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Volumn 162, Issue 12, 1999, Pages 7426-7433

Alterations in C3 activation and binding caused by phosphorylation by a casein kinase released from activated human platelets

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATED PROTEIN C; CASEIN KINASE; CLASSICAL COMPLEMENT PATHWAY C3 C5 CONVERTASE; COMPLEMENT COMPONENT C3; VITRONECTIN;

EID: 0033564687     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (32)

References (41)
  • 1
    • 0000815852 scopus 로고
    • Amino-acid sequence and the occurrence of phosphorus in human fibrinopeptides
    • Blombäck, B., M. Blombäck, P. Edman, and B. Hessel. 1962. Amino-acid sequence and the occurrence of phosphorus in human fibrinopeptides. Nature 193:883.
    • (1962) Nature , vol.193 , pp. 883
    • Blombäck, B.1    Blombäck, M.2    Edman, P.3    Hessel, B.4
  • 2
    • 0028344095 scopus 로고
    • Platelet coagulation factor Va: The major secretory platelet phosphoprotein
    • Rand, M. D., M. Kalafatis, and K. G. Mann. 1994. Platelet coagulation factor Va: the major secretory platelet phosphoprotein. Blood 83:2180.
    • (1994) Blood , vol.83 , pp. 2180
    • Rand, M.D.1    Kalafatis, M.2    Mann, K.G.3
  • 3
    • 0026052579 scopus 로고
    • Cyclic AMP-dependent protein kinase phosphorylates serine 378 in vitronectin
    • Mehringer, J. H., C. J. Weigel, and D. M. Tollefsen. 1991. Cyclic AMP-dependent protein kinase phosphorylates serine 378 in vitronectin. Biochem. Biophys. Res. Commun. 179:655.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 655
    • Mehringer, J.H.1    Weigel, C.J.2    Tollefsen, D.M.3
  • 4
    • 0024348663 scopus 로고
    • Phosphorylation of complement factor C3 in vivo
    • Martin, S. C. 1989. Phosphorylation of complement factor C3 in vivo. Biochem. J. 261:1051.
    • (1989) Biochem. J. , vol.261 , pp. 1051
    • Martin, S.C.1
  • 5
    • 0030721601 scopus 로고    scopus 로고
    • Phosphorylation of complement component C3 after synthesis in U937 cells by a putative CK2, which is regulated by CD11b: Evidence that membrane-bound proteases preferentially cleave phosphorylated C3
    • Nilsson Ekdahl, K., and B. Nilsson. 1997. Phosphorylation of complement component C3 after synthesis in U937 cells by a putative CK2, which is regulated by CD11b: evidence that membrane-bound proteases preferentially cleave phosphorylated C3. Biochem. J. 328:625.
    • (1997) Biochem. J. , vol.328 , pp. 625
    • Nilsson Ekdahl, K.1    Nilsson, B.2
  • 6
    • 0022257328 scopus 로고
    • Phosphorylation in vitro of fibrinogen from three mammalian species with four different protein kinases
    • Humble, E., P. Heldin, P. O. Forsberg, and L. Engström. 1985. Phosphorylation in vitro of fibrinogen from three mammalian species with four different protein kinases. Arch. Biochem. Biophys. 241:225.
    • (1985) Arch. Biochem. Biophys. , vol.241 , pp. 225
    • Humble, E.1    Heldin, P.2    Forsberg, P.O.3    Engström, L.4
  • 7
    • 0024489992 scopus 로고
    • Dephosphorylation of human fibrinogen, previously phosphorylated in vitro by protein kinase C, by whole blood or intestinal alkaline phosphatase
    • Forsberg, P. O. 1989. Dephosphorylation of human fibrinogen, previously phosphorylated in vitro by protein kinase C, by whole blood or intestinal alkaline phosphatase. Thromb. Res. 53:1.
    • (1989) Thromb. Res. , vol.53 , pp. 1
    • Forsberg, P.O.1
  • 8
    • 0025760729 scopus 로고
    • The effects of in vitro phosphorylation and dephosphorylation on the thrombin-induced gelation and plasmin degradation of fibrinogen
    • Martin, S. C., P. O. Forsberg, and S. D. Eriksson. 1991. The effects of in vitro Phosphorylation and dephosphorylation on the thrombin-induced gelation and plasmin degradation of fibrinogen. Thromb. Res. 61:243.
    • (1991) Thromb. Res. , vol.61 , pp. 243
    • Martin, S.C.1    Forsberg, P.O.2    Eriksson, S.D.3
  • 9
    • 0027452658 scopus 로고
    • Phosphorylation of factor Va and factor VIIla by activated platelets
    • Kalafatis, M., M. D. Rand, R. J. Jenny, Y. H. Ehrlich, and K. G. Mann. 1993. Phosphorylation of factor Va and factor VIIla by activated platelets. Blood 81:704.
    • (1993) Blood , vol.81 , pp. 704
    • Kalafatis, M.1    Rand, M.D.2    Jenny, R.J.3    Ehrlich, Y.H.4    Mann, K.G.5
  • 10
    • 0031038474 scopus 로고    scopus 로고
    • 362 by protein kinase C attenuates its cleavage by plasmin
    • 362 by protein kinase C attenuates its cleavage by plasmin. Eur. J. Biochem. 243:493.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 493
    • Gechtman, Z.1    Shaltiel, S.2
  • 11
    • 0025329565 scopus 로고
    • In vitro phosphorylation of human complement factor C3 by protein kinase A and protein kinase C
    • Forsberg, P. O., S. C. Martin, B. Nilsson, P. Ekman, U. R. Nilsson, and L. Engström. 1990. In vitro phosphorylation of human complement factor C3 by protein kinase A and protein kinase C. J. Biol. Chem. 265:2941.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2941
    • Forsberg, P.O.1    Martin, S.C.2    Nilsson, B.3    Ekman, P.4    Nilsson, U.R.5    Engström, L.6
  • 12
    • 0025987531 scopus 로고
    • Leishmanial protein kinases phosphorylate components of the complement system
    • Hermoso, T., Z. Fishelson, S. I. Becker, K. Hirschberg, and C. L. Jaffe. 1991. Leishmanial protein kinases phosphorylate components of the complement system. EMBO J. 10:4061.
    • (1991) EMBO J. , vol.10 , pp. 4061
    • Hermoso, T.1    Fishelson, Z.2    Becker, S.I.3    Hirschberg, K.4    Jaffe, C.L.5
  • 13
    • 0029065297 scopus 로고
    • Phosphorylation of complement component C3 and C3 fragments by a human platelet protein kinase: Inhibition of factor I mediated cleavage of C3b
    • Nilsson Ekdahl, K., and B. Nilsson. 1995. Phosphorylation of complement component C3 and C3 fragments by a human platelet protein kinase: inhibition of factor I mediated cleavage of C3b. J. Immunol. 154:6502.
    • (1995) J. Immunol. , vol.154 , pp. 6502
    • Nilsson Ekdahl, K.1    Nilsson, B.2
  • 14
    • 0031445543 scopus 로고    scopus 로고
    • Increased phosphate content in complement component C3, fibrinogen, vitronectin, and other plasma proteins in systemic lupus erythematosus: Covariations with platelet activation and possible association with thrombosis
    • Nilsson Ekdahl, K., L. Rönnblom, G. Sturfeldt, and B. Nilsson. 1997. Increased phosphate content in complement component C3, fibrinogen, vitronectin, and other plasma proteins in systemic lupus erythematosus: covariations with platelet activation and possible association with thrombosis. Arthritis Rheum. 40:2178.
    • (1997) Arthritis Rheum. , vol.40 , pp. 2178
    • Nilsson Ekdahl, K.1    Rönnblom, L.2    Sturfeldt, G.3    Nilsson, B.4
  • 15
    • 0029924746 scopus 로고    scopus 로고
    • Tubing loops as a model for cardiopulmonary bypass circuits: Both the biomaterial and the blood-gas interfaces induce complement activation in an in vitro model
    • Gong, J., R. Larsson, K. Nilsson Ekdahl, T. E. Mollnes, U. R. Nilsson, and B. Nilsson. 1996. Tubing loops as a model for cardiopulmonary bypass circuits: both the biomaterial and the blood-gas interfaces induce complement activation in an in vitro model. J. Clin. Immunol. 16:223.
    • (1996) J. Clin. Immunol. , vol.16 , pp. 223
    • Gong, J.1    Larsson, R.2    Nilsson Ekdahl, K.3    Mollnes, T.E.4    Nilsson, U.R.5    Nilsson, B.6
  • 16
    • 0019862044 scopus 로고
    • Large scale isolation of functionally active components of the human complement system
    • Hammer, C. H., G. H. Wirtz, L. Renfer, H. D. Gresham, and B. F. Tack. 1981. Large scale isolation of functionally active components of the human complement system. J. Biol. Chem. 256:3995.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3995
    • Hammer, C.H.1    Wirtz, G.H.2    Renfer, L.3    Gresham, H.D.4    Tack, B.F.5
  • 17
    • 0021745965 scopus 로고
    • Isolation and characterization of a 33,000-Dalton fragment of complement factor B with catalytic and C3b binding activity
    • Lambris, J. D., and H. J. Müller-Eberhard. 1984. Isolation and characterization of a 33,000-Dalton fragment of complement factor B with catalytic and C3b binding activity. J. Biol. Chem. 259:12685.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12685
    • Lambris, J.D.1    Müller-Eberhard, H.J.2
  • 18
    • 0025765610 scopus 로고
    • Purification of human complement factor D from the peritoneal fluid of patients on chronic ambulatory peritoneal dialysis
    • Catana, E., and J. A. Schifferli. 1991. Purification of human complement factor D from the peritoneal fluid of patients on chronic ambulatory peritoneal dialysis. J. Immunol. Methods 138:265.
    • (1991) J. Immunol. Methods , vol.138 , pp. 265
    • Catana, E.1    Schifferli, J.A.2
  • 19
    • 0019922677 scopus 로고
    • Generation of three different fragments of bound C3 with purified factor I or serum
    • Ross, G. D., J. D. Lambris, J. A. Cain, and S. L. Newman. 1982. Generation of three different fragments of bound C3 with purified factor I or serum. J. Immunol. 129:2051.
    • (1982) J. Immunol. , vol.129 , pp. 2051
    • Ross, G.D.1    Lambris, J.D.2    Cain, J.A.3    Newman, S.L.4
  • 20
    • 0028897483 scopus 로고
    • Shedding of tyrosine and serine/threonine ectoprotein kinases from human leukemic cells
    • Paas, Y., and Z. Fishelson. 1995. Shedding of tyrosine and serine/threonine ectoprotein kinases from human leukemic cells. Arch. Biochem. Biophys. 316:780.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 780
    • Paas, Y.1    Fishelson, Z.2
  • 21
    • 0026670131 scopus 로고
    • Purification and characterization of porcine C3: Studies of the biologically active protein and its split products
    • Storm, K. E., G. Artursson, and U. R. Nilsson. 1992. Purification and characterization of porcine C3: studies of the biologically active protein and its split products. Vet. Immunol. Immunopathol. 34:47.
    • (1992) Vet. Immunol. Immunopathol. , vol.34 , pp. 47
    • Storm, K.E.1    Artursson, G.2    Nilsson, U.R.3
  • 23
    • 0025728718 scopus 로고
    • Phosphorylation and dephosphorylation of human platelet surface proteins by an ecto-protein kinase/phosphatase system
    • Naik, U. P., E. Kornecki, and Y. H. Ehrlich. 1991. Phosphorylation and dephosphorylation of human platelet surface proteins by an ecto-protein kinase/phosphatase system. Biochim. Biophys. Acta 1092:256.
    • (1991) Biochim. Biophys. Acta , vol.1092 , pp. 256
    • Naik, U.P.1    Kornecki, E.2    Ehrlich, Y.H.3
  • 24
    • 0024515028 scopus 로고
    • A newly synthesized selective casein kinase I inhibitor, N-(2-aminoethyl)-5-cloroisoquinoline-8-sulfonamide, and affinity purification of casein kinase I from bovine testis
    • Chijiwa, T., M. Hagiwara, and H. Hidaka. 1989. A newly synthesized selective casein kinase I inhibitor, N-(2-aminoethyl)-5-cloroisoquinoline-8-sulfonamide, and affinity purification of casein kinase I from bovine testis. J. Biol. Chem. 264:4924.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4924
    • Chijiwa, T.1    Hagiwara, M.2    Hidaka, H.3
  • 25
    • 0023000520 scopus 로고
    • Casein type II is involved in the inhibition by 5,6-dichloro-1-β-D-ribofuranosylbenzimidazole of specific RNA polymerase II transcription
    • Zandomeni, R., M. Zandomeni, D. Shugar, and R. Weinmann. 1986. Casein type II is involved in the inhibition by 5,6-dichloro-1-β-D-ribofuranosylbenzimidazole of specific RNA polymerase II transcription. J. Biol. Chem. 261:3414.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3414
    • Zandomeni, R.1    Zandomeni, M.2    Shugar, D.3    Weinmann, R.4
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 28
    • 0027427608 scopus 로고
    • Quantification of subnanomolar amounts of phosphate bound to seryl and threonyl residues in phosphoproteins using alkaline hydrolysis and malachite green
    • Ekman, P., and O. Jäger. 1993. Quantification of subnanomolar amounts of phosphate bound to seryl and threonyl residues in phosphoproteins using alkaline hydrolysis and malachite green. Anal. Biochem. 214:138.
    • (1993) Anal. Biochem. , vol.214 , pp. 138
    • Ekman, P.1    Jäger, O.2
  • 30
    • 0027339666 scopus 로고
    • Conformational epitopes of C3 reflecting its mode of binding to an artificial polymer surface
    • Nilsson, U. R., K.-E. Storm, H. Elwing, and B. Nilsson. 1993. Conformational epitopes of C3 reflecting its mode of binding to an artificial polymer surface. Mol. Immunol. 30:211.
    • (1993) Mol. Immunol. , vol.30 , pp. 211
    • Nilsson, U.R.1    Storm, K.-E.2    Elwing, H.3    Nilsson, B.4
  • 31
    • 0025096668 scopus 로고
    • The complement component C4 of mammals
    • Dodds, A. W., and S. K. A. Law. 1990. The complement component C4 of mammals. Biochem. J. 265:495.
    • (1990) Biochem. J. , vol.265 , pp. 495
    • Dodds, A.W.1    Law, S.K.A.2
  • 32
    • 0031573407 scopus 로고    scopus 로고
    • Cloning and chromosomal mapping of human casein kinase 1 γ2 (CKSNK1G2)
    • Kitabayashi, A. N., J. Kusudda, M. Hirani, and K. Hashimoto. 1997. Cloning and chromosomal mapping of human casein kinase 1 γ2 (CKSNK1G2). Genomics 46:133.
    • (1997) Genomics , vol.46 , pp. 133
    • Kitabayashi, A.N.1    Kusudda, J.2    Hirani, M.3    Hashimoto, K.4
  • 34
    • 0013141948 scopus 로고
    • Human complement component C3: cDNA coding sequence and derived primary structure
    • de Bruijn, M. H. L., and G. H. Fey. 1985. Human complement component C3: cDNA coding sequence and derived primary structure. Proc. Natl. Acad. Sci. USA 82:708.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 708
    • De Bruijn, M.H.L.1    Fey, G.H.2
  • 35
    • 0026587028 scopus 로고
    • The comparative efficiencies of the Ser(P)-, Thr(P)- and Tyr(P)-residues as specificity determinants for casein kinase-1
    • Meggio, F., J. W. Perich, O. Marin, and L. A. Pinna. 1992. The comparative efficiencies of the Ser(P)-, Thr(P)- and Tyr(P)-residues as specificity determinants for casein kinase-1. Biochem. Biophys. Res. Commun. 182:1460.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1460
    • Meggio, F.1    Perich, J.W.2    Marin, O.3    Pinna, L.A.4
  • 36
    • 0027415918 scopus 로고
    • Identification of a major binding site for complement C3 on the IgG1 heavy chain
    • Shohet, J. M., P. Pemberton, and M. C. Carroll. 1993. Identification of a major binding site for complement C3 on the IgG1 heavy chain. J. Biol. Chem. 268:5866.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5866
    • Shohet, J.M.1    Pemberton, P.2    Carroll, M.C.3
  • 37
    • 0027988132 scopus 로고
    • Covalent attachment of human complement C3 to IgG: Identification of the amino acid residue involved in ester linkage formation
    • Sahu, A., and M. K. Pangburn. 1994. Covalent attachment of human complement C3 to IgG: identification of the amino acid residue involved in ester linkage formation. J. Biol. Chem. 269:28997.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28997
    • Sahu, A.1    Pangburn, M.K.2
  • 38
    • 0029119566 scopus 로고
    • Tyrosine is a potential site for covalent attachment of activated complement component C3
    • Sahu, A., and M. K. Pangburn. 1995. Tyrosine is a potential site for covalent attachment of activated complement component C3. Mol. Immunol. 32:711.
    • (1995) Mol. Immunol. , vol.32 , pp. 711
    • Sahu, A.1    Pangburn, M.K.2
  • 39
    • 0032557324 scopus 로고    scopus 로고
    • X-ray crystal structure of C3d: A C3 fragment and ligand of complement receptor 2
    • Nagar, B., R. G. Jones, R. J. Diefenbach, D. E. Isenman, and J. M. Rini. 1998. X-ray crystal structure of C3d: a C3 fragment and ligand of complement receptor 2. Science 280:1277.
    • (1998) Science , vol.280 , pp. 1277
    • Nagar, B.1    Jones, R.G.2    Diefenbach, R.J.3    Isenman, D.E.4    Rini, J.M.5
  • 40
    • 0031043135 scopus 로고    scopus 로고
    • The internal thioester and the covalent binding properties of the complement proteins C3 and C4
    • Law, S. K. A., and A. W. Dodds. 1997. The internal thioester and the covalent binding properties of the complement proteins C3 and C4. Protein Sci. 6:263.
    • (1997) Protein Sci. , vol.6 , pp. 263
    • Law, S.K.A.1    Dodds, A.W.2
  • 41
    • 0022474684 scopus 로고
    • The role of complement and its receptor in the elimination of immune complexes
    • Schifferli, J. A., C. N. Ng, and D. K. Peters. 1986. The role of complement and its receptor in the elimination of immune complexes. N. Engl. J. Med. 315:486.
    • (1986) N. Engl. J. Med. , vol.315 , pp. 486
    • Schifferli, J.A.1    Ng, C.N.2    Peters, D.K.3


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