메뉴 건너뛰기




Volumn 271, Issue 21, 2004, Pages 4275-4283

Reformable intramolecular cross-linking of the N-terminal domain of heparin cofactor II: Effects on enzyme inhibition

Author keywords

Thrombin; Dermatan sulfate; Heparin; Heparin cofactor II; Serpin(s)

Indexed keywords

CHYMOTRYPSIN A; DERMATAN SULFATE; DISULFIDE; DITHIOTHREITOL; GLYCOSAMINOGLYCAN; HEPARIN COFACTOR II; IODOACETAMIDE; PROTEINASE; SERINE PROTEINASE INHIBITOR; THROMBIN;

EID: 8644259055     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04367.x     Document Type: Article
Times cited : (11)

References (42)
  • 3
    • 0021989130 scopus 로고
    • The protease specificity of heparin cofactor II
    • Parker, K.A. & Tollefsen, D.M. (1985) The protease specificity of heparin cofactor II. J. Biol. Chem. 260, 3501-3505.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3501-3505
    • Parker, K.A.1    Tollefsen, D.M.2
  • 5
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins, P.G.W. (2002) Serpin structure, mechanism, and function. Chem. Rev. 102, 4751-4804.
    • (2002) Chem. Rev. , vol.102 , pp. 4751-4804
    • Gettins, P.G.W.1
  • 6
    • 0033608984 scopus 로고    scopus 로고
    • Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 Å and full insertion of the reactive center loop into beta-sheet A
    • Stratikos, E. & Gettins, P.G.W. (1999) Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 Å and full insertion of the reactive center loop into beta-sheet A. Proc. Natl Acad. Sci. USA 96, 4808-4813.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4808-4813
    • Stratikos, E.1    Gettins, P.G.W.2
  • 7
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-proteinase complex shows inhibition by deformation
    • Huntington, J.A., Read, R.J. & Carrell, R.W. (2000) Structure of a serpin-proteinase complex shows inhibition by deformation. Nature 407, 923-926.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 8
    • 0347695991 scopus 로고    scopus 로고
    • Localization of an antithrombin exosite that promotes rapid inhibition of factors Xa and IXa dependent on heparin activation of the serpin
    • Izaguirre, G., Zhang, W., Swanson, R., Bedsted, T. & Olson, S.T. (2003) Localization of an antithrombin exosite that promotes rapid inhibition of factors Xa and IXa dependent on heparin activation of the serpin. J. Biol. Chem. 278, 51433-51440.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51433-51440
    • Izaguirre, G.1    Zhang, W.2    Swanson, R.3    Bedsted, T.4    Olson, S.T.5
  • 9
    • 0025230672 scopus 로고
    • On the activation of human leuserpin-2, a thrombin inhibitor, by glycosaminoglycans
    • Ragg, H., Ulshöfer, T. & Gerewitz, J. (1990) On the activation of human leuserpin-2, a thrombin inhibitor, by glycosaminoglycans. J. Biol. Chem. 265, 5211-5218.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5211-5218
    • Ragg, H.1    Ulshöfer, T.2    Gerewitz, J.3
  • 10
    • 0025789987 scopus 로고
    • The N-terminal acidic domain of heparin cofactor II mediates the inhibition of α-thrombin in the presence of glycosaminoglycans
    • Van Deerlin, V.M.D. & Tollefsen, D.M. (1991) The N-terminal acidic domain of heparin cofactor II mediates the inhibition of α-thrombin in the presence of glycosaminoglycans. J. Biol. Chem. 266, 20223-20231.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20223-20231
    • Van Deerlin, V.M.D.1    Tollefsen, D.M.2
  • 11
    • 0037205406 scopus 로고    scopus 로고
    • Aspartic acid residues 72 and 75 and tyrosine-sulfate 73 of heparin cofactor II promote intramolecular interactions during glycosaminoglycan binding and thrombin inhibition
    • Mitchell, J.W. & Church, F.C. (2002) Aspartic acid residues 72 and 75 and tyrosine-sulfate 73 of heparin cofactor II promote intramolecular interactions during glycosaminoglycan binding and thrombin inhibition. J. Biol. Chem. 277, 19823-19830.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19823-19830
    • Mitchell, J.W.1    Church, F.C.2
  • 12
    • 0037143655 scopus 로고    scopus 로고
    • Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism
    • Baglin, T.P., Carrell, R.W., Church, F.C., Esmon, C.T. & Huntington, J.A. (2002) Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism. Proc. Natl Acad. Sci. USA 99, 11079-11084.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11079-11084
    • Baglin, T.P.1    Carrell, R.W.2    Church, F.C.3    Esmon, C.T.4    Huntington, J.A.5
  • 13
    • 0022639105 scopus 로고
    • A new member of the plasma protease inhibitor gene family
    • Ragg, H. (1986) A new member of the plasma protease inhibitor gene family. Nucleic Acids Res. 14, 1073-1088.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 1073-1088
    • Ragg, H.1
  • 14
    • 0024297509 scopus 로고
    • Heparin cofactor II: cDNA sequence, chromosome localization, restriction fragment length polymorphism, and expression in Escherichia coli
    • Blinder, M.A., Marasa, J.C., Reynolds, C.H., Deaven, L.L. & Tollefsen, D.M. (1988) Heparin cofactor II: cDNA sequence, chromosome localization, restriction fragment length polymorphism, and expression in Escherichia coli. Biochemistry 27, 752-759.
    • (1988) Biochemistry , vol.27 , pp. 752-759
    • Blinder, M.A.1    Marasa, J.C.2    Reynolds, C.H.3    Deaven, L.L.4    Tollefsen, D.M.5
  • 15
    • 0021081920 scopus 로고
    • Heparin-catalyzed inhibitor/protease reactions: Kinetic evidence for a common mechanism of action of heparin
    • Griffith, M.J. (1983) Heparin-catalyzed inhibitor/protease reactions: kinetic evidence for a common mechanism of action of heparin. Proc. Natl Acad. Sci. USA 80, 5460-5464.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 5460-5464
    • Griffith, M.J.1
  • 16
    • 1642276048 scopus 로고    scopus 로고
    • The preferred pathway of glycosaminoglycan-accelerated inactivation of thrombin by heparin cofactor II
    • Verhamme, I.M., Bock, P.E. & Jackson, C.M. (2004) The preferred pathway of glycosaminoglycan-accelerated inactivation of thrombin by heparin cofactor II. J. Biol. Chem. 279, 9785-9795.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9785-9795
    • Verhamme, I.M.1    Bock, P.E.2    Jackson, C.M.3
  • 17
    • 0033600756 scopus 로고    scopus 로고
    • Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II
    • Liaw, P.C., Austin, R.C., Fredenburgh, J.C., Stafford, A.R. & Weitz, J.I. (1999) Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II. J. Biol. Chem. 274, 27597-27604.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27597-27604
    • Liaw, P.C.1    Austin, R.C.2    Fredenburgh, J.C.3    Stafford, A.R.4    Weitz, J.I.5
  • 18
    • 0032553446 scopus 로고    scopus 로고
    • Role of thrombin anion-binding exosite-I in the formation of thrombin-serpin complexes
    • Myles, T., Church, F.C., Whinna, H.C., Monard, D. & Stone, S.R. (1998) Role of thrombin anion-binding exosite-I in the formation of thrombin-serpin complexes. J. Biol. Chem. 273, 31203-31208.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31203-31208
    • Myles, T.1    Church, F.C.2    Whinna, H.C.3    Monard, D.4    Stone, S.R.5
  • 19
    • 0028303486 scopus 로고
    • A rapid and efficient one-tube PCR-based mutagenesis technique using Pfu DNA polymerase
    • Picard, V., Ersdal-Badju, E., Lu, A. & Bock, S. (1994) A rapid and efficient one-tube PCR-based mutagenesis technique using Pfu DNA polymerase. Nucleic Acids Res. 22, 2587-2591.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 2587-2591
    • Picard, V.1    Ersdal-Badju, E.2    Lu, A.3    Bock, S.4
  • 20
    • 0031013799 scopus 로고    scopus 로고
    • Simultaneous introduction of multiple mutations using overlap extension PCR
    • Ge, L. & Rudolph, P. (1997) Simultaneous introduction of multiple mutations using overlap extension PCR. Biotechniques 22, 28-30.
    • (1997) Biotechniques , vol.22 , pp. 28-30
    • Ge, L.1    Rudolph, P.2
  • 21
    • 0036183726 scopus 로고    scopus 로고
    • Tyrosine sulfation and N-glycosylation of human heparin cofactor II from plasma and recombinant Chinese hamster ovary cells and their effects on heparin binding
    • Böhme, C., Nimtz, M., Grabenhorst, E., Conradt, H.S., Strathmann, A. & Ragg, H. (2002) Tyrosine sulfation and N-glycosylation of human heparin cofactor II from plasma and recombinant Chinese hamster ovary cells and their effects on heparin binding. Eur. J. Biochem. 269, 977-988.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 977-988
    • Böhme, C.1    Nimtz, M.2    Grabenhorst, E.3    Conradt, H.S.4    Strathmann, A.5    Ragg, H.6
  • 22
    • 0020445435 scopus 로고
    • A one-step purification of membrane proteins using a high efficiency immunomatrix
    • Schneider, C., Newman, R.A., Sutherland, D.R., Asser, U. & Greaves, M.F. (1982) A one-step purification of membrane proteins using a high efficiency immunomatrix. J. Biol. Chem. 257, 10766-10769.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10766-10769
    • Schneider, C.1    Newman, R.A.2    Sutherland, D.R.3    Asser, U.4    Greaves, M.F.5
  • 23
    • 0026410275 scopus 로고
    • Analysis and isolation of human transferrin receptor using the OKT-9 monoclonal antibody covalently crosslinked to magnetic beads
    • Karlsson, G.B. & Platt, F.M. (1991) Analysis and isolation of human transferrin receptor using the OKT-9 monoclonal antibody covalently crosslinked to magnetic beads. Anal. Biochem. 199, 219-222.
    • (1991) Anal. Biochem. , vol.199 , pp. 219-222
    • Karlsson, G.B.1    Platt, F.M.2
  • 24
    • 0037112617 scopus 로고    scopus 로고
    • Renaturation of human proinsulin - A study on refolding and conversion to insulin
    • Winter, J., Lilie, H. & Rudolph, R. (2002) Renaturation of human proinsulin - a study on refolding and conversion to insulin. Anal. Biochem. 310, 148-155.
    • (2002) Anal. Biochem. , vol.310 , pp. 148-155
    • Winter, J.1    Lilie, H.2    Rudolph, R.3
  • 25
    • 0033522912 scopus 로고    scopus 로고
    • Use of a disulfide cross-linking strategy to study muscarinic receptor structure and mechanisms of activation
    • Zeng, F.Y., Hopp, A., Soldner, A. & Wess, J. (1999) Use of a disulfide cross-linking strategy to study muscarinic receptor structure and mechanisms of activation. J. Biol. Chem. 274, 16629-16640.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16629-16640
    • Zeng, F.Y.1    Hopp, A.2    Soldner, A.3    Wess, J.4
  • 26
    • 8644286424 scopus 로고
    • Cyanogen bromide cleavage
    • (Kellner, R., Lottspeich, F. & Meyer, H.E., eds). VCH-Verlagsgesellschaft, Weinheim, Germany
    • Kellner, R. (1994) Cyanogen bromide cleavage. In Microcharacterization of Proteins (Kellner, R., Lottspeich, F. & Meyer, H.E., eds), pp. 19-22. VCH-Verlagsgesellschaft, Weinheim, Germany.
    • (1994) Microcharacterization of Proteins , pp. 19-22
    • Kellner, R.1
  • 27
    • 0029026723 scopus 로고
    • Active-site titration of peptidases
    • Knight, C.G. (1995) Active-site titration of peptidases. Methods Enzymol. 248, 85-101.
    • (1995) Methods Enzymol. , vol.248 , pp. 85-101
    • Knight, C.G.1
  • 28
    • 0031031144 scopus 로고    scopus 로고
    • Heparin promotes proteolytic inactivation by thrombin of a reactive site mutant (L444R) of recombinant heparin cofactor II
    • Ciaccia, A.V., Willemze, A.J. & Church, F.C. (1997) Heparin promotes proteolytic inactivation by thrombin of a reactive site mutant (L444R) of recombinant heparin cofactor II. J. Biol. Chem. 272, 888-893.
    • (1997) J. Biol. Chem. , vol.272 , pp. 888-893
    • Ciaccia, A.V.1    Willemze, A.J.2    Church, F.C.3
  • 29
    • 0031064380 scopus 로고    scopus 로고
    • Probing protein folding and stability using disulfide bonds
    • Darby, N. & Creighton, T.E. (1997) Probing protein folding and stability using disulfide bonds. Mol. Biotechnol. 7, 57-77.
    • (1997) Mol. Biotechnol. , vol.7 , pp. 57-77
    • Darby, N.1    Creighton, T.E.2
  • 30
    • 0020617887 scopus 로고
    • Activation of heparin cofactor II by dermatan sulfate
    • Tollefsen, D.M., Pestka, C.A. & Monafo, W.J. (1983) Activation of heparin cofactor II by dermatan sulfate. J. Biol. Chem. 258, 6713-6716.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6713-6716
    • Tollefsen, D.M.1    Pestka, C.A.2    Monafo, W.J.3
  • 31
    • 0023607206 scopus 로고
    • Structure-function relationships in heparin cofactor II: Spectral analysis of aromatic residues and absence of a role for sulfhydryl groups in thrombin inhibition
    • Church, F.C., Meade, J.B. & Pratt, C.W. (1987) Structure-function relationships in heparin cofactor II: spectral analysis of aromatic residues and absence of a role for sulfhydryl groups in thrombin inhibition. Arch. Biochem. Biophys. 259, 331-340.
    • (1987) Arch. Biochem. Biophys. , vol.259 , pp. 331-340
    • Church, F.C.1    Meade, J.B.2    Pratt, C.W.3
  • 32
    • 0026319603 scopus 로고
    • Stabilization of functional proteins by introduction of multiple disulfide bonds
    • Matsumura, M. & Matthews, B.W. (1991) Stabilization of functional proteins by introduction of multiple disulfide bonds. Methods Enzymol. 202, 336-356.
    • (1991) Methods Enzymol. , vol.202 , pp. 336-356
    • Matsumura, M.1    Matthews, B.W.2
  • 33
    • 0029665077 scopus 로고    scopus 로고
    • 2+-induced conformational transitions in calmodulin with disulfide bonds
    • 2+-induced conformational transitions in calmodulin with disulfide bonds. J. Biol. Chem. 271, 7479-7483.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7479-7483
    • Tan, R.Y.1    Mabuchi, Y.2    Grabarek, Z.3
  • 34
    • 0032167422 scopus 로고    scopus 로고
    • Conformational changes necessary for gene regulation by Tet repressor assayed by reversible disulfide bond formation
    • Tiebel, B., Aung-Hilbrich, L.M., Schnappinger, D. & Hillen, W. (1998) Conformational changes necessary for gene regulation by Tet repressor assayed by reversible disulfide bond formation. EMBO J. 17, 5112-5119.
    • (1998) EMBO J. , vol.17 , pp. 5112-5119
    • Tiebel, B.1    Aung-Hilbrich, L.M.2    Schnappinger, D.3    Hillen, W.4
  • 35
    • 0035932996 scopus 로고    scopus 로고
    • Reversibly locking a protein fold in an active conformation with a disulfide bond: Integrin alphaL I domains with high affinity and antagonist activity in vivo
    • Shimaoka, M., Lu, C., Palframan, R.T., von Andrian, U.H., McCormack, A., Takagi, J. & Springer, T.A. (2001) Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin alphaL I domains with high affinity and antagonist activity in vivo. Proc. Natl Acad. Sci. USA 98, 6009-6014.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6009-6014
    • Shimaoka, M.1    Lu, C.2    Palframan, R.T.3    Von Andrian, U.H.4    McCormack, A.5    Takagi, J.6    Springer, T.A.7
  • 36
    • 0038606342 scopus 로고    scopus 로고
    • Immobilization of the distal hinge in the labile serpin plasminogen activator inhibitor 1: Identification of a transition state with distinct conformational and functional properties
    • De Taeye, B., Compernolle, G., Dewilde, M., Biesemans, W. & Declerck, P.J. (2003) Immobilization of the distal hinge in the labile serpin plasminogen activator inhibitor 1: identification of a transition state with distinct conformational and functional properties. J. Biol. Chem. 278, 23899-23905.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23899-23905
    • De Taeye, B.1    Compernolle, G.2    Dewilde, M.3    Biesemans, W.4    Declerck, P.J.5
  • 37
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P.E. & Dyson, H.J. (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293, 321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 38
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky, V.N. (2002) What does it mean to be natively unfolded? Eur. J. Biochem. 269, 2-12.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 39
    • 0022998259 scopus 로고
    • Identification of two sites of sulfation of human heparin cofactor II
    • Hortin, G., Tollefsen, D.M. & Strauss, A.W. (1986) Identification of two sites of sulfation of human heparin cofactor II. J. Biol. Chem. 261, 15827-15830.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15827-15830
    • Hortin, G.1    Tollefsen, D.M.2    Strauss, A.W.3
  • 40
    • 0025641213 scopus 로고
    • Glycosaminoglycan-mediated leuserpin-2/thrombin interaction: Structure-function relationships
    • Ragg, H., Ulshöfer, T. & Gerewitz, J. (1990) Glycosaminoglycan-mediated leuserpin-2/thrombin interaction: structure-function relationships. J. Biol. Chem. 265, 22386-22391.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22386-22391
    • Ragg, H.1    Ulshöfer, T.2    Gerewitz, J.3
  • 41
    • 0037464489 scopus 로고    scopus 로고
    • Zinc ions promote the interaction between heparin and heparin cofactor II
    • Eckert, R. & Ragg, H. (2003) Zinc ions promote the interaction between heparin and heparin cofactor II. FEBS Lett. 541, 121-125.
    • (2003) FEBS Lett. , vol.541 , pp. 121-125
    • Eckert, R.1    Ragg, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.