Regulation of extravascular fibrinolysis by factor XIII

Uchino, Ryojin; Cardinali, M.; Chung, Soo‐Il

doi:10.1016/0268-9499(91)90049-a

Cited by 14 publications

(13 citation statements)

References 20 publications

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“…43 Evaluation of the influence of factor XIII-mediated cross-linking of fibrin on fibrinolysis by elastase, carried out with pure fibrin clots as well as with normal plasma and factor XIII-deficient plasma clots, showed that the lysis of polymerized fibrin was significantly delayed. [43][44][45] The difference in the susceptibility of fibrinogen to elas tase compared to fibrin might be due to steric hindrance of elastase cleavage sites of fibrinogen chains when they are assembled in an insoluble gel of fibrin. 46 The faster lysis of non-cross-linked fibrin, compared to factor XIIIpolymerized fibrin, suggests some structural differences between the two forms of fibrin with respect to accessible cleavage sites available to elastase, such as shown for other proteases.…”

Section: Fibrin(ogen) Degradation In Vitromentioning

confidence: 99%

“…SDS-PAGE analysis of cross-linked and non-cross-linked fibrin degradation by elastase showed that in non-cross-linked fibrin the a chains appear to be degraded first. [43][44][45] In cross-linked fibrin α-chain poly mers, α-chain monomers and γ-γ dimer were frag mented. [43][44][45] In both, cross-linked and non-cross-linked fibrin (3 chains appeared unaffected in the early stages of degradation.…”

Section: Fibrin(ogen) Degradation In Vitromentioning

confidence: 99%

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Fibrin Degradation in the Synovial Fluid of Rheumatoid Arthritis Patients: A Model for Extravascular Fibrinolysis

Carmassi¹,

Negri²,

Morale³

et al. 1996

Semin Thromb Hemost

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The patterns of degradation and the influence of factor XIII polymerization on fibrin stability were examined in vitro following incubation with leukocyte elastase. In vivo experiments, various factor XIII-polymerized fibrin clots were implanted subcutaneously in mice to evaluate the stability of clots in the extravascular space. Both in vitro and in vivo lysis proceeded faster with nonpolymerized fibrin and was not influenced by the presence of cross-linked alpha 2-plasmin inhibitor. In vivo lysis of implanted clots was prevented by elastatinal, powerful elastase inhibitor, suggesting that granulocyte elastase is chiefly responsible for clot lysis in the extravascular space. To further extend investigations on the mechanisms of fibrinolysis in tissues, we evaluated fibrin and its degradation products in the synovial space. Expression of factor XIII in synovial cells and activities of coagulation factors, fibrinolytic enzymes, and inhibitors were investigated in the synovial fluid of rheumatoid arthritis patients. Immunohistochemical analysis showed deposits of insoluble fibrin on synovial membranes and pannus to an extent related to the progression of the disease. Factor XIII was expressed by fibroblasts and macrophages in the early stages of the disease, whereas in advanced stages factor XIII staining was associated with fibrin. The reduction of certain coagulation factors and high level of thrombin-antithrombin complexes in synovial fluid show a steady activation of the coagulation cascade. The evaluation of fibrinogen degradation products and the pattern of degradation of synovial fibrin(ogen) suggest the participation of leukocyte elastase in fibrin(ogen) lysis in synovial tissue of rheumatoid arthritis.

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Section: Fibrin(ogen) Degradation In Vitromentioning

confidence: 99%

Section: Fibrin(ogen) Degradation In Vitromentioning

confidence: 99%

Fibrin Degradation in the Synovial Fluid of Rheumatoid Arthritis Patients: A Model for Extravascular Fibrinolysis

Carmassi¹,

Negri²,

Morale³

et al. 1996

Semin Thromb Hemost

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“…These findings suggest that the oxidizing environment that exists during the inflamma tory state could affect the cross-linking of fibrin and its stability. In fact, fibrin is found to be extensively crosslinked 114,115 in the presence of red blood cells, which are known to release glutathione, whereas in inflammatory sites where oxidative conditions prevail, fibrin is found to be partially cross-linked. [116][117][118]…”

Section: Albuminmentioning

confidence: 99%

“…At the same time, the results agree with other tissue fi brinolysis findings that cross-linking of fibrin is one of the key factors that contributes to fibrin stability in vivo. 115…”

Section: Localized Shwartzman Reaction (Lsr)mentioning

confidence: 99%

“…In an effort to understand the level of structural modification that provides in vivo stability, 125 I-labeled fibrin clots under various cross-linked conditions, were implanted subcutaneously into Bal/c mice and the rate of degradation of the 125 I-labeled fibrin clots examined. 115 Cross-linking of fibrin in the presence of a high level of factor XIIIa resulted in complete conversion of 7-chain monomers to γ-γ dimers and extensive covalent poly merization of the α-chain monomers. This fibrin, cate gorized as fully cross-linked (FXL), showed a 50% clot lysis time (LT 50 ) of 9.6 days.…”

Section: Subcutaneous Fibrinolysismentioning

confidence: 99%

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Factors That Control Extravascular Fibrinolysis

Chung¹,

Lee²,

Uchino³

et al. 1996

Semin Thromb Hemost

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The physiological and pathophysiological state of tissues determines the exudation of plasma proteins, hemostasis, and fibrinolysis, i.e., inflammation, injury, and malignancy. The physiological controls of extravascular fibrinolysis ultimately rest on a balance between generation of the fibrinolytic enzyme(s), i.e., plasmin, elastase, cathepsins, etc., and inhibitors of the fibrinolytic enzyme(s), i.e., plasminogen activator inhibitors, alpha-2 plasmin inhibitor, alpha 1-protease inhibitors, etc. Moreover, it is the structural modification of fibrin that determines its stability toward proteolytic enzymes and physical duress. The structural modification of fibrin involves factor XIIIa-mediated cross-linking of interfibrin chains and alpha 2-plasmin inhibitor to fibrin. In turn, there are a number of agents that influence factor XIIIa catalytic activity (e.g., sulfhydryl agents, albumin, erythrocytes). The two key proenzymes, factor XIII and plasminogen, are tightly bound with the circulating fibrinogen molecules. Such high selective affinity for fibrin(ogen) provides the reaction specificity in a complex tissue fluid milieu and governs the kinetics of fibrinolysis. Any agents that interfere with such binding reactions, e.g., autoantibodies, may also affect the fibrinolytic reactions. Understanding these unique biochemical controls of factors involved in fibrinolysis may provide an insight into the complex regulatory process of extravascular fibrinolysis.

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