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Volumn 22, Issue 5, 1996, Pages 369-376

Determinants of substrate specificity for factor XIII

Author keywords

factor XIIIa; factor XIIIa substrate complex; fibrin; fibronectin; 2 antiplasma

Indexed keywords

ALPHA 2 ANTIPLASMIN; BLOOD CLOTTING FACTOR 13A; FIBRIN; FIBRONECTIN; MONOCLONAL ANTIBODY;

EID: 0030468786     PISSN: 00946176     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-2007-999034     Document Type: Review
Times cited : (37)

References (47)
  • 1
    • 0022924078 scopus 로고
    • Activation of blood coagulation factor XIIIa
    • Lorand L: Activation of blood coagulation factor XIIIa. Ann NY Acad Sci 485:144-158, 1986.
    • (1986) Ann NY Acad Sci , vol.485 , pp. 144-158
    • Lorand, L.1
  • 2
    • 0016267498 scopus 로고
    • Calcium-dependent unmasking of active-center cysteine during activation of fibrin stabilizing factor
    • Curtis CG, KL Brown, RB Credo, RA Domanik, A Gray, P Stenberg, L Lorand: Calcium-dependent unmasking of active-center cysteine during activation of fibrin stabilizing factor. Biochemistry 13:3774-3780, 1974.
    • (1974) Biochemistry , vol.13 , pp. 3774-3780
    • Curtis, C.G.1    Brown, K.L.2    Credo, R.B.3    Domanik, R.A.4    Gray, A.5    Stenberg, P.6    Lorand, L.7
  • 3
    • 0025819769 scopus 로고
    • Role of calcium ion in the generation of factor XIII activity
    • Hornyak TJ, JA Shafer: Role of calcium ion in the generation of factor XIII activity. Biochemistry 30:6175-6182, 1991.
    • (1991) Biochemistry , vol.30 , pp. 6175-6182
    • Hornyak, T.J.1    Shafer, J.A.2
  • 4
    • 0015935236 scopus 로고
    • Human factor XIII from plasma and platelets. Molecular weights, subunit structure, proteolytic activation and cross-linking of fibrinogen and fibrin
    • Schwartz ML, SV Pizzo, RL Hill, PA McKee: Human factor XIII from plasma and platelets. Molecular weights, subunit structure, proteolytic activation and cross-linking of fibrinogen and fibrin. J Biol Chem 248:1395-1407, 1973.
    • (1973) J Biol Chem , vol.248 , pp. 1395-1407
    • Schwartz, M.L.1    Pizzo, S.V.2    Hill, R.L.3    McKee, P.A.4
  • 7
    • 0022496583 scopus 로고
    • Amino acid sequence of the b subunit of human factor XIII, a protein composed of ten repetitive segments
    • Ichinose A, BA McMullen, K Fujikawa, EW Davie: Amino acid sequence of the b subunit of human factor XIII, a protein composed of ten repetitive segments. Biochemistry 25:4633-4638, 1986.
    • (1986) Biochemistry , vol.25 , pp. 4633-4638
    • Ichinose, A.1    McMullen, B.A.2    Fujikawa, K.3    Davie, E.W.4
  • 8
    • 0025356997 scopus 로고
    • Complete cDNA sequence encoding the B subunit of human factor XIII
    • Grundmann U, C Nerlich, T Rein, G Zettlmeissl: Complete cDNA sequence encoding the B subunit of human factor XIII. Nucleic Acid Res 18:2817-2818, 1990.
    • (1990) Nucleic Acid Res , vol.18 , pp. 2817-2818
    • Grundmann, U.1    Nerlich, C.2    Rein, T.3    Zettlmeissl, G.4
  • 10
    • 0028291204 scopus 로고
    • Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules
    • Pedersen LC, VC Yee, PD Bishop, I Le Trong, DC Teller, RE Stenkamp: Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules. Prot Sci 3:1131-1135, 1994.
    • (1994) Prot Sci , vol.3 , pp. 1131-1135
    • Pedersen, L.C.1    Yee, V.C.2    Bishop, P.D.3    Le Trong, I.4    Teller, D.C.5    Stenkamp, R.E.6
  • 11
    • 0040386245 scopus 로고
    • Structure and function of factor XIII
    • Colman RW, J Hirsh, VJ Marder, EW Salzman (Eds): Lippincott, Philadelphia
    • McDonagh J: Structure and function of factor XIII. In: Colman RW, J Hirsh, VJ Marder, EW Salzman (Eds): Hemostasis and Thrombosis: Basic Principles and Clinical Practice. 2nd ed. Lippincott, Philadelphia, 1987, pp 289-301.
    • (1987) Hemostasis and Thrombosis: Basic Principles and Clinical Practice. 2nd Ed. , pp. 289-301
    • McDonagh, J.1
  • 13
    • 0020596436 scopus 로고
    • Contribution of fibrin stabilization to clot strength
    • Shen L, L Lorand: Contribution of fibrin stabilization to clot strength. J Clin Invest 71:1336-1341, 1983.
    • (1983) J Clin Invest , vol.71 , pp. 1336-1341
    • Shen, L.1    Lorand, L.2
  • 14
    • 0020077284 scopus 로고
    • 2-plasmin inhibitor to fibrin in inhibition of fibrinolysis and in hemostasis
    • 2-plasmin inhibitor to fibrin in inhibition of fibrinolysis and in hemostasis. J Clin Invest 69:536-542, 1982.
    • (1982) J Clin Invest , vol.69 , pp. 536-542
    • Sakata, Y.1    Aoki, N.2
  • 15
    • 0016719143 scopus 로고
    • Crosslinking of cold-insoluble globulin by fibrin-stabilizing factor
    • Mosher DF: Crosslinking of cold-insoluble globulin by fibrin-stabilizing factor. J Biol Chem 250:6614-6621, 1975.
    • (1975) J Biol Chem , vol.250 , pp. 6614-6621
    • Mosher, D.F.1
  • 16
    • 0017735718 scopus 로고
    • Amine binding sites in acyl intermediates of transglutaminases. Human blood plasma enzyme (activated coagulation factor XIII) and guinea pig liver enzyme
    • Gross M, NK Whetzel, JE Folk: Amine binding sites in acyl intermediates of transglutaminases. Human blood plasma enzyme (activated coagulation factor XIII) and guinea pig liver enzyme. J Biol Chem 252:3752-3759, 1977.
    • (1977) J Biol Chem , vol.252 , pp. 3752-3759
    • Gross, M.1    Whetzel, N.K.2    Folk, J.E.3
  • 17
    • 0017757433 scopus 로고
    • Physical evidence for an apolar binding site near the catalytic center of human α-thrombin
    • Berliner LJ, YYW Shen: Physical evidence for an apolar binding site near the catalytic center of human α-thrombin. Biochemistry 16:4622-4626, 1977.
    • (1977) Biochemistry , vol.16 , pp. 4622-4626
    • Berliner, L.J.1    Shen, Y.Y.W.2
  • 18
    • 0021142637 scopus 로고
    • Structural features of glutamine substrates for transglutaminases. Role of extended interactions in the specificity of human plasma factor XIIIa and of the guinea pig liver enzyme
    • Gorman JJ, JE Folk: Structural features of glutamine substrates for transglutaminases. Role of extended interactions in the specificity of human plasma factor XIIIa and of the guinea pig liver enzyme. J Biol Chem 259:9007-9010, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 9007-9010
    • Gorman, J.J.1    Folk, J.E.2
  • 19
    • 0023687916 scopus 로고
    • The binding sites on fibrin(ogen) for guinea pig liver transglutaminase are similar to those of blood coagulation factor XIII
    • Achyuthan KE, A Mary, CS Greenberg: The binding sites on fibrin(ogen) for guinea pig liver transglutaminase are similar to those of blood coagulation factor XIII. J Biol Chem 263:14296-14301, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 14296-14301
    • Achyuthan, K.E.1    Mary, A.2    Greenberg, C.S.3
  • 20
    • 0020698882 scopus 로고
    • Mechanism and basis for specificity of transglutaminase-catalyzed ε-(γ-glutamyl) lysine bond formation
    • Folk JE: Mechanism and basis for specificity of transglutaminase-catalyzed ε-(γ-glutamyl) lysine bond formation. Adv Enzymol 54:1-56, 1983.
    • (1983) Adv Enzymol , vol.54 , pp. 1-56
    • Folk, J.E.1
  • 21
    • 0019887851 scopus 로고
    • Structural features of glutamine substrates for transglutaminases. Specificities of human plasma factor XIIIa and the guinea pig liver enzyme toward synthetic peptides
    • Gorman JJ, JE Folk: Structural features of glutamine substrates for transglutaminases. Specificities of human plasma factor XIIIa and the guinea pig liver enzyme toward synthetic peptides. J Biol Chem 256:2712-2715, 1981.
    • (1981) J Biol Chem , vol.256 , pp. 2712-2715
    • Gorman, J.J.1    Folk, J.E.2
  • 22
    • 0017600292 scopus 로고
    • Amino acid sequence studies on the α-chain of human fibrinogen. Isolation and characterization of two linked α-chained cyanogen bromide fragments from fully crosslinked fibrin
    • Doolittle RF, KG Cassman, BA Cottrell, SJ Friezner: Amino acid sequence studies on the α-chain of human fibrinogen. Isolation and characterization of two linked α-chained cyanogen bromide fragments from fully crosslinked fibrin. Biochemistry 16:1715-1719, 1977.
    • (1977) Biochemistry , vol.16 , pp. 1715-1719
    • Doolittle, R.F.1    Cassman, K.G.2    Cottrell, B.A.3    Friezner, S.J.4
  • 23
    • 0022979474 scopus 로고
    • 2-plasmin inhibitor
    • 2-plasmin inhibitor. J Biol Chem 261:15591-15595, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 15591-15595
    • Kimura, S.1    Aoki, N.2
  • 26
    • 0026593429 scopus 로고
    • A unique factor XIII inhibitor to a fibrin binding site on factor XIIIA
    • Fukue H, K Anderson, P McPhedran, J Clyne, J McDonagh: A unique factor XIII inhibitor to a fibrin binding site on factor XIIIA. Blood 79:65-74, 1992.
    • (1992) Blood , vol.79 , pp. 65-74
    • Fukue, H.1    Anderson, K.2    McPhedran, P.3    Clyne, J.4    McDonagh, J.5
  • 27
    • 0017904888 scopus 로고
    • Bovine plasma cold-insoluble globulin: Gross structure and function
    • Iwanaga S, K Suzuki, S Hashimoto: Bovine plasma cold-insoluble globulin: Gross structure and function. Ann NY Acad Sci 312:56-73, 1978.
    • (1978) Ann NY Acad Sci , vol.312 , pp. 56-73
    • Iwanaga, S.1    Suzuki, K.2    Hashimoto, S.3
  • 28
    • 0023215552 scopus 로고
    • Characterization of thrombospondin as a substrate for factor XIII transglutaminase
    • Lynch GW, HW Slayter, BE Miller, J McDonagh: Characterization of thrombospondin as a substrate for factor XIII transglutaminase. J Biol Chem 262:1772-1778, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 1772-1778
    • Lynch, G.W.1    Slayter, H.W.2    Miller, B.E.3    McDonagh, J.4
  • 29
    • 0014940727 scopus 로고
    • The cold-insoluble globulin of human plasma. I. Purification, primary characterization, and relationship to fibrinogen and other cold-insoluble fraction components
    • Mosesson MW, RA Umfleet: The cold-insoluble globulin of human plasma. I. Purification, primary characterization, and relationship to fibrinogen and other cold-insoluble fraction components. J Biol Chem 245:5728-5736, 1970.
    • (1970) J Biol Chem , vol.245 , pp. 5728-5736
    • Mosesson, M.W.1    Umfleet, R.A.2
  • 30
    • 0014526059 scopus 로고
    • Diagnostic and genetic studies on fibrin-stabilizing factor with a new assay based on amine incorporation
    • Lorand L, T Urayama, JW De Kiewiet, HL Nossel: Diagnostic and genetic studies on fibrin-stabilizing factor with a new assay based on amine incorporation. J Clin Invest 48:1054-1064, 1969.
    • (1969) J Clin Invest , vol.48 , pp. 1054-1064
    • Lorand, L.1    Urayama, T.2    De Kiewiet, J.W.3    Nossel, H.L.4
  • 31
    • 0020645335 scopus 로고
    • Specificity of fibronectin-fibrin cross-linking
    • Mosher DF, RB Johnson: Specificity of fibronectin-fibrin cross-linking. Ann NY Acad Sci 408:583-594, 1983.
    • (1983) Ann NY Acad Sci , vol.408 , pp. 583-594
    • Mosher, D.F.1    Johnson, R.B.2
  • 33
    • 0006425177 scopus 로고
    • Plasma fibronectin: Structure and function
    • McDonagh J (ed): Marcel Dekker, New York
    • McDonagh J, M Hada, M Kaminski: Plasma fibronectin: Structure and function. In: McDonagh J (ed): Plasma Fibronectin and Fibrin Formation. Marcel Dekker, New York 1985, pp 121-148.
    • (1985) Plasma Fibronectin and Fibrin Formation , pp. 121-148
    • McDonagh, J.1    Hada, M.2    Kaminski, M.3
  • 34
    • 0023583663 scopus 로고
    • Influence of factor XIII and fibronectin on fiber size in thrombin-induced fibrin gels
    • Carr ME, DA Gabriel, J McDonagh: Influence of factor XIII and fibronectin on fiber size in thrombin-induced fibrin gels. J Lab Clin Med 110:747-752, 1987.
    • (1987) J Lab Clin Med , vol.110 , pp. 747-752
    • Carr, M.E.1    Gabriel, D.A.2    McDonagh, J.3
  • 35
    • 0019781878 scopus 로고
    • 2-plasmin inhibitor and fibronectin to fibrin by fibrin-stabilizing factor
    • 2-plasmin inhibitor and fibronectin to fibrin by fibrin-stabilizing factor. Biochim Biophys Acta 661:280-286, 1981.
    • (1981) Biochim Biophys Acta , vol.661 , pp. 280-286
    • Tamaki, T.1    Aoki, N.2
  • 36
    • 0024234639 scopus 로고
    • Isolation of a fibrin-binding fragment from blood coagulation factor XIII capable of cross-linking fibrin(ogen)
    • Greenberg CS, JJ Enghild, A Mary, JV Dobson, KE Achyuthan: Isolation of a fibrin-binding fragment from blood coagulation factor XIII capable of cross-linking fibrin(ogen). Biochem J 256:1013-1019, 1988.
    • (1988) Biochem J , vol.256 , pp. 1013-1019
    • Greenberg, C.S.1    Enghild, J.J.2    Mary, A.3    Dobson, J.V.4    Achyuthan, K.E.5
  • 37
    • 0026569887 scopus 로고
    • Interactions of factor XIII with fibrin as substrate and cofactor
    • Hornyak TJ, JA Shafer: Interactions of factor XIII with fibrin as substrate and cofactor. Biochemistry 31:423-429, 1992.
    • (1992) Biochemistry , vol.31 , pp. 423-429
    • Hornyak, T.J.1    Shafer, J.A.2
  • 38
    • 0022374973 scopus 로고
    • Regulation of formation of factor XIIIa by its fibrin substrates
    • Lewis SD, TJ Janus, L Lorand, JA Shafer: Regulation of formation of factor XIIIa by its fibrin substrates. Biochemistry 24:6772-6777, 1985.
    • (1985) Biochemistry , vol.24 , pp. 6772-6777
    • Lewis, S.D.1    Janus, T.J.2    Lorand, L.3    Shafer, J.A.4
  • 39
    • 0021797623 scopus 로고
    • The effect of fibrin polymers on thrombin-catalyzed plasma factor XIIIa formation
    • Greenberg CS, CC Miraglia: The effect of fibrin polymers on thrombin-catalyzed plasma factor XIIIa formation. Blood 66:466-469, 1985.
    • (1985) Blood , vol.66 , pp. 466-469
    • Greenberg, C.S.1    Miraglia, C.C.2
  • 40
    • 0015152036 scopus 로고
    • Mechanism of action of guinea pig liver transglutaminase. VIII. Active site studies with "reporter" group-labeled halomethyl ketones
    • Folk JE, M Gross: Mechanism of action of guinea pig liver transglutaminase. VIII. Active site studies with "reporter" group-labeled halomethyl ketones. J Biol Chem 246:6683-6691, 1971.
    • (1971) J Biol Chem , vol.246 , pp. 6683-6691
    • Folk, J.E.1    Gross, M.2
  • 41
    • 0015500905 scopus 로고
    • Kinetic studies with transglutaminases. The human blood enzymes (activated coagulation factor XIII) and the guinea pig hair follicle enzyme
    • Chung SI, JE Folk: Kinetic studies with transglutaminases. The human blood enzymes (activated coagulation factor XIII) and the guinea pig hair follicle enzyme. J Biol Chem 247:2798-2807, 1972.
    • (1972) J Biol Chem , vol.247 , pp. 2798-2807
    • Chung, S.I.1    Folk, J.E.2
  • 42
    • 0016703755 scopus 로고
    • Effects of calcium ion and covalent crosslinking on formation and elasticity of fibrin gels
    • Shen LL, J Hermans, J McDonagh, RP McDonagh Jr, M Carr: Effects of calcium ion and covalent crosslinking on formation and elasticity of fibrin gels. Thromb Res 6:255-265, 1975.
    • (1975) Thromb Res , vol.6 , pp. 255-265
    • Shen, L.L.1    Hermans, J.2    McDonagh, J.3    McDonagh Jr., R.P.4    Carr, M.5
  • 43
    • 0015121378 scopus 로고
    • The influence of fibrin crosslinking on the kinetics of urokinase-induced clot lysis
    • McDonagh RP Jr, J McDonagh, F Ducken: The influence of fibrin crosslinking on the kinetics of urokinase-induced clot lysis. Br J Haematol 21:323-332, 1971.
    • (1971) Br J Haematol , vol.21 , pp. 323-332
    • McDonagh Jr., R.P.1    McDonagh, J.2    Ducken, F.3
  • 44
    • 0015498627 scopus 로고
    • Documentation of the plasma factor XIII deficiency in man
    • Duckert F: Documentation of the plasma factor XIII deficiency in man. Ann NY Acad Sci 202:190-199, 1972.
    • (1972) Ann NY Acad Sci , vol.202 , pp. 190-199
    • Duckert, F.1
  • 45
    • 0018386560 scopus 로고
    • Fibrin crosslinks and lysis rates
    • Gaffney PJ, AN Whitaker: Fibrin crosslinks and lysis rates. Thromb Res 14:85-94, 1979.
    • (1979) Thromb Res , vol.14 , pp. 85-94
    • Gaffney, P.J.1    Whitaker, A.N.2
  • 47
    • 0016853736 scopus 로고
    • Lysis of crosslinked and non-crosslinked purified fibrin
    • Haverkate F: Lysis of crosslinked and non-crosslinked purified fibrin. Thromb Diath Haemorrh 34:584-585, 1975.
    • (1975) Thromb Diath Haemorrh , vol.34 , pp. 584-585
    • Haverkate, F.1


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