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Volumn 7, Issue 2, 2012, Pages 146-151

Tissue plasminogen activator-independent roles of neuroserpin in the central nervous system

Author keywords

Cerebral ischemia; Familial encephalopathy with neuroserpin inclusion bodies; Neuroserpin; Serpin; Tissue type plasminogen activator; Tumor

Indexed keywords

CADHERIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; NEUROSERPIN; PLASMIN; TISSUE PLASMINOGEN ACTIVATOR;

EID: 84856426234     PISSN: 16735374     EISSN: 18767958     Source Type: Journal    
DOI: 10.3969/j.issn.1673-5374.2012.02.012     Document Type: Article
Times cited : (6)

References (59)
  • 1
    • 0024454850 scopus 로고
    • Purification of axonin-1, a protein that is secreted from axons during neurogenesis
    • Ruegg MA, Stoeckli ET, Kuhn TB, et al. Purification of axonin-1, a protein that is secreted from axons during neurogenesis. EMBO J. 1989;8(1):55-63.
    • (1989) EMBO J. , vol.8 , Issue.1 , pp. 55-63
    • Ruegg, M.A.1    Stoeckli, E.T.2    Kuhn, T.B.3
  • 2
    • 0031452755 scopus 로고    scopus 로고
    • Neuroserpin, a brain-associated inhibitor of tissue plasminogen activator is localized primarily in neurons. Implications for the regulation of motor learning and neuronal survival
    • Hastings GA, Coleman TA, Haudenschild CC, et al. Neuroserpin, a brain-associated inhibitor of tissue plasminogen activator is localized primarily in neurons. Implications for the regulation of motor learning and neuronal survival. J Biol Chem. 1997;272(52): 33062-33067.
    • (1997) J Biol Chem. , vol.272 , Issue.52 , pp. 33062-33067
    • Hastings, G.A.1    Coleman, T.A.2    Haudenschild, C.C.3
  • 3
    • 0029977875 scopus 로고    scopus 로고
    • Neuroserpin, an axonally secreted serine protease inhibitor
    • Osterwalder T, Contartese J, Stoeckli ET, et al. Neuroserpin, an axonally secreted serine protease inhibitor. EMBO J. 1996;15(12): 2944-2953.
    • (1996) EMBO J. , vol.15 , Issue.12 , pp. 2944-2953
    • Osterwalder, T.1    Contartese, J.2    Stoeckli, E.T.3
  • 4
    • 0033401819 scopus 로고    scopus 로고
    • Neuronal depolarization enhances the transcription of the neuronal serine protease inhibitor neuroserpin
    • Berger P, Kozlov SV, Cinelli P, et al. Neuronal depolarization enhances the transcription of the neuronal serine protease inhibitor neuroserpin. Mol Cell Neurosci. 1999;14(6):455-467.
    • (1999) Mol Cell Neurosci. , vol.14 , Issue.6 , pp. 455-467
    • Berger, P.1    Kozlov, S.V.2    Cinelli, P.3
  • 5
    • 0030690117 scopus 로고    scopus 로고
    • Expression of neuroserpin, an inhibitor of tissue plasminogen activator, in the developing and adult nervous system of the mouse
    • Krueger SR, Ghisu GP, Cinelli P, et al. Expression of neuroserpin, an inhibitor of tissue plasminogen activator, in the developing and adult nervous system of the mouse. J Neurosci. 1997;17(23): 8984-8996.
    • (1997) J Neurosci. , vol.17 , Issue.23 , pp. 8984-8996
    • Krueger, S.R.1    Ghisu, G.P.2    Cinelli, P.3
  • 6
    • 77649266122 scopus 로고    scopus 로고
    • Neuroserpin is expressed in early stage of neurogenesis in adult rat hippocampus
    • Yamada M, Takahashi K, Ukai W, et al. Neuroserpin is expressed in early stage of neurogenesis in adult rat hippocampus. Neuroreport. 2010;21(2):138-142.
    • (2010) Neuroreport. , vol.21 , Issue.2 , pp. 138-142
    • Yamada, M.1    Takahashi, K.2    Ukai, W.3
  • 7
    • 0026453524 scopus 로고
    • The expression of tissue and urokinase-type plasminogen activators in neural development suggests different modes of proteolytic involvement in neuronal growth
    • Sumi Y, Dent MA, Owen DE, et al. The expression of tissue and urokinase-type plasminogen activators in neural development suggests different modes of proteolytic involvement in neuronal growth. Development. 1992;116(3):625-637.
    • (1992) Development. , vol.116 , Issue.3 , pp. 625-637
    • Sumi, Y.1    Dent, M.A.2    Owen, D.E.3
  • 8
    • 3242688902 scopus 로고    scopus 로고
    • Tissue-type plasminogen activator and neuroserpin: A well-balanced act in the nervous system?
    • Yepes M, Lawrence DA. Tissue-type plasminogen activator and neuroserpin: a well-balanced act in the nervous system? Trends Cardiovasc Med. 2004;14(5):173-180.
    • (2004) Trends Cardiovasc Med. , vol.14 , Issue.5 , pp. 173-180
    • Yepes, M.1    Lawrence, D.A.2
  • 9
    • 10044224511 scopus 로고    scopus 로고
    • New functions for an old enzyme: Nonhemostatic roles for tissue-type plasminogen activator in the central nervous system
    • Yepes M, Lawrence DA. New functions for an old enzyme: nonhemostatic roles for tissue-type plasminogen activator in the central nervous system. Exp Biol Med. 2004;229(11):1097-1104.
    • (2004) Exp Biol Med. , vol.229 , Issue.11 , pp. 1097-1104
    • Yepes, M.1    Lawrence, D.A.2
  • 10
    • 9444240943 scopus 로고
    • Mice lacking the gene encoding tissue-type plasminogen activator show a selective interference with late-phase long-term potentiation in both Schaffer collateral and mossy fiber pathways
    • Huang YY, Bach ME, Lipp HP, et al. Mice lacking the gene encoding tissue-type plasminogen activator show a selective interference with late-phase long-term potentiation in both Schaffer collateral and mossy fiber pathways. Proc Natl Acad Sci U S A. 1966;93(16):8699-8704.
    • (1966) Proc Natl Acad Sci U S A. , vol.93 , Issue.16 , pp. 8699-8704
    • Huang, Y.Y.1    Bach, M.E.2    Lipp, H.P.3
  • 11
    • 5644251587 scopus 로고    scopus 로고
    • Cleavage of proBDNF by tPA/plasmin is essential for long-term hippocampal plasticity
    • Pang PT, Teng HK, Zaitsev E, et al. Cleavage of proBDNF by tPA/plasmin is essential for long-term hippocampal plasticity. Science. 2004;306(5695):487-491.
    • (2004) Science. , vol.306 , Issue.5695 , pp. 487-491
    • Pang, P.T.1    Teng, H.K.2    Zaitsev, E.3
  • 12
    • 0037031298 scopus 로고    scopus 로고
    • Adjuvant treatment with neuroserpin increases the therapeutic window for tissue-type plasminogen activator administration in a rat model of embolic stroke
    • Zhang Z, Zhang L, Yepes M, et al. Adjuvant treatment with neuroserpin increases the therapeutic window for tissue-type plasminogen activator administration in a rat model of embolic stroke. Circulation. 2002;106(6):740-745.
    • (2002) Circulation. , vol.106 , Issue.6 , pp. 740-745
    • Zhang, Z.1    Zhang, L.2    Yepes, M.3
  • 13
    • 0036084622 scopus 로고    scopus 로고
    • Regulation of seizure spreading by neuroserpin and tissue-type plasminogen activator is plasminogen independent
    • Yepes M, Sandkvist M, Coleman TA, et al. Regulation of seizure spreading by neuroserpin and tissue-type plasminogen activator is plasminogen independent. J Clin Invest. 2002;109(12): 1571-1578.
    • (2002) J Clin Invest. , vol.109 , Issue.12 , pp. 1571-1578
    • Yepes, M.1    Sandkvist, M.2    Coleman, T.A.3
  • 14
    • 0031951510 scopus 로고    scopus 로고
    • Tissue plasminogen activator (tPA) increases neuronal damage after focal cerebral ischemia in wild-type and tPA-deficient mice
    • Wang YF, Tsirka SE, Strickland S, et al. Tissue plasminogen activator (tPA) increases neuronal damage after focal cerebral ischemia in wild-type and tPA-deficient mice. Nat Med. 1998;4(2): 228-231.
    • (1998) Nat Med. , vol.4 , Issue.2 , pp. 228-231
    • Wang, Y.F.1    Tsirka, S.E.2    Strickland, S.3
  • 16
    • 0035823595 scopus 로고    scopus 로고
    • The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
    • Silverman GA, Bird PI, Carrell RW, et al. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J Biol Chem. 2001; 276(36):33293-33296
    • (2001) J Biol Chem. , vol.276 , Issue.36 , pp. 33293-33296
    • Silverman, G.A.1    Bird, P.I.2    Carrell, R.W.3
  • 17
    • 67650713938 scopus 로고    scopus 로고
    • Conformational pathology of the serpins: Themes, variations, and therapeutic strategies
    • Gooptu B, Lomas DA. Conformational pathology of the serpins: themes, variations, and therapeutic strategies. Annu Rev Biochem. 2009;78:147-176.
    • (2009) Annu Rev Biochem. , vol.78 , pp. 147-176
    • Gooptu, B.1    Lomas, D.A.2
  • 18
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington JA, Read RJ, Carrell RW. Structure of a serpin-protease complex shows inhibition by deformation. Nature. 2000; 407(6806):923-926.
    • (2000) Nature. , vol.407 , Issue.6806 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 19
    • 63449087596 scopus 로고    scopus 로고
    • Human neuroserpin: Structure and time-dependent inhibition
    • Ricagno S, Caccia S, Sorrentino G, et al. Human neuroserpin: structure and time-dependent inhibition. J Mol Biol. 2009;388(1): 109-121.
    • (2009) J Mol Biol. , vol.388 , Issue.1 , pp. 109-121
    • Ricagno, S.1    Caccia, S.2    Sorrentino, G.3
  • 20
    • 33645078896 scopus 로고    scopus 로고
    • Neuroserpin: A serpin to think about
    • Miranda E, Lomas DA. Neuroserpin: a serpin to think about. Cell Mol Life Sci. 2006;63(6):709-722.
    • (2006) Cell Mol Life Sci. , vol.63 , Issue.6 , pp. 709-722
    • Miranda, E.1    Lomas, D.A.2
  • 21
    • 60449094498 scopus 로고    scopus 로고
    • Heart disease and stroke statistics--2009 update: A report from the American Heart Association Statistics Committee and Stroke Statistics Subcommittee
    • Lloyd-Jones D, Adams R, Carnethon M, et al. Heart disease and stroke statistics--2009 update: a report from the American Heart Association Statistics Committee and Stroke Statistics Subcommittee. Circulation. 2009;119(3):480-486.
    • (2009) Circulation. , vol.119 , Issue.3 , pp. 480-486
    • Lloyd-Jones, D.1    Adams, R.2    Carnethon, M.3
  • 22
    • 48249103532 scopus 로고    scopus 로고
    • Tissue plasminogen activator (tPA) and matrix metalloproteinases in the pathogenesis of stroke: Therapeutic strategies
    • Adibhatla RM, Hatcher JF. Tissue plasminogen activator (tPA) and matrix metalloproteinases in the pathogenesis of stroke: therapeutic strategies. CNS Neurol Disord Drug Targets. 2008; 7(3):243-253.
    • (2008) CNS Neurol Disord Drug Targets. , vol.7 , Issue.3 , pp. 243-253
    • Adibhatla, R.M.1    Hatcher, J.F.2
  • 23
    • 0028783948 scopus 로고
    • Tissue plasminogen activator for acute ischemic stroke
    • The National Institute of Neurological Disorders and Stroke rtPA Stroke Study Group
    • The National Institute of Neurological Disorders and Stroke rtPA Stroke Study Group. Tissue plasminogen activator for acute ischemic stroke. N Engl J Med. 1995;333(24):1581-1587.
    • (1995) N Engl J Med. , vol.333 , Issue.24 , pp. 1581-1587
  • 24
    • 0034746189 scopus 로고    scopus 로고
    • The proteolytic activity of tissue-plasminogen activator enhances NMDA receptor-mediated signaling
    • Nicole O, Docagne F, Ali C, et al. The proteolytic activity of tissue-plasminogen activator enhances NMDA receptor-mediated signaling. Nat Med. 2001;7(1):59-64.
    • (2001) Nat Med. , vol.7 , Issue.1 , pp. 59-64
    • Nicole, O.1    Docagne, F.2    Ali, C.3
  • 25
    • 28344454373 scopus 로고    scopus 로고
    • The brain-specific tissue-type plasminogen activator inhibitor, neuroserpin, protects neurons against excitotoxicity both in vitro and in vivo
    • Lebeurrier N, Liot G, Lopez-Atalaya JP, et al. The brain-specific tissue-type plasminogen activator inhibitor, neuroserpin, protects neurons against excitotoxicity both in vitro and in vivo. Mol Cell Neurosci. 2005;30(4):552-558.
    • (2005) Mol Cell Neurosci. , vol.30 , Issue.4 , pp. 552-558
    • Lebeurrier, N.1    Liot, G.2    Lopez-Atalaya, J.P.3
  • 26
    • 34548140119 scopus 로고    scopus 로고
    • Tissue plasminogen activator: Beyond thrombolysis
    • Benarroch EE. Tissue plasminogen activator: beyond thrombolysis. Neurology. 2007;69(8):799-802.
    • (2007) Neurology. , vol.69 , Issue.8 , pp. 799-802
    • Benarroch, E.E.1
  • 27
    • 0034661923 scopus 로고    scopus 로고
    • Neuroserpin reduces cerebral infarct volume and protects neurons from ischemia-induced apoptosis
    • Yepes M, Sandkvist M, Wong MK, et al. Neuroserpin reduces cerebral infarct volume and protects neurons from ischemia-induced apoptosis. Blood. 2000;96(2):569-576.
    • (2000) Blood. , vol.96 , Issue.2 , pp. 569-576
    • Yepes, M.1    Sandkvist, M.2    Wong, M.K.3
  • 28
    • 0035652035 scopus 로고    scopus 로고
    • Neuroserpin, a neuroprotective factor in focal ischemic stroke
    • Cinelli P, Madani R, Tsuzuki N, et al. Neuroserpin, a neuroprotective factor in focal ischemic stroke. Mol Cell Neurosci. 2001;18(5):443-457.
    • (2001) Mol Cell Neurosci. , vol.18 , Issue.5 , pp. 443-457
    • Cinelli, P.1    Madani, R.2    Tsuzuki, N.3
  • 29
    • 79951581270 scopus 로고    scopus 로고
    • Neuroprotective effect of neuroserpin in rat primary cortical cultures after oxygen and glucose deprivation and tPA
    • Rodríguez-González R, Agulla J, Pérez-Mato M, et al. Neuroprotective effect of neuroserpin in rat primary cortical cultures after oxygen and glucose deprivation and tPA. Neurochem Int. 2011;58(3):337-343.
    • (2011) Neurochem Int. , vol.58 , Issue.3 , pp. 337-343
    • Rodríguez-González, R.1    Agulla, J.2    Pérez-Mato, M.3
  • 30
    • 33746933820 scopus 로고    scopus 로고
    • Tissue-type plasminogen activator rescues neurones from serum deprivation-induced apoptosis through a mechanism independent of its proteolytic activity
    • Liot G, Roussel BD, Lebeurrier N, et al. Tissue-type plasminogen activator rescues neurones from serum deprivation-induced apoptosis through a mechanism independent of its proteolytic activity. J Neurochem. 2006;98(5):1458-1464.
    • (2006) J Neurochem. , vol.98 , Issue.5 , pp. 1458-1464
    • Liot, G.1    Roussel, B.D.2    Lebeurrier, N.3
  • 31
    • 77953182892 scopus 로고    scopus 로고
    • Tissue-type plasminogen activator is a neuroprotectant in the mouse hippocampus
    • Echeverry R, Wu J, Haile WB, et al. Tissue-type plasminogen activator is a neuroprotectant in the mouse hippocampus. J Clin Invest. 2010;120(6):2194-2205.
    • (2010) J Clin Invest. , vol.120 , Issue.6 , pp. 2194-2205
    • Echeverry, R.1    Wu, J.2    Haile, W.B.3
  • 32
    • 0033597411 scopus 로고    scopus 로고
    • Nonproteolytic neuroprotection by human recombinant tissue plasminogen activator
    • Kim YH, Park JH, Hong SH, et al. Nonproteolytic neuroprotection by human recombinant tissue plasminogen activator. Science. 1999;284(54):647-650.
    • (1999) Science. , vol.284 , Issue.54 , pp. 647-650
    • Kim, Y.H.1    Park, J.H.2    Hong, S.H.3
  • 33
    • 78149324499 scopus 로고    scopus 로고
    • Neuroserpin protects neurons from ischemia-induced plasmin-mediated cell death independently of tissue-type plasminogen activator inhibition
    • Wu J, Echeverry R, Guzman J, et al. Neuroserpin protects neurons from ischemia-induced plasmin-mediated cell death independently of tissue-type plasminogen activator inhibition. Am J Pathol. 2010;177(5):2576-2584.
    • (2010) Am J Pathol. , vol.177 , Issue.5 , pp. 2576-2584
    • Wu, J.1    Echeverry, R.2    Guzman, J.3
  • 34
    • 44849132907 scopus 로고    scopus 로고
    • Deleterious effects of plasminogen activators in neonatal cerebral hypoxia-ischemia
    • Adhami F, Yu D, Yin W, et al. Deleterious effects of plasminogen activators in neonatal cerebral hypoxia-ischemia. Am J Pathol. 2008;172(6):1704-1716.
    • (2008) Am J Pathol. , vol.172 , Issue.6 , pp. 1704-1716
    • Adhami, F.1    Yu, D.2    Yin, W.3
  • 35
    • 0242363128 scopus 로고    scopus 로고
    • The contribution of protease-activated receptor 1 to neuronal damage caused by transient focal cerebral ischemia
    • Junge CE, Sugawara T, Mannaioni G, et al. The contribution of protease-activated receptor 1 to neuronal damage caused by transient focal cerebral ischemia. Proc Natl Acad Sci U S A. 2003;100(22):13019-13024.
    • (2003) Proc Natl Acad Sci U S A. , vol.100 , Issue.22 , pp. 13019-13024
    • Junge, C.E.1    Sugawara, T.2    Mannaioni, G.3
  • 36
    • 33847067475 scopus 로고    scopus 로고
    • A Study of the oxidation-induced conformational and functional changes in neuroserpin
    • Mohsenifar A, Lotfi AS, Ranjbar B, et al. A Study of the oxidation-induced conformational and functional changes in neuroserpin. Iran Biomed J. 2007;11(1):41-46.
    • (2007) Iran Biomed J. , vol.11 , Issue.1 , pp. 41-46
    • Mohsenifar, A.1    Lotfi, A.S.2    Ranjbar, B.3
  • 37
    • 77749289262 scopus 로고    scopus 로고
    • Neuroserpin, a thrombolytic serine protease inhibitor (serpin), blocks transplant vasculopathy with associated modification of T-helper cell subsets
    • Munuswamy-Ramanujam G, Dai E, Liu L, et al. Neuroserpin, a thrombolytic serine protease inhibitor (serpin), blocks transplant vasculopathy with associated modification of T-helper cell subsets. Thromb Haemost. 2010;103(3):545-555.
    • (2010) Thromb Haemost. , vol.103 , Issue.3 , pp. 545-555
    • Munuswamy-Ramanujam, G.1    Dai, E.2    Liu, L.3
  • 38
    • 0031568893 scopus 로고    scopus 로고
    • Human neuroserpin (PI12): CDNA cloning and chromosomal localization to 3q26
    • Schrimpf SP, Bleiker AJ, Brecevic L, et al. Human neuroserpin (PI12): cDNA cloning and chromosomal localization to 3q26. Genomics. 1997;40(1):55-62.
    • (1997) Genomics. , vol.40 , Issue.1 , pp. 55-62
    • Schrimpf, S.P.1    Bleiker, A.J.2    Brecevic, L.3
  • 39
    • 0033795221 scopus 로고    scopus 로고
    • Tissue-specific cancer-related serpin gene cluster at human chromosome band 3q26
    • Chang WS, Chang NT, Lin SC, et al. Tissue-specific cancer-related serpin gene cluster at human chromosome band 3q26. Genes Chromosomes Cancer. 2000;29(3):240-255.
    • (2000) Genes Chromosomes Cancer. , vol.29 , Issue.3 , pp. 240-255
    • Chang, W.S.1    Chang, N.T.2    Lin, S.C.3
  • 40
    • 20344378684 scopus 로고    scopus 로고
    • Neuroserpin (PI-12) is upregulated in high-grade prostate cancer and is associated with survival
    • Hasumi H, Ishiguro H, Nakamura M, et al. Neuroserpin (PI-12) is upregulated in high-grade prostate cancer and is associated with survival. Int J Cancer. 2005;115(6):911-916.
    • (2005) Int J Cancer. , vol.115 , Issue.6 , pp. 911-916
    • Hasumi, H.1    Ishiguro, H.2    Nakamura, M.3
  • 41
    • 33947204625 scopus 로고    scopus 로고
    • Gene expression profiling reveals Potential biomarkers of human hepatocellular carcinoma
    • Jia HL, Ye QH, Qin LX, et al. Gene expression profiling reveals Potential biomarkers of human hepatocellular carcinoma. Clin Cancer Res. 2007;13(4):1133-1139.
    • (2007) Clin Cancer Res. , vol.13 , Issue.4 , pp. 1133-1139
    • Jia, H.L.1    Ye, Q.H.2    Qin, L.X.3
  • 42
    • 67651122900 scopus 로고    scopus 로고
    • c-Myc regulates the coordinated transcription of brain disease-related PDCD10-SERPINI1 bidirectional gene pair
    • Chen PY, Chang WS, Lai YK, et al. c-Myc regulates the coordinated transcription of brain disease-related PDCD10-SERPINI1 bidirectional gene pair. Mol Cell Neurosci. 2009;42(1):23-32.
    • (2009) Mol Cell Neurosci. , vol.42 , Issue.1 , pp. 23-32
    • Chen, P.Y.1    Chang, W.S.2    Lai, Y.K.3
  • 43
    • 0037071891 scopus 로고    scopus 로고
    • Maspin sensitizes breast carcinoma cells to induced apoptosis
    • Jiang N, Meng Y, Zhang S, et al. Maspin sensitizes breast carcinoma cells to induced apoptosis. Oncogene. 2002;21(26): 4089-4098.
    • (2002) Oncogene. , vol.21 , Issue.26 , pp. 4089-4098
    • Jiang, N.1    Meng, Y.2    Zhang, S.3
  • 44
    • 0042062324 scopus 로고    scopus 로고
    • Roles of pericellular proteolysis by membrane type-1 matrix metalloproteinase in cancer invasion and angiogenesis
    • Seiki M, Yana I. Roles of pericellular proteolysis by membrane type-1 matrix metalloproteinase in cancer invasion and angiogenesis. Cancer Sci. 2003;94(7):569-574.
    • (2003) Cancer Sci. , vol.94 , Issue.7 , pp. 569-574
    • Seiki, M.1    Yana, I.2
  • 45
    • 0034141363 scopus 로고    scopus 로고
    • Neuroserpin is expressed in the pituitary and adrenal glands and induces the extension of neurite-like processes in AtT-20 cells
    • Hill RM, Parmar PK, Coates LC, et al. Neuroserpin is expressed in the pituitary and adrenal glands and induces the extension of neurite-like processes in AtT-20 cells. Biochem J. 2000;345(Pt 3): 595-601.
    • (2000) Biochem J. , vol.345 , Issue.PART 3 , pp. 595-601
    • Hill, R.M.1    Parmar, P.K.2    Coates, L.C.3
  • 46
    • 0036733176 scopus 로고    scopus 로고
    • Neuroserpin regulates neurite outgrowth in nerve growth factor-treated PC12 cells
    • Parmar PK, Coates LC, Pearson JF, et al. Neuroserpin regulates neurite outgrowth in nerve growth factor-treated PC12 cells. J Neurochem. 2002;82(6):1406-1415.
    • (2002) J Neurochem. , vol.82 , Issue.6 , pp. 1406-1415
    • Parmar, P.K.1    Coates, L.C.2    Pearson, J.F.3
  • 47
    • 42449095860 scopus 로고    scopus 로고
    • Neuroserpin regulates N-cadherin-mediated cell adhesion independently of its activity as an inhibitor of tissue plasminogen activator
    • Lee TW, Coates LC, Birch NP. Neuroserpin regulates N-cadherin-mediated cell adhesion independently of its activity as an inhibitor of tissue plasminogen activator. J Neurosci Res. 2008; 86(6):1243-1253.
    • (2008) J Neurosci Res. , vol.86 , Issue.6 , pp. 1243-1253
    • Lee, T.W.1    Coates, L.C.2    Birch, N.P.3
  • 48
    • 0038016429 scopus 로고    scopus 로고
    • Impaired explorative behavior and neophobia in genetically modified mice lacking or overexpressing the extracellular serine protease inhibitor neuroserpin
    • Madani R, Kozlov S, Akhmendov A, et al. Impaired explorative behavior and neophobia in genetically modified mice lacking or overexpressing the extracellular serine protease inhibitor neuroserpin. Mol Cell Neurosci. 2003;23(3):473-494.
    • (2003) Mol Cell Neurosci. , vol.23 , Issue.3 , pp. 473-494
    • Madani, R.1    Kozlov, S.2    Akhmendov, A.3
  • 49
    • 0038157213 scopus 로고    scopus 로고
    • Impaired fibrinolysis in multiple sclerosis: A role for tissue plasminogen activator inhibitors
    • Gveric D, Herrera B, Petzold A, et al. Impaired fibrinolysis in multiple sclerosis: a role for tissue plasminogen activator inhibitors. Brain. 2003;126(7):1590-1598.
    • (2003) Brain. , vol.126 , Issue.7 , pp. 1590-1598
    • Gveric, D.1    Herrera, B.2    Petzold, A.3
  • 50
    • 33747860195 scopus 로고    scopus 로고
    • N-cadherin signaling in synapse formation and neuronal physiology
    • Bruses JL. N-cadherin signaling in synapse formation and neuronal physiology. Mol Neurobiol. 2006;33(3):237-252.
    • (2006) Mol Neurobiol. , vol.33 , Issue.3 , pp. 237-252
    • Bruses, J.L.1
  • 51
    • 77955494880 scopus 로고    scopus 로고
    • Neuroserpin regulates the density of dendritic protrusions and dendritic spine shape in cultured hippocampal neurons
    • Borges VM, Lee TW, Christie DL, et al. Neuroserpin regulates the density of dendritic protrusions and dendritic spine shape in cultured hippocampal neurons. J Neurosci Res. 2010;88(12): 2610-2617.
    • (2010) J Neurosci Res. , vol.88 , Issue.12 , pp. 2610-2617
    • Borges, V.M.1    Lee, T.W.2    Christie, D.L.3
  • 52
    • 0033598346 scopus 로고    scopus 로고
    • Familial dementia caused by polymerization of mutant neuroserpin
    • Davis RL, Shrimpton AE, Holohan PD, et al. Familial dementia caused by polymerization of mutant neuroserpin. Nature. 1999; 401(6751):376-379.
    • (1999) Nature. , vol.401 , Issue.6751 , pp. 376-379
    • Davis, R.L.1    Shrimpton, A.E.2    Holohan, P.D.3
  • 53
    • 0037193809 scopus 로고    scopus 로고
    • Association between conformational mutations in neuroserpin and onset and severity of dementia
    • Davis RL, Shrimpton AE, Carrell RW, et al. Association between conformational mutations in neuroserpin and onset and severity of dementia. Lancet. 2002;359(9325):2242-2247.
    • (2002) Lancet. , vol.359 , Issue.9325 , pp. 2242-2247
    • Davis, R.L.1    Shrimpton, A.E.2    Carrell, R.W.3
  • 54
    • 20244381143 scopus 로고    scopus 로고
    • Oxygen glucose deprivation switches the transport of tPA across the blood-brain barrier from an LRP-dependent to an increased LRP-independent process
    • Benchenane K, Berezowski V, Fernandez-Monreal M, et al. Oxygen glucose deprivation switches the transport of tPA across the blood-brain barrier from an LRP-dependent to an increased LRP-independent process. Stroke. 2005;36(5):1065-1070.
    • (2005) Stroke. , vol.36 , Issue.5 , pp. 1065-1070
    • Benchenane, K.1    Berezowski, V.2    Fernandez-Monreal, M.3
  • 55
    • 69249104575 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins
    • Kroeger H, Miranda E, MacLeod I, et al. Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins. J Biol Chem. 2009;284(34):22793-22802.
    • (2009) J Biol Chem. , vol.284 , Issue.34 , pp. 22793-22802
    • Kroeger, H.1    Miranda, E.2    McLeod, I.3
  • 56
    • 39449111277 scopus 로고    scopus 로고
    • Sequestration of mutated 1-antitrypsin into inclusion bodies is a cell-protective mechanism to maintain endoplasmic reticulum function
    • Granell S, Baldini G, Mohammad S, et al. Sequestration of mutated 1-antitrypsin into inclusion bodies is a cell-protective mechanism to maintain endoplasmic reticulum function. Mol Biol Cell. 2008;19(2):572-586.
    • (2008) Mol Biol Cell. , vol.19 , Issue.2 , pp. 572-586
    • Granell, S.1    Baldini, G.2    Mohammad, S.3
  • 57
    • 44349122437 scopus 로고    scopus 로고
    • The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB
    • Miranda E, MacLeod I, Davies MJ, et al. The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB. Hum Mol Genet. 2008;17(11):1527-1539.
    • (2008) Hum Mol Genet. , vol.17 , Issue.11 , pp. 1527-1539
    • Miranda, E.1    McLeod, I.2    Davies, M.J.3
  • 58
    • 33745204166 scopus 로고    scopus 로고
    • A rat model of human FENIB (familial encephalopathy with neuroserpin inclusion bodies)
    • Takano K, Kitao Y, Inagi R, et al. A rat model of human FENIB (familial encephalopathy with neuroserpin inclusion bodies). Biochem Biophys Res Commun. 2006;346(3):1040-1047.
    • (2006) Biochem Biophys Res Commun. , vol.346 , Issue.3 , pp. 1040-1047
    • Takano, K.1    Kitao, Y.2    Inagi, R.3
  • 59
    • 67650526104 scopus 로고    scopus 로고
    • Neuroserpin polymers activate NF-B by a calcium signaling pathway that is independent of the unfolded protein response
    • Davies MJ, Miranda E, Roussel BD, et al. Neuroserpin polymers activate NF-B by a calcium signaling pathway that is independent of the unfolded protein response. J Biol Chem. 2009;284(27): 18202-18209.
    • (2009) J Biol Chem. , vol.284 , Issue.27 , pp. 18202-18209
    • Davies, M.J.1    Miranda, E.2    Roussel, B.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.