메뉴 건너뛰기




Volumn 3, Issue 1, 2011, Pages

The protective effects of plasma gelsolin on stroke outcome in rats

Author keywords

Endothelin 1 induced mcao; Ischemic stroke; Plasma gelsolin; Protective effect

Indexed keywords

ACTIN BINDING PROTEIN; ALTEPLASE; CALCIUM BINDING PROTEIN; CALCIUM CHANNEL; ENDOTHELIN 1; GELSOLIN; TRIPHENYLTETRAZOLIUM;

EID: 81255138901     PISSN: None     EISSN: 20407378     Source Type: Journal    
DOI: 10.1186/2040-7378-3-13     Document Type: Article
Times cited : (24)

References (44)
  • 5
    • 0033512004 scopus 로고    scopus 로고
    • Inflammatory mediators and stroke: new opportunities for novel therapeutics
    • Barone FC, Feuerstein GZ. Inflammatory mediators and stroke: new opportunities for novel therapeutics. J Cereb Blood Flow Metab 1999, 19:819-34.
    • (1999) J Cereb Blood Flow Metab , vol.19 , pp. 819-834
    • Barone, F.C.1    Feuerstein, G.Z.2
  • 9
    • 0022487183 scopus 로고
    • Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain
    • Kwiatkowski DJ, Stossel TP, Orkin SH, Mole JE, Colten HR, Yin HL. Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. Nature 1986, 323:455-8.
    • (1986) Nature , vol.323 , pp. 455-458
    • Kwiatkowski, D.J.1    Stossel, T.P.2    Orkin, S.H.3    Mole, J.E.4    Colten, H.R.5    Yin, H.L.6
  • 10
    • 0018667209 scopus 로고
    • Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein
    • Yin HL, Stossel TP. Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein. Nature 1979, 281:583-6.
    • (1979) Nature , vol.281 , pp. 583-586
    • Yin, H.L.1    Stossel, T.P.2
  • 11
    • 0023241956 scopus 로고
    • Capacity of human serum to depolymerize actin filaments
    • Janmey PA, Lind SE. Capacity of human serum to depolymerize actin filaments. Blood 1987, 70:524-30.
    • (1987) Blood , vol.70 , pp. 524-530
    • Janmey, P.A.1    Lind, S.E.2
  • 12
    • 0021356287 scopus 로고
    • Structure and biosynthesis of cytoplasmic and secreted variants of gelsolin
    • Yin HL, Kwiatkowski DJ, Mole JE, Cole FS. Structure and biosynthesis of cytoplasmic and secreted variants of gelsolin. J Biol Chem 1984, 259:5271-6.
    • (1984) J Biol Chem , vol.259 , pp. 5271-5276
    • Yin, H.L.1    Kwiatkowski, D.J.2    Mole, J.E.3    Cole, F.S.4
  • 13
    • 0022483525 scopus 로고
    • Role of plasma gelsolin and the vitamin D-binding protein in clearing actin from the circulation
    • Lind SE, Smith DB, Janmey PA, Stossel TP. Role of plasma gelsolin and the vitamin D-binding protein in clearing actin from the circulation. J Clin Invest 1986, 78:736-42.
    • (1986) J Clin Invest , vol.78 , pp. 736-742
    • Lind, S.E.1    Smith, D.B.2    Janmey, P.A.3    Stossel, T.P.4
  • 14
    • 0242569370 scopus 로고    scopus 로고
    • Proteomics analysis of phosphotyrosyl-proteins in human lumbar cerebrospinal fluid
    • Yuan X, Desiderio DM. Proteomics analysis of phosphotyrosyl-proteins in human lumbar cerebrospinal fluid. J Proteome Res 2003, 2:476-87.
    • (2003) J Proteome Res , vol.2 , pp. 476-487
    • Yuan, X.1    Desiderio, D.M.2
  • 15
    • 0022971813 scopus 로고
    • Interaction of plasma gelsolin with ADP-actin
    • Coue M, Korn ED. Interaction of plasma gelsolin with ADP-actin. J Biol Chem 1986, 261:3628-31.
    • (1986) J Biol Chem , vol.261 , pp. 3628-3631
    • Coue, M.1    Korn, E.D.2
  • 16
    • 0026569069 scopus 로고
    • The extracellular actin-scavenger system and actin toxicity
    • Lee WM, Galbraith RM. The extracellular actin-scavenger system and actin toxicity. N Engl J Med 1992, 326:1335-41.
    • (1992) N Engl J Med , vol.326 , pp. 1335-1341
    • Lee, W.M.1    Galbraith, R.M.2
  • 18
    • 0020336060 scopus 로고
    • Further characterization of the Ca2+-dependent F-actin-depolymerizing protein of human serum
    • Thorstensson R, Utter G, Norberg R. Further characterization of the Ca2+-dependent F-actin-depolymerizing protein of human serum. Eur J Biochem 1982, 126:11-6.
    • (1982) Eur J Biochem , vol.126 , pp. 11-16
    • Thorstensson, R.1    Utter, G.2    Norberg, R.3
  • 19
    • 0023751926 scopus 로고
    • Depression of gelsolin levels and detection of gelsolin-actin complexes in plasma of patients with acute lung injury
    • Lind SE, Smith DB, Janmey PA, Stossel TP. Depression of gelsolin levels and detection of gelsolin-actin complexes in plasma of patients with acute lung injury. Am Rev Respir Dis 1988, 138:429-34.
    • (1988) Am Rev Respir Dis , vol.138 , pp. 429-434
    • Lind, S.E.1    Smith, D.B.2    Janmey, P.A.3    Stossel, T.P.4
  • 24
    • 0032322955 scopus 로고    scopus 로고
    • Quantitative electroencephalographic changes due to middle cerebral artery occlusion by endothelin 1 in conscious rats
    • Moyanova S, Kortenska L, Kirov R, Iliev I. Quantitative electroencephalographic changes due to middle cerebral artery occlusion by endothelin 1 in conscious rats. Arch Physiol Biochem 1998, 106:384-91.
    • (1998) Arch Physiol Biochem , vol.106 , pp. 384-391
    • Moyanova, S.1    Kortenska, L.2    Kirov, R.3    Iliev, I.4
  • 25
    • 0034794176 scopus 로고    scopus 로고
    • A serial MR study of cerebral blood flow changes and lesion development following endothelin-1-induced ischemia in rats
    • Biernaskie J, Corbett D, Peeling J, Wells J, Lei H. A serial MR study of cerebral blood flow changes and lesion development following endothelin-1-induced ischemia in rats. Magn Reson Med 2001, 46:827-30.
    • (2001) Magn Reson Med , vol.46 , pp. 827-830
    • Biernaskie, J.1    Corbett, D.2    Peeling, J.3    Wells, J.4    Lei, H.5
  • 26
    • 0030043728 scopus 로고    scopus 로고
    • Laser-Doppler evaluation of rat brain microcirculation: comparison with the [14C]-iodoantipyrine method suggests discordance during cerebral blood flow increases
    • Fabricius M, Lauritzen M. Laser-Doppler evaluation of rat brain microcirculation: comparison with the [14C]-iodoantipyrine method suggests discordance during cerebral blood flow increases. J Cereb Blood Flow Metab 1996, 16:156-61.
    • (1996) J Cereb Blood Flow Metab , vol.16 , pp. 156-161
    • Fabricius, M.1    Lauritzen, M.2
  • 27
    • 0033950675 scopus 로고    scopus 로고
    • CNS plasticity and assessment of forelimb sensorimotor outcome in unilateral rat models of stroke, cortical ablation, parkinsonism and spinal cord injury
    • Schallert T, Fleming SM, Leasure JL, Tillerson JL, Bland ST. CNS plasticity and assessment of forelimb sensorimotor outcome in unilateral rat models of stroke, cortical ablation, parkinsonism and spinal cord injury. Neuropharmacology 2000, 39:777-87.
    • (2000) Neuropharmacology , vol.39 , pp. 777-787
    • Schallert, T.1    Fleming, S.M.2    Leasure, J.L.3    Tillerson, J.L.4    Bland, S.T.5
  • 29
    • 0027164675 scopus 로고
    • Perivascular microapplication of endothelin-1: a new model of focal cerebral ischaemia in the rat
    • Sharkey J, Ritchie IM, Kelly PA. Perivascular microapplication of endothelin-1: a new model of focal cerebral ischaemia in the rat. J Cereb Blood Flow Metab 1993, 13:865-71.
    • (1993) J Cereb Blood Flow Metab , vol.13 , pp. 865-871
    • Sharkey, J.1    Ritchie, I.M.2    Kelly, P.A.3
  • 31
    • 0034635549 scopus 로고    scopus 로고
    • Gelsolin in complex with phosphatidylinositol 4, 5-bisphosphate inhibits caspase-3 and -9 to retard apoptotic progression
    • Azuma T, Koths K, Flanagan L, Kwiatkowski D. Gelsolin in complex with phosphatidylinositol 4, 5-bisphosphate inhibits caspase-3 and -9 to retard apoptotic progression. J Biol Chem 2000, 275:3761-6.
    • (2000) J Biol Chem , vol.275 , pp. 3761-3766
    • Azuma, T.1    Koths, K.2    Flanagan, L.3    Kwiatkowski, D.4
  • 32
    • 41149124866 scopus 로고    scopus 로고
    • Inhibition of histone deacetylation protects wildtype but not gelsolin-deficient mice from ischemic brain injury
    • Yildirim F, Gertz K, Kronenberg G, Harms C, Fink KB, Meisel A, Endres M. Inhibition of histone deacetylation protects wildtype but not gelsolin-deficient mice from ischemic brain injury. Exp Neurol 2008, 210:531-42.
    • (2008) Exp Neurol , vol.210 , pp. 531-542
    • Yildirim, F.1    Gertz, K.2    Kronenberg, G.3    Harms, C.4    Fink, K.B.5    Meisel, A.6    Endres, M.7
  • 33
    • 0030807917 scopus 로고    scopus 로고
    • The actin-severing protein gelsolin modulates calcium channel and NMDA receptor activities and vulnerability to excitotoxicity in hippocampal neurons
    • Furukawa K, Fu W, Li Y, Witke W, Kwiatkowski DJ, Mattson MP. The actin-severing protein gelsolin modulates calcium channel and NMDA receptor activities and vulnerability to excitotoxicity in hippocampal neurons. J Neurosci 1997, 17:8178-86.
    • (1997) J Neurosci , vol.17 , pp. 8178-8186
    • Furukawa, K.1    Fu, W.2    Li, Y.3    Witke, W.4    Kwiatkowski, D.J.5    Mattson, M.P.6
  • 37
    • 0032531960 scopus 로고    scopus 로고
    • Gelsolin and functionally similar actin-binding proteins are regulated by lysophosphatidic acid
    • Meerschaert K, De Corte V, De Ville Y, Vandekerckhove J, Gettemans J. Gelsolin and functionally similar actin-binding proteins are regulated by lysophosphatidic acid. EMBO J 1998, 17:5923-32.
    • (1998) EMBO J , vol.17 , pp. 5923-5932
    • Meerschaert, K.1    De Corte, V.2    De Ville, Y.3    Vandekerckhove, J.4    Gettemans, J.5
  • 39
  • 40
    • 57049140460 scopus 로고    scopus 로고
    • [Relationship between plasma lysophosphatidic acid levels and prognosis of ischemic stroke]
    • Lou XL, Zhan XP, Li XP. [Relationship between plasma lysophosphatidic acid levels and prognosis of ischemic stroke]. Zhongguo Wei Zhong Bing Ji Jiu Yi Xue 2008, 20:689-90.
    • (2008) Zhongguo Wei Zhong Bing Ji Jiu Yi Xue , vol.20 , pp. 689-690
    • Lou, X.L.1    Zhan, X.P.2    Li, X.P.3
  • 41
    • 35148874280 scopus 로고    scopus 로고
    • Lysophosphatidic acid regulates inflammation-related genes in human endothelial cells through LPA1 and LPA3
    • Lin CI, Chen CN, Lin PW, Chang KJ, Hsieh FJ, Lee H. Lysophosphatidic acid regulates inflammation-related genes in human endothelial cells through LPA1 and LPA3. Biochem Biophys Res Commun 2007, 363:1001-8.
    • (2007) Biochem Biophys Res Commun , vol.363 , pp. 1001-1008
    • Lin, C.I.1    Chen, C.N.2    Lin, P.W.3    Chang, K.J.4    Hsieh, F.J.5    Lee, H.6
  • 42
    • 84989065240 scopus 로고
    • Detection of the actin scavenger system in burn wound fluid
    • Grinnell F, Baxter CR, Zhu M, Yin HL. Detection of the actin scavenger system in burn wound fluid. Wound Repair Regen 1993, 1:236-43.
    • (1993) Wound Repair Regen , vol.1 , pp. 236-243
    • Grinnell, F.1    Baxter, C.R.2    Zhu, M.3    Yin, H.L.4
  • 43
    • 84857353057 scopus 로고    scopus 로고
    • In Vivo Evidence that the Increase in Matrix Metalloproteinase Activity Occurs Early after Cerebral Ischemia
    • Martin A, Garofalakis A, Tavitian B. In Vivo Evidence that the Increase in Matrix Metalloproteinase Activity Occurs Early after Cerebral Ischemia. Mol Imaging
    • Mol Imaging
    • Martin, A.1    Garofalakis, A.2    Tavitian, B.3
  • 44
    • 0029822375 scopus 로고    scopus 로고
    • Degradation of cross-linked fibrin by matrix metalloproteinase 3 (stromelysin 1): hydrolysis of the gamma Gly 404-Ala 405 peptide bond
    • Bini A, Itoh Y, Kudryk BJ, Nagase H. Degradation of cross-linked fibrin by matrix metalloproteinase 3 (stromelysin 1): hydrolysis of the gamma Gly 404-Ala 405 peptide bond. Biochemistry 1996, 35:13056-63.
    • (1996) Biochemistry , vol.35 , pp. 13056-13063
    • Bini, A.1    Itoh, Y.2    Kudryk, B.J.3    Nagase, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.