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Volumn 91, Issue 3, 2004, Pages 465-472

Both lysine-clusters of the NH2-terminal prion-protein fragment PrP23-110 are essential for t-PA mediated plasminogen activation

Author keywords

Heparins glycosaminoglycans; Plasminogen activators; Protein function activity; Proteolysis pericellular

Indexed keywords

ALANINE; GLYCOSAMINOGLYCAN; HEPARIN; LYSINE; MUTANT PROTEIN; PLASMINOGEN; PRION PROTEIN; TISSUE PLASMINOGEN ACTIVATOR; PLASMIN; PLASMINOGEN ACTIVATOR; RECOMBINANT PROTEIN;

EID: 1642299772     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/th03-06-0382     Document Type: Article
Times cited : (19)

References (27)
  • 1
    • 0037018914 scopus 로고    scopus 로고
    • Plasminogen activation is stimulated by prion protein and regulated in a copper-dependent manner
    • Ellis V, Daniels M, Misra R, et al.. Plasminogen activation is stimulated by prion protein and regulated in a copper-dependent manner. Biochemistry 2002; 41(22): 6891-6.
    • (2002) Biochemistry , vol.41 , Issue.22 , pp. 6891-6896
    • Ellis, V.1    Daniels, M.2    Misra, R.3
  • 2
    • 12444344294 scopus 로고    scopus 로고
    • Stimulation of plasminogen activation by recombinant cellular prion protein is conserved in the NH(2)-terminal fragment PrP23-110
    • Praus M, Kettelgerdes G, Baier M, et al.. Stimulation of plasminogen activation by recombinant cellular prion protein is conserved in the NH(2)-terminal fragment PrP23-110. Thromb Haemost 2003; 89(5): 812-9.
    • (2003) Thromb. Haemost. , vol.89 , Issue.5 , pp. 812-919
    • Praus, M.1    Kettelgerdes, G.2    Baier, M.3
  • 3
    • 0029027854 scopus 로고
    • Truncated Forms of the Human Prion Protein in Normal Brain and in Prion Diseases
    • Chen SG, Teplow DB, Parchi P, et al.. Truncated Forms of the Human Prion Protein in Normal Brain and in Prion Diseases. J Biol Chem 1995; 270(32): 19173-80.
    • (1995) J. Biol. Chem. , vol.270 , Issue.32 , pp. 19173-19180
    • Chen, S.G.1    Teplow, D.B.2    Parchi, P.3
  • 4
    • 0035851151 scopus 로고    scopus 로고
    • The Disintegrins ADAM10 and TACE Contribute to the Constitutive and Phorbol Ester-regulated Normal Cleavage of the Cellular Prion Protein
    • Vincent B, Paitel E, Saftig P, et al.. The Disintegrins ADAM10 and TACE Contribute to the Constitutive and Phorbol Ester-regulated Normal Cleavage of the Cellular Prion Protein. J Biol Chem 2001; 276(41): 37743-6.
    • (2001) J. Biol. Chem. , vol.276 , Issue.41 , pp. 37743-37746
    • Vincent, B.1    Paitel, E.2    Saftig, P.3
  • 5
    • 0033151831 scopus 로고    scopus 로고
    • Enhanced hippocampal long-term potentiation and learning by increased neuronal expression of tissue-type plasminogen activator in transgenic: Mice
    • Madani R, Hulo S, Toni N, et al.. Enhanced hippocampal long-term potentiation and learning by increased neuronal expression of tissue-type plasminogen activator in transgenic: Mice. Embo J 1999; 18(11): 3007-12.
    • (1999) Embo J. , vol.18 , Issue.11 , pp. 3007-3012
    • Madani, R.1    Hulo, S.2    Toni, N.3
  • 6
    • 0029945837 scopus 로고    scopus 로고
    • Modulated expression of plasminogen activator system components in cultured cells from dissociated mouse dorsal root ganglia
    • Hayden SM, Seeds NW. Modulated expression of plasminogen activator system components in cultured cells from dissociated mouse dorsal root ganglia. J Neurosci 1996; 16(7): 2307-17.
    • (1996) J. Neurosci. , vol.16 , Issue.7 , pp. 2307-2317
    • Hayden, S.M.1    Seeds, N.W.2
  • 7
    • 0031470554 scopus 로고    scopus 로고
    • Neuronal death in the hippocampus is promoted by plasmin-catalyzed degradation of laminin
    • Chen ZL, Strickland S. Neuronal death in the hippocampus is promoted by plasmin-catalyzed degradation of laminin. Cell 1997; 91(7): 917-25.
    • (1997) Cell , vol.91 , Issue.7 , pp. 917-925
    • Chen, Z.L.1    Strickland, S.2
  • 8
    • 0029556177 scopus 로고
    • Tissue plasminogen activator induction in Purkinje neurons after cerebellar motor learning
    • Seeds NW, Williams BL, Bickford PC. Tissue plasminogen activator induction in Purkinje neurons after cerebellar motor learning. Science 1995; 270(5244): 1992-4.
    • (1995) Science , vol.270 , Issue.5244 , pp. 1992-1994
    • Seeds, N.W.1    Williams, B.L.2    Bickford, P.C.3
  • 9
    • 0032057384 scopus 로고    scopus 로고
    • Tissue plasminogen activator mediates reverse occlusion plasticity in visual cortex
    • Muller CM, Griesinger CB. Tissue plasminogen activator mediates reverse occlusion plasticity in visual cortex. Nat Neurosci 1998; 1(1): 47-53.
    • (1998) Nat. Neurosci. , vol.1 , Issue.1 , pp. 47-53
    • Muller, C.M.1    Griesinger, C.B.2
  • 10
    • 0017847923 scopus 로고
    • Molecular mechanism of physiological fibrinolysis
    • Wiman B, Collen D. Molecular mechanism of physiological fibrinolysis. Nature 1978; 272(5653): 549-50.
    • (1978) Nature , vol.272 , Issue.5653 , pp. 549-550
    • Wiman, B.1    Collen, D.2
  • 11
    • 0028791659 scopus 로고
    • Structural features mediating fibrin selectivity of vampire bat plasminogen activators
    • Bringmann P, Gruber D, Liese A, et al.. Structural features mediating fibrin selectivity of vampire bat plasminogen activators. J Biol Chem 1995; 270(43): 25596-603.
    • (1995) J. Biol. Chem. , vol.270 , Issue.43 , pp. 25596-25603
    • Bringmann, P.1    Gruber, D.2    Liese, A.3
  • 12
    • 0022974681 scopus 로고
    • On the interaction of the finger and the kringle-2 domain of fissue-type plasminogen activator with fibrin. Inhibition of kringle-2 binding to fibrin by epsilon-amino caproic acid
    • van Zonneveld AJ, Veerman H, Pannekoek H. On the interaction of the finger and the kringle-2 domain of fissue-type plasminogen activator with fibrin. Inhibition of kringle-2 binding to fibrin by epsilon-amino caproic acid. J Biol Chem 1986; 261(30): 14214-8.
    • (1986) J. Biol. Chem. , vol.261 , Issue.30 , pp. 14214-14218
    • van Zonneveld, A.J.1    Veerman, H.2    Pannekoek, H.3
  • 13
    • 0021804064 scopus 로고
    • Quantitative characterization of the binding of plasminogen to intact fibrin clots, lysine-sepharose, and fibrin cleaved by plasmin
    • Bok RA, Mangel WF. Quantitative characterization of the binding of plasminogen to intact fibrin clots, lysine-sepharose, and fibrin cleaved by plasmin. Biochemistry 1985; 24(13): 3279-86.
    • (1985) Biochemistry , vol.24 , Issue.13 , pp. 3279-3286
    • Bok, R.A.1    Mangel, W.F.2
  • 14
    • 0038399786 scopus 로고    scopus 로고
    • Cooperative binding of dominant-negative prion protein to kringle domains
    • Ryon C, Prusiner SB, Legname G. Cooperative binding of dominant-negative prion protein to kringle domains. J Mol Biol 2003; 329(2): 323-33.
    • (2003) J. Mol. Biol. , vol.329 , Issue.2 , pp. 323-333
    • Ryon, C.1    Prusiner, S.B.2    Legname, G.3
  • 15
    • 0037166240 scopus 로고    scopus 로고
    • Identification of the heparan sulfate binding sites in the cellular prion protein
    • Warner RG, Hundt C, Weiss S, et al.. Identification of the heparan sulfate binding sites in the cellular prion protein. J Biol Chem 2002; 277(21): 18421-30.
    • (2002) J. Biol. Chem. , vol.277 , Issue.21 , pp. 18421-18430
    • Warner, R.G.1    Hundt, C.2    Weiss, S.3
  • 16
    • 0344613422 scopus 로고    scopus 로고
    • Cellular heparan sulfate participates in the metabolism of prions
    • Kovalchuk O, Tzaban S, Tal Y, et al.. Cellular heparan sulfate participates in the metabolism of prions. J Biol Chem 2003;18: 18.
    • (2003) J. Biol. Chem. , vol.18 , pp. 18
    • Kovalchuk, O.1    Tzaban, S.2    Tal, Y.3
  • 17
    • 0141994735 scopus 로고    scopus 로고
    • Cellular heparan sulfate participates in the metabolism of prions
    • Ben-Zaken O, Tzaban S, Tal Y, et al.. Cellular heparan sulfate participates in the metabolism of prions. J Biol Chem 2003;278(41):40041-9.
    • (2003) J. Biol. Chem. , vol.278 , Issue.41 , pp. 40041-40049
    • Ben-Zaken, O.1    Tzaban, S.2    Tal, Y.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227(259): 680-5.
    • (1970) Nature , vol.227 , Issue.259 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger H, von Jagow G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal Biochem 1991; 199(2): 223-31.
    • (1991) Anal. Biochem. , vol.199 , Issue.2 , pp. 223-231
    • Schagger, H.1    von Jagow, G.2
  • 20
    • 0033567955 scopus 로고    scopus 로고
    • Characterization and polyanion-binding properties of purified recombinant prion protein
    • Brimacombe DB, Bennett AD, Wusteman FS, et al.. Characterization and polyanion-binding properties of purified recombinant prion protein. Biochem J 1999; 342(Pt 3): 605-13.
    • (1999) Biochem. J. , vol.342 , Issue.PART 3 , pp. 605-613
    • Brimacombe, D.B.1    Bennett, A.D.2    Wusteman, F.S.3
  • 21
    • 0024433514 scopus 로고
    • Anticoagulant low molecular weight heparin does not enhance the activation of plasminogen by tissue plasminogen activator
    • Andrade-Gordon P, Strickland S. Anticoagulant low molecular weight heparin does not enhance the activation of plasminogen by tissue plasminogen activator. J Biol Chem 1989; 264(26): 15177-81.
    • (1989) J. Biol. Chem. , vol.264 , Issue.26 , pp. 15177-15181
    • Andrade-Gordon, P.1    Strickland, S.2
  • 22
    • 0037340432 scopus 로고    scopus 로고
    • Molecular mechanisms of initiation of fibrinolysis by fibrin
    • Medved L, Nieuwenhuizen W. Molecular mechanisms of initiation of fibrinolysis by fibrin. Thromb Haemost 2003; 89(3): 409-19.
    • (2003) Thromb. Haemost. , vol.89 , Issue.3 , pp. 409-419
    • Medved, L.1    Nieuwenhuizen, W.2
  • 23
    • 0034707048 scopus 로고    scopus 로고
    • Binding of disease-associated prion protein to plasminogen
    • Fischer MB, Roeckl C, Parizek P, et al.. Binding of disease-associated prion protein to plasminogen. Nature 2000; 408(6811): 479-83.
    • (2000) Nature , vol.408 , Issue.6811 , pp. 479-483
    • Fischer, M.B.1    Roeckl, C.2    Parizek, P.3
  • 24
    • 0020056939 scopus 로고
    • An enhancing effect of poly-lysine on the activation of plasminogen
    • Allen RA. An enhancing effect of poly-lysine on the activation of plasminogen. Thromb Haemost 1982; 47(1): 41-5.
    • (1982) Thromb. Haemost. , vol.47 , Issue.1 , pp. 41-45
    • Allen, R.A.1
  • 25
    • 0242662244 scopus 로고    scopus 로고
    • The Octapeptide Repeats in Mammalian Prion Protein Constitute a pH-dependent Folding and Aggregation Site
    • Zahn R. The Octapeptide Repeats in Mammalian Prion Protein Constitute a pH-dependent Folding and Aggregation Site. J Mol Biol 2003; 334(3): 477-88.
    • (2003) J. Mol. Biol. , vol.334 , Issue.3 , pp. 477-488
    • Zahn, R.1
  • 26
    • 0027535855 scopus 로고
    • Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells
    • Caughey B, Raymond GJ. Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells. J Virol 1993; 67(2): 643-50.
    • (1993) J. Virol. , vol.67 , Issue.2 , pp. 643-650
    • Caughey, B.1    Raymond, G.J.2
  • 27
    • 10744231357 scopus 로고    scopus 로고
    • Small improvement seen in teenager with vCJD
    • Mayor S. Small improvement seen in teenager with vCJD. BMJ 2003; 327(7418): 765.
    • (2003) BMJ , vol.327 , Issue.7418 , pp. 765
    • Mayor, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.