanced glycation end product ligands for the receptor for advanced glycation endproducts: biochemical characterization and formation kinetics. Anal Biochem 324:68-78
    • (2004) Anal Biochem , vol.324 , pp. 68-78
    • Valencia, J.V.1    Weldon, S.C.2    Quinn, D.3
  • 5
    • 1542752823 scopus 로고    scopus 로고
    • Does diabetes protect or provoke Alzheimer's disease? Insights into the pathobiology and future treatment of Alzheimer's disease
    • Grossman H (2003) Does diabetes protect or provoke Alzheimer's disease? Insights into the pathobiology and future treatment of Alzheimer's disease. CNS Spectr 8:815-823
    • (2003) CNS Spectr , vol.8 , pp. 815-823
    • Grossman, H.1
  • 6
    • 0142180141 scopus 로고    scopus 로고
    • Glycation induces formation of amyloid cross-b structure in albumin
    • Bouma B, Kroon-Batenburg LMJ, Wu YP et al (2003) Glycation induces formation of amyloid cross-b structure in albumin. J Biol Chem 278:41810-41819
    • (2003) J Biol Chem , vol.278 , pp. 41810-41819
    • Bouma, B.1    Kroon-Batenburg, L.M.J.2    Wu, Y.P.3
  • 7
    • 0033616575 scopus 로고    scopus 로고
    • Designing conditions for in vitro formation of amyloid protofilaments and fibrils
    • Chiti F, Webster P, Taddei N et al (1999) Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc Natl Acad Sci USA 96:3590-3594
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3590-3594
    • Chiti, F.1    Webster, P.2    Taddei, N.3
  • 9
    • 48749113102 scopus 로고    scopus 로고
    • Microglial cell death induced by glycated bovine serum albumin: Nitric oxide involvement
    • Khazaei MR, Habibi-Rezaei M, Karimzadeh F et al (2008) Microglial cell death induced by glycated bovine serum albumin: nitric oxide involvement. J Biochem 144:197-206
    • (2008) J Biochem , vol.144 , pp. 197-206
    • Khazaei, M.R.1    Habibi-Rezaei, M.2    Karimzadeh, F.3
  • 10
    • 33846023647 scopus 로고    scopus 로고
    • Lysozyme amyloid oligomers and fibrils induce cellular death via different apoptotic/necrotic pathways
    • Gharibyan AL, Zamotin V, Yanamandra K et al (2007) Lysozyme amyloid oligomers and fibrils induce cellular death via different apoptotic/necrotic pathways. J Mol Biol 365:1337-1349
    • (2007) J Mol Biol , vol.365 , pp. 1337-1349
    • Gharibyan, A.L.1    Zamotin, V.2    Yanamandra, K.3
  • 11
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
    • Yan SD, Chen X, Fu J et al (1996) RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease. Nature 382:685-691
    • (1996) Nature , vol.382 , pp. 685-691
    • Yan, S.D.1    Chen, X.2    Fu, J.3
  • 12
    • 0000920292 scopus 로고    scopus 로고
    • Amyloid beta-peptide receptor for advanced glycation end product interaction elicits neuronal expression of macrophage colony stimulating factor: A proinflammatory pathway in Alzheimer's disease
    • Yan SD, Zhu H, Fu J et al (1997) Amyloid beta-peptide receptor for advanced glycation end product interaction elicits neuronal expression of macrophage colony stimulating factor: a proinflammatory pathway in Alzheimer's disease. Proc Natl Acad Sci USA 94:5296-5301
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5296-5301
    • Yan, S.D.1    Zhu, H.2    Fu, J.3
  • 13
    • 0037131412 scopus 로고    scopus 로고
    • Myelin basic proteinprimed T cells induce nitric oxide synthase in microglial cells: Implications for multiple sclerosis
    • Dasgupta S, Jana M, Liu X et al (2002) Myelin basic proteinprimed T cells induce nitric oxide synthase in microglial cells: implications for multiple sclerosis. J Biol Chem 277:39327-39333
    • (2002) J Biol Chem , vol.277 , pp. 39327-39333
    • Dasgupta, S.1    Jana, M.2    Liu, X.3
  • 14
    • 0028023944 scopus 로고
    • Glycated tau protein in Alzheimer's disease: A mechanism for induction of oxidant stress
    • Yan SD, Chen X, Scmidt AM et al (1994) Glycated tau protein in Alzheimer's disease: a mechanism for induction of oxidant stress. Proc Natl Acad Sci USA 91:7781-7791
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7781-7791
    • Yan, S.D.1    Chen, X.2    Scmidt, A.M.3
  • 15
    • 0028363366 scopus 로고
    • Advanced glycation end products contribute to amyloidosis in Alzheimer disease
    • Vitek MP, Bhattacharya K, Glendening JM et al (1994) Advanced glycation end products contribute to amyloidosis in Alzheimer disease. Proc Natl Acad Sci USA 91:4766-4770
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4766-4770
    • Vitek, M.P.1    Bhattacharya, K.2    Glendening, J.M.3
  • 16
    • 0036838889 scopus 로고    scopus 로고
    • Nicotine breaks down preformed Alzheimer's beta-amyloid fibrils in vitro
    • Ono K, Hasegawa K, Yamada M et al (2002) Nicotine breaks down preformed Alzheimer's beta-amyloid fibrils in vitro. Biol Psychiatry 52:880-886
    • (2002) Biol Psychiatry , vol.52 , pp. 880-886
    • Ono, K.1    Hasegawa, K.2    Yamada, M.3
  • 17
    • 20044370990 scopus 로고    scopus 로고
    • Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo
    • Yang F, Lim GP, Begum AN et al (2005) Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J Biol Chem 280:5892-5901
    • (2005) J Biol Chem , vol.280 , pp. 5892-5901
    • Yang, F.1    Lim, G.P.2    Begum, A.N.3
  • 18
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct
    • Necula M, Kayed R, Milton S et al (2007) Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct. J Biol Chem 282:10311-10324
    • (2007) J Biol Chem , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3
  • 19
    • 33947415364 scopus 로고    scopus 로고
    • Conformational stability of A beta-, 25-35 in the presence of thiazolidine derivatives
    • Campiglia P, Esposito C, Scrima M et al (2007) Conformational stability of A beta-, 25-35 in the presence of thiazolidine derivatives. Chem Biol Drug Des 69:111-118
    • (2007) Chem Biol Drug Des , vol.69 , pp. 111-118
    • Campiglia, P.1    Esposito, C.2    Scrima, M.3
  • 20
    • 1642453817 scopus 로고    scopus 로고
    • Both the D-,+ and L-,-enantiomers of nicotine inhibit A beta aggregation and cytotoxicity
    • Moore SA, Huckerby TN, Gibson GL et al (2004) Both the D-,+ and L-,-enantiomers of nicotine inhibit A beta aggregation and cytotoxicity. Biochemistry 43:819-826
    • (2004) Biochemistry , vol.43 , pp. 819-826
    • Moore, S.A.1    Huckerby, T.N.2    Gibson, G.L.3
  • 21
    • 0029956783 scopus 로고    scopus 로고
    • Nicotine inhibits amyloid formation by the β-peptide
    • Salomon AR, Marcinowski KJ, Friedland RP et al (1996) Nicotine inhibits amyloid formation by the β-peptide. Biochemistry 35:13568-13578
    • (1996) Biochemistry , vol.35 , pp. 13568-13578
    • Salomon, A.R.1    Marcinowski, K.J.2    Friedland, R.P.3
  • 22
    • 0013889689 scopus 로고
    • Determination of free amino groups in proteins by trinitrobenzene sulfonic acid
    • Habeeb AF (1966) Determination of free amino groups in proteins by trinitrobenzene sulfonic acid. Anal Biochem 14:328-336
    • (1966) Anal Biochem , vol.14 , pp. 328-336
    • Habeeb, A.F.1
  • 23
    • 0022922108 scopus 로고
    • Characterization of ameboid microglia isolated from developing mammalian brain
    • Giulian D, Baker TJ (1986) Characterization of ameboid microglia isolated from developing mammalian brain. J Neurosci 6:2163-2178
    • (1986) J Neurosci , vol.6 , pp. 2163-2178
    • Giulian, D.1    Baker, T.J.2
  • 25
    • 0022928028 scopus 로고
    • Microassays for superoxide and hydrogen peroxide production and nitroblue tetrazolium reduction using an enzyme immunoassay microplate reader
    • Pick E (1986) Microassays for superoxide and hydrogen peroxide production and nitroblue tetrazolium reduction using an enzyme immunoassay microplate reader. Methods Enzymol 132:407-421
    • (1986) Methods Enzymol , vol.132 , pp. 407-421
    • Pick, E.1
  • 26
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by Congo red spectral shift assay
    • Klunk WE, Jacob RF, Mason RP (1999) Quantifying amyloid by Congo red spectral shift assay. Methods Enzymol 309:285-305
    • (1999) Methods Enzymol , vol.309 , pp. 285-305
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 27
    • 0037223866 scopus 로고    scopus 로고
    • Carnosine promotes the heat denaturation of glycated protein
    • Yeargans GS, Seidler NW (2003) Carnosine promotes the heat denaturation of glycated protein. Biochem Biophys Res Commun 300:75-80
    • (2003) Biochem Biophys Res Commun , vol.300 , pp. 75-80
    • Yeargans, G.S.1    Seidler, N.W.2
  • 28
    • 0034649197 scopus 로고    scopus 로고
    • Glycation of a spartate amino transferase and conformational flexibility
    • Seidler NW, Seibel I (2000) Glycation of a spartate amino transferase and conformational flexibility. Biochem Biophys Res Commun 277:47-50
    • (2000) Biochem Biophys Res Commun , vol.277 , pp. 47-50
    • Seidler, N.W.1    Seibel, I.2
  • 29
    • 33845768784 scopus 로고    scopus 로고
    • Microglia-mediated neurotoxicity: Uncovering the molecular mechanisms
    • Block ML, Zecca L, Hong J (2007) Microglia-mediated neurotoxicity: uncovering the molecular mechanisms. Nat Rev Neurosci 8:57-69
    • (2007) Nat Rev Neurosci , vol.8 , pp. 57-69
    • Block, M.L.1    Zecca, L.2    Hong, J.3
  • 30
    • 0034996659 scopus 로고    scopus 로고
    • Activation of NADPH oxidase by AGE links oxidant stress to altered gene expression via RAGE
    • Wautier MP, Chappey O, Corda S et al (2001) Activation of NADPH oxidase by AGE links oxidant stress to altered gene expression via RAGE. Am J Physiol Endocrinol Metab 280:E685-E694
    • (2001) Am J Physiol Endocrinol Metab , vol.280
    • Wautier, M.P.1    Chappey, O.2    Corda, S.3
  • 31
    • 0027989808 scopus 로고
    • Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis
    • Koopman G, Reutelingsperger CP et al (1994) Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis. Blood 84:1415-1420
    • (1994) Blood , vol.84 , pp. 1415-1420
    • Koopman, G.1    Reutelingsperger, C.P.2
  • 32
    • 2942598335 scopus 로고    scopus 로고
    • Nicotine reduces A beta in the brain and cerebral vessels of APPsw mice
    • Hellstrom-Lindahl E, Court J, Keverne J et al (2004) Nicotine reduces A beta in the brain and cerebral vessels of APPsw mice. Eur J Neurosci 19:2703-2710
    • (2004) Eur J Neurosci , vol.19 , pp. 2703-2710
    • Hellstrom-Lindahl, E.1    Court, J.2    Keverne, J.3
  • 33
    • 0035251815 scopus 로고    scopus 로고
    • Nicotine and its interaction with bamyloid protein: A short review
    • Zamani MR, Allen YS (2001) Nicotine and its interaction with bamyloid protein: a short review. Biol Psychiatry 49:221-232
    • (2001) Biol Psychiatry , vol.49 , pp. 221-232
    • Zamani, M.R.1    Allen, Y.S.2
  • 34
    • 33644892764 scopus 로고    scopus 로고
    • Probing the molecular basis of protein function through chemistry
    • Roelfes G, Mootz HD (2006) Probing the molecular basis of protein function through chemistry. Chem Biochem 7:545-549
    • (2006) Chem Biochem , vol.7 , pp. 545-549
    • Roelfes, G.1    Mootz, H.D.2
  • 35
    • 0035251678 scopus 로고    scopus 로고
    • Nicotine and amyloid formation
    • Zeng H, Zhang Y, Peng LJ et al (2001) Nicotine and amyloid formation. Biol Psychiatry 49:248-257
    • (2001) Biol Psychiatry , vol.49 , pp. 248-257
    • Zeng, H.1    Zhang, Y.2    Peng, L.J.3
  • 36
    • 0031051509 scopus 로고    scopus 로고
    • Smoking and oestrogen-replacement therapy as protective factors for Alzheimer's disease
    • Lerner A, Koss E, Debanne S et al (1997) Smoking and oestrogen- replacement therapy as protective factors for Alzheimer's disease. Lancet 349:403-404
    • (1997) Lancet , vol.349 , pp. 403-404
    • Lerner, A.1    Koss, E.2    Debanne, S.3
  • 37
    • 0029054285 scopus 로고
    • Nicotine patches in Alzheimer's disease: Pilot study on learning, memory, and safety
    • Wilson AL, Langley LK, Monley J et al (1995) Nicotine patches in Alzheimer's disease: pilot study on learning, memory, and safety. Pharmacol Biochem Behav 51:509-514
    • (1995) Pharmacol Biochem Behav , vol.51 , pp. 509-514
    • Wilson, A.L.1    Langley, L.K.2    Monley, J.3
  • 38
    • 0030773730 scopus 로고    scopus 로고
    • Does smoking protect from Alzheimer's disease? Alzheimer-type changes in 301 unselected brains from patients with known smoking history
    • Ulrich J, Johannson-Locher G, Seiler WO et al (1997) Does smoking protect from Alzheimer's disease? Alzheimer-type changes in 301 unselected brains from patients with known smoking history. Acta Neuropathol 94:450-454
    • (1997) Acta Neuropathol , vol.94 , pp. 450-454
    • Ulrich, J.1    Johannson-Locher, G.2    Seiler, W.O.3
  • 39
    • 63849213473 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor signalling: Roles in Alzheimer's disease and amyloid neuroprotection
    • Buckingham SB, Jones AK, Brown LA et al (2009) Nicotinic acetylcholine receptor signalling: roles in Alzheimer's disease and amyloid neuroprotection. Pharmacol Rev 61:39-61
    • (2009) Pharmacol Rev , vol.61 , pp. 39-61
    • Buckingham, S.B.1    Jones, A.K.2    Brown, L.A.3
  • 40
    • 1842453822 scopus 로고    scopus 로고
    • Nicotine attenuates beta-amyloid peptideinduced neurotoxicity, free radical and calcium accumulation in hippocampal neuronal cultures
    • Liu Q, Zhao B (2004) Nicotine attenuates beta-amyloid peptideinduced neurotoxicity, free radical and calcium accumulation in hippocampal neuronal cultures. Br J Pharmacol 141:746-754
    • (2004) Br J Pharmacol , vol.141 , pp. 746-754
    • Liu, Q.1    Zhao, B.2
  • 41
    • 33845660726 scopus 로고    scopus 로고
    • Nicotine attenuates betaamyloid-induced neurotoxicity by regulating metal homeostasis
    • Zhang J, Liu Q, Chen Q et al (2006) Nicotine attenuates betaamyloid-induced neurotoxicity by regulating metal homeostasis. FASEB J 20:1212-1214
    • (2006) FASEB J , vol.20 , pp. 1212-1214
    • Zhang, J.1    Liu, Q.2    Chen, Q.3
  • 42
    • 0034477343 scopus 로고    scopus 로고
    • The conformation alteration of mouse hepatic histones after reaction with nicotine in vitro
    • Wu X, Sun H, Liu Y (2000) The conformation alteration of mouse hepatic histones after reaction with nicotine in vitro. Chin Sci Bull 45:825-829
    • (2000) Chin Sci Bull , vol.45 , pp. 825-829
    • Wu, X.1    Sun, H.2    Liu, Y.3
  • 43
    • 0036498983 scopus 로고    scopus 로고
    • Effects of thermal denaturation on protein glycation
    • Seidler NW, Yeargans GS (2002) Effects of thermal denaturation on protein glycation. Life Sci 70:1789-1799
    • (2002) Life Sci , vol.70 , pp. 1789-1799
    • Seidler, N.W.1    Yeargans, G.S.2
  • 44
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter DC, Ho JX (1994) Structure of serum albumin. Adv Protein Chem 45:153-203
    • (1994) Adv Protein Chem , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 45
    • 0018827178 scopus 로고
    • Temperature behaviour of human serum albumin
    • Wetzel R, Becker M, Behlke J et al (1980) Temperature behaviour of human serum albumin. Eur J Biochem 104:469-478
    • (1980) Eur J Biochem , vol.104 , pp. 469-478
    • Wetzel, R.1    Becker, M.2    Behlke, J.3
  • 46
    • 0017273658 scopus 로고
    • Raman studies of bovine serum albumin
    • Lin VJC, Koenig JL (1976) Raman studies of bovine serum albumin. Biopolymers 15:203-218
    • (1976) Biopolymers , vol.15 , pp. 203-218
    • Lin, V.J.C.1    Koenig, J.L.2
  • 47
    • 0019535245 scopus 로고
    • Electron microscopy of network structures in thermally-induced globular protein gels
    • Clark AH, Judge FJ, Richards JB et al (1981) Electron microscopy of network structures in thermally-induced globular protein gels. Int J Pept Protein Res 17:380-392
    • (1981) Int J Pept Protein Res , vol.17 , pp. 380-392
    • Clark, A.H.1    Judge, F.J.2    Richards, J.B.3
  • 48
    • 0019536747 scopus 로고
    • Infrared and laserraman spectroscopic studies of thermally-induced globular protein gels
    • Clark AH, Saunderson DHP, Suggett A (1981) Infrared and laserraman spectroscopic studies of thermally-induced globular protein gels. Int J Pept Protein Res 17:353-364
    • (1981) Int J Pept Protein Res , vol.17 , pp. 353-364
    • Clark, A.H.1    Saunderson, D.H.P.2    Suggett, A.3
  • 49
    • 29844442152 scopus 로고    scopus 로고
    • Investigation on the surface hydrophobicity and aggregation kinetics of human calprotectin in the presence of calcium
    • Yousefi R, Ardestani SK, Saboury AA et al (2005) Investigation on the surface hydrophobicity and aggregation kinetics of human calprotectin in the presence of calcium. J Biochem Mol Biol 38:407-413
    • (2005) J Biochem Mol Biol , vol.38 , pp. 407-413
    • Yousefi, R.1    Ardestani, S.K.2    Saboury, A.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.