메뉴 건너뛰기




Volumn 162, Issue 1, 1996, Pages 43-49

Hierarchies in the binding of human factor XIII, factor XIIIa, and endothelial cell transglutaminase to human plasma fibrinogen, fibrin, and fibronectin

Author keywords

Binding; Factor XIII; Fibrin; Fibrinogen; Fibronectin; Transglutaminase

Indexed keywords

BLOOD CLOTTING FACTOR 13; BLOOD CLOTTING FACTOR 13A; FIBRIN; FIBRINOGEN; FIBRONECTIN; LIGAND; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 0029852433     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00250994     Document Type: Article
Times cited : (19)

References (28)
  • 1
    • 0026338017 scopus 로고
    • Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg CS, Birckbichler PJ, Rice RH: Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues. FASEB J 5:3071-3077, 1991
    • (1991) FASEB J , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 2
    • 0023697021 scopus 로고
    • Factor XIII-induced crosslinking in solutions of fibrinogen and fibronectin
    • Procyk R, Blomback B: Factor XIII-induced crosslinking in solutions of fibrinogen and fibronectin. Biochim Biophys Acta 967: 304-313, 1988
    • (1988) Biochim Biophys Acta , vol.967 , pp. 304-313
    • Procyk, R.1    Blomback, B.2
  • 3
    • 0020630776 scopus 로고
    • Fibronectin. Effect of disulfide bond reduction on its physical and functional properties
    • Williams EC, Janmey PA, Johnson RB, Mosher DF: Fibronectin. Effect of disulfide bond reduction on its physical and functional properties. J Biol Chem 258: 5911-5914, 1983
    • (1983) J Biol Chem , vol.258 , pp. 5911-5914
    • Williams, E.C.1    Janmey, P.A.2    Johnson, R.B.3    Mosher, D.F.4
  • 4
    • 0016719143 scopus 로고
    • Cross-linking of cold-insoluble globulin by fibrin-stabilizing factor
    • Mosher DF: Cross-linking 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
  • 5
    • 0025328948 scopus 로고
    • Binding and degradation of blood coagulation factor XIII by cultured fibroblasts
    • Barry ELR, Mosher DF: Binding and degradation of blood coagulation factor XIII by cultured fibroblasts. J Biol Chem 265: 9302-9307, 1990
    • (1990) J Biol Chem , vol.265 , pp. 9302-9307
    • Barry, E.L.R.1    Mosher, D.F.2
  • 6
    • 0023543523 scopus 로고
    • The transglutaminase in vascular cells and tissues could provide an alternate pathway for fibrin stabilization
    • Greenberg CS, Achyuthan KE, Borowitz MJ, Shuman MA: The transglutaminase in vascular cells and tissues could provide an alternate pathway for fibrin stabilization. Blood 70: 702-709, 1987
    • (1987) Blood , vol.70 , pp. 702-709
    • Greenberg, C.S.1    Achyuthan, K.E.2    Borowitz, M.J.3    Shuman, M.A.4
  • 7
    • 0018200368 scopus 로고
    • Cellular transglutaminase, growth, and transformation
    • Birckbichler PJ, Patterson MK Jr.: Cellular transglutaminase, growth, and transformation. Ann NY Acad Sci 312: 355-365, 1978
    • (1978) Ann NY Acad Sci , vol.312 , pp. 355-365
    • Birckbichler, P.J.1    Patterson Jr., M.K.2
  • 8
    • 0025837326 scopus 로고
    • Tissue (type II) transglutaminase covalently incorporates itself, fibrinogen, or fibronectin into high molecular weight complexes on the extracellular surface of isolated hepatocytes. Use of 2-[2-oxopropylthio]imidazolium derivatives as cellular transglutaminase inactivators
    • Barsigian C, Stern AM, Martinez J: Tissue (type II) transglutaminase covalently incorporates itself, fibrinogen, or fibronectin into high molecular weight complexes on the extracellular surface of isolated hepatocytes. Use of 2-[2-oxopropyl)thio]imidazolium derivatives as cellular transglutaminase inactivators. J Biol Chem 266: 22501-22509, 1991
    • (1991) J Biol Chem , vol.266 , pp. 22501-22509
    • Barsigian, C.1    Stern, A.M.2    Martinez, J.3
  • 9
    • 0027375114 scopus 로고
    • Transglutaminases catalyze cross-linking of plasminogen to fibronectin and human endothelial cells
    • Bendixen E, Borth W, Harpel PC: Transglutaminases catalyze cross-linking of plasminogen to fibronectin and human endothelial cells. J Biol Chem 268: 21962-21967, 1993
    • (1993) J Biol Chem , vol.268 , pp. 21962-21967
    • Bendixen, E.1    Borth, W.2    Harpel, P.C.3
  • 10
    • 0028231735 scopus 로고
    • Transglutaminase-mediated processing of fibronectin by endothelial cell monolayers
    • Martinez J, Chalupowicz DG, Roush RK, Sheth A, Barsigian C: Transglutaminase-mediated processing of fibronectin by endothelial cell monolayers. Biochemistry 33: 2538-2545, 1994
    • (1994) Biochemistry , vol.33 , pp. 2538-2545
    • Martinez, J.1    Chalupowicz, D.G.2    Roush, R.K.3    Sheth, A.4    Barsigian, C.5
  • 11
    • 0025885719 scopus 로고
    • Localization of cellular transglutaminase on the extracellular matrix after wounding: Characteristics of the matrix bound enzyme
    • Upchurch HF, Conway E, Patterson Jr. MK, Maxwell MD: Localization of cellular transglutaminase on the extracellular matrix after wounding: Characteristics of the matrix bound enzyme. J Cell Physiol 149:375-382, 1991
    • (1991) J Cell Physiol , vol.149 , pp. 375-382
    • Upchurch, H.F.1    Conway, E.2    Patterson Jr., M.K.3    Maxwell, M.D.4
  • 12
    • 0028170881 scopus 로고
    • Increase in ε-(γ-glutamyl)lysine crosslinks in the atherosclerotic aortas
    • Bowness JM, Venditti M, Tarr AH, Taylor JR: Increase in ε-(γ-glutamyl)lysine crosslinks in the atherosclerotic aortas. Atherosclerosis 111:247-253, 1994
    • (1994) Atherosclerosis , vol.111 , pp. 247-253
    • Bowness, J.M.1    Venditti, M.2    Tarr, A.H.3    Taylor, J.R.4
  • 13
    • 0026729988 scopus 로고
    • Immunoelectrophoretic and immunohistochemical characterizations of fibrinogen derivatives in atherosclerotic aortic intimas and vascular prosthesis pseudo-intimas
    • Valenzuela R, Shainoff JR, DiBello PM, Urbanic DA, Anderson JM, Matsueda GR, Kudryk BJ: Immunoelectrophoretic and immunohistochemical characterizations of fibrinogen derivatives in atherosclerotic aortic intimas and vascular prosthesis pseudo-intimas. Am J Pathol 141: 861-880, 1992
    • (1992) Am J Pathol , vol.141 , pp. 861-880
    • Valenzuela, R.1    Shainoff, J.R.2    DiBello, P.M.3    Urbanic, D.A.4    Anderson, J.M.5    Matsueda, G.R.6    Kudryk, B.J.7
  • 15
    • 0021284162 scopus 로고
    • ε-(γ-glutamic)lysine cross-link: Method of analysis, occurrence in extracellular and cellular proteins
    • ε-(γ-glutamic)lysine cross-link: method of analysis, occurrence in extracellular and cellular proteins. Meth Enzymol 107: 241-257, 1984
    • (1984) Meth Enzymol , vol.107 , pp. 241-257
    • Loewy, A.G.1
  • 18
    • 0023687916 scopus 로고
    • The binding sites on fibrin(ogen) for guinea pig liver transglutaminase are similar to those of blood coagulation factor XIII. Characterization of the binding of liver transglutaminase to fibrin
    • Achyuthan KE, Mary A, Greenberg CS: The binding sites on fibrin(ogen) for guinea pig liver transglutaminase are similar to those of blood coagulation factor XIII. Characterization of the binding of liver transglutaminase to fibrin. 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
    • 0020316936 scopus 로고
    • The zymogen forms of blood coagulation factor XIII bind specifically to fibrinogen
    • Greenberg CS, Shuman MA: The zymogen forms of blood coagulation factor XIII bind specifically to fibrinogen. J Biol Chem 257: 6096-6101, 1982
    • (1982) J Biol Chem , vol.257 , pp. 6096-6101
    • Greenberg, C.S.1    Shuman, M.A.2
  • 21
    • 0026083164 scopus 로고
    • Characterization of the kinetic pathway for fibrin promotion of α-thrombin-catalyzed activation of plasma factor XIII
    • Naski MC, Lorand L, Shafer JA: Characterization of the kinetic pathway for fibrin promotion of α-thrombin-catalyzed activation of plasma factor XIII. Biochemistry 30: 934-941, 1991
    • (1991) Biochemistry , vol.30 , pp. 934-941
    • Naski, M.C.1    Lorand, L.2    Shafer, J.A.3
  • 22
    • 0026569887 scopus 로고
    • Interactions of factor XIII with fibrin as substrate and cofactor
    • Hornyak TJ, Shafer JA: 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
  • 23
    • 0028283181 scopus 로고
    • A microtiter plate assay for factor XIII A-chain fibrin interactions
    • Achyuthan KE, Santiago MA, Greenberg CS: A microtiter plate assay for factor XIII A-chain fibrin interactions. Anal Biochem 219: 43-48, 1994
    • (1994) Anal Biochem , vol.219 , pp. 43-48
    • Achyuthan, K.E.1    Santiago, M.A.2    Greenberg, C.S.3
  • 24
    • 0023140632 scopus 로고
    • Factor XIIIa formation promoted by complexing of α-thrombin, fibrin, and plasma factor XIII
    • Greenberg CS, Achyuthan KE, Fenton JW: Factor XIIIa formation promoted by complexing of α-thrombin, fibrin, and plasma factor XIII. Blood 69: 867-871, 1987
    • (1987) Blood , vol.69 , pp. 867-871
    • Greenberg, C.S.1    Achyuthan, K.E.2    Fenton, J.W.3
  • 25
    • 0023751852 scopus 로고
    • b-chains prevent the proteolytic inactivation of the a-chains of plasma factor XIII
    • Mary A, Achyuthan KE, Greenberg CS: b-chains prevent the proteolytic inactivation of the a-chains of plasma factor XIII. Biochim Biophys Acta 966: 328-335, 1988
    • (1988) Biochim Biophys Acta , vol.966 , pp. 328-335
    • Mary, A.1    Achyuthan, K.E.2    Greenberg, C.S.3
  • 26
    • 0024533495 scopus 로고
    • Interaction of a 59-kDa connective tissue matrix protein with collagen I and collagen II
    • Hedbom E, Heinegard D: Interaction of a 59-kDa connective tissue matrix protein with collagen I and collagen II. J Biol Chem 264: 6898-6905, 1989
    • (1989) J Biol Chem , vol.264 , pp. 6898-6905
    • Hedbom, E.1    Heinegard, D.2
  • 27
    • 0021035369 scopus 로고
    • Studies on the mechanism of thrombin. Interaction with fibrin
    • Kaminski MP, McDonagh J: Studies on the mechanism of thrombin. Interaction with fibrin. J Biol Chem 258: 10530-10535, 1983
    • (1983) J Biol Chem , vol.258 , pp. 10530-10535
    • Kaminski, M.P.1    McDonagh, J.2
  • 28
    • 0001520606 scopus 로고
    • A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli: I. Purification and characterization of alkaline phosphatase
    • Garen A, Levinthal C: A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli: I. Purification and characterization of alkaline phosphatase. Biochim Biophys Acta: 38: 470-483, 1960
    • (1960) Biochim Biophys Acta , vol.38 , pp. 470-483
    • Garen, A.1    Levinthal, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.