Fibrinolysis and Proteolysis最新文献_第10页

Prothrombin promotes the invasiveness of melanoma cells by a different mechanism from thrombin 凝血酶原促进黑色素瘤细胞侵袭的机制与凝血酶不同

Fibrinolysis and Proteolysis Pub Date : 1999-11-01 DOI: 10.1054/FIPR.2000.0040

Hong Zhou, E. Gabazza, T. Sano, Y. Adachi, Koji Suzuki

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引用次数: 3

Subject index to Volume 13 第13卷的主题索引

Fibrinolysis and Proteolysis Pub Date : 1999-11-01 DOI: 10.1054/fipr.2000.0049

引用次数: 0

Soluble thrombomodulin quenches thrombin-mediated neutralization of PAI-1 activity and inhibits fibrinolysis through a TAFI independent mechanism 可溶性血栓调节蛋白通过TAFI独立机制抑制凝血酶介导的PAI-1活性中和和纤维蛋白溶解

Fibrinolysis and Proteolysis Pub Date : 1999-11-01 DOI: 10.1054/FIPR.2000.0041

T. Urano, H. Ihara, Yasuhiro Suzuki, N. Nagai, Y. Takada, A. Takada

{"title":"Soluble thrombomodulin quenches thrombin-mediated neutralization of PAI-1 activity and inhibits fibrinolysis through a TAFI independent mechanism","authors":"T. Urano, H. Ihara, Yasuhiro Suzuki, N. Nagai, Y. Takada, A. Takada","doi":"10.1054/FIPR.2000.0041","DOIUrl":"https://doi.org/10.1054/FIPR.2000.0041","url":null,"abstract":"Abstract Objective: To evaluate the effect of thrombomodulin on thrombin-mediated neutralization of plasminogen activator inhibitor 1 (PAl-1) activity which results in the enhancement of the fibrinolytic activity. Design: We studied the effect of recombinant human soluble TM (rhs TM) on the interaction between human thrombin and PAI-1. Its subsequent effect on tissue plasminogen activator (tPA)-induced lysis of PAl-1 enriched fibrin clot was also evaluated. Results: rhsTM abolished the high molecular weight complex formation between thrombin and PAl-1 and quenched the neutralization of PAl-1 activity by thrombin in a dose-dependent manner. rhsTM also caused dose-dependent inhibition of tPA-induced lysis of PAl-1 enriched fibrin clots in a purified system, which had been shown to be accelerated by increasing concentration of thrombin by neutralizing PAl-1 activity. This inhibition was not observed when PAl-1 was not present in the fibrin clot. Euglobulin clot lysis time (ECLT), which is determined by the balance between tPA and PAl-1, was prolonged by rhsTM. This prolongation was partially abolished by anti-PAl-1 polyclonal IgG, but was unaffected by potato carboxyl peptidase inhibitor. Conclusion: The inhibition of thrombin-dependent enhancement of fibrinolysis by TM appears to involve a mechanism of quenching of thrombin-mediated neutralization of PAl-1 activity which is independent of thrombin activatable fibrinolysis inhibitor (TAFl).","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"90 1","pages":"264-271"},"PeriodicalIF":0.0,"publicationDate":"1999-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91527000","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 4

Immunohistochemical analysis of the plasminogen activation system and the matrix metalloproteinases in normal and atherosclerotic human vessels 正常和动脉粥样硬化人血管中纤溶酶原激活系统和基质金属蛋白酶的免疫组织化学分析

Fibrinolysis and Proteolysis Pub Date : 1999-11-01 DOI: 10.1054/fipr.1999.0044

M.J. Wijnberg, J. Slomp, J.H. Verheijen

{"title":"Immunohistochemical analysis of the plasminogen activation system and the matrix metalloproteinases in normal and atherosclerotic human vessels","authors":"M.J. Wijnberg, J. Slomp, J.H. Verheijen","doi":"10.1054/fipr.1999.0044","DOIUrl":"https://doi.org/10.1054/fipr.1999.0044","url":null,"abstract":"<div><p>In this study we examined the localization of the plasminogen activation system and the matrix metalloproteinases in normal human arteries, arteries with diffuse intimal thickenings and atherosclerotic arteries. We found that MMP-1, MMP-2, MMP-3, TIMP-1 and TIMP-2 did not stain differently in normal arteries, arteries with intimal thickening and atherosclerotic arteries. MMP-9 staining was, however, increased in atherosclerotic arteries as compared to normal arteries and arteries with diffuse intimal thickening. For u-PA there were no differences between normal arteries, arteries with intimal thickening and atherosclerotic arteries. t-PA staining was decreased in the media of atherosclerotic arteries as compared to both normal and intima-thickened arteries. In contrast, PAI-1 staining was elevated in the intima of atherosclerotic arteries as compared to the media. While u-PAR was elevated in the intima of arteries with intimal thickening, staining was weaker in the intima of atherosclerotic arteries, as compared to the intima of normal arteries. These results suggest that both the plasminogen activation system and the MMP system might be involved in the process of atherosclerosis most likely in different steps and stages in this process.</p></div>","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"13 6","pages":"Pages 252-258"},"PeriodicalIF":0.0,"publicationDate":"1999-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1054/fipr.1999.0044","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71824432","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 2

Soluble thrombomodulin quenches thrombin-mediated neutralization of PAI-1 activity and inhibits fibrinolysis through a TAFI independent mechanism 可溶性血栓调节蛋白通过TAFI独立机制抑制凝血酶介导的PAI-1活性中和和纤维蛋白溶解

Fibrinolysis and Proteolysis Pub Date : 1999-11-01 DOI: 10.1054/fipr.2000.0041

T. Urano , H. Ihara , Y. Suzuki , N. Nagai , Y. Takada , A. Takada

{"title":"Soluble thrombomodulin quenches thrombin-mediated neutralization of PAI-1 activity and inhibits fibrinolysis through a TAFI independent mechanism","authors":"T. Urano , H. Ihara , Y. Suzuki , N. Nagai , Y. Takada , A. Takada","doi":"10.1054/fipr.2000.0041","DOIUrl":"https://doi.org/10.1054/fipr.2000.0041","url":null,"abstract":"<div><p><em>Objective:</em> To evaluate the effect of thrombomodulin on thrombin-mediated neutralization of plasminogen activator inhibitor 1 (PAl-1) activity which results in the enhancement of the fibrinolytic activity.</p><p><em>Design:</em> We studied the effect of recombinant human soluble TM (rhs TM) on the interaction between human thrombin and PAI-1. Its subsequent effect on tissue plasminogen activator (tPA)-induced lysis of PAl-1 enriched fibrin clot was also evaluated.</p><p><em>Results:</em> rhsTM abolished the high molecular weight complex formation between thrombin and PAl-1 and quenched the neutralization of PAl-1 activity by thrombin in a dose-dependent manner. rhsTM also caused dose-dependent inhibition of tPA-induced lysis of PAl-1 enriched fibrin clots in a purified system, which had been shown to be accelerated by increasing concentration of thrombin by neutralizing PAl-1 activity. This inhibition was not observed when PAl-1 was not present in the fibrin clot. Euglobulin clot lysis time (ECLT), which is determined by the balance between tPA and PAl-1, was prolonged by rhsTM. This prolongation was partially abolished by anti-PAl-1 polyclonal IgG, but was unaffected by potato carboxyl peptidase inhibitor.</p><p><em>Conclusion:</em> The inhibition of thrombin-dependent enhancement of fibrinolysis by TM appears to involve a mechanism of quenching of thrombin-mediated neutralization of PAl-1 activity which is independent of thrombin activatable fibrinolysis inhibitor (TAFl).</p></div>","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"13 6","pages":"Pages 264-271"},"PeriodicalIF":0.0,"publicationDate":"1999-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1054/fipr.2000.0041","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71824201","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 4

Immunohistochemical analysis of the plasminogen activation system and the matrix metalloproteinases in normal and atherosclerotic human vessels 正常和动脉粥样硬化人血管中纤溶酶原激活系统和基质金属蛋白酶的免疫组织化学分析

Fibrinolysis and Proteolysis Pub Date : 1999-11-01 DOI: 10.1054/FIPR.1999.0044

M. Wijnberg, J. Slomp, J. Verheijen

{"title":"Immunohistochemical analysis of the plasminogen activation system and the matrix metalloproteinases in normal and atherosclerotic human vessels","authors":"M. Wijnberg, J. Slomp, J. Verheijen","doi":"10.1054/FIPR.1999.0044","DOIUrl":"https://doi.org/10.1054/FIPR.1999.0044","url":null,"abstract":"In this study we examined the localization of the plasminogen activation system and the matrix metalloproteinases in normal human arteries, arteries with diffuse intimal thickenings and atherosclerotic arteries. We found that MMP-1, MMP-2, MMP-3, TIMP-1 and TIMP-2 did not stain differently in normal arteries, arteries with intimal thickening and atherosclerotic arteries. MMP- 9 staining was, however, increased in atherosclerotic arteries as compared to normal arteries and arteries with diffuse intimal thickening. For u-PA there were no differences between normal arteries, arteries with intimal thickening and atherosclerotic arteries, t-PA staining was decreased in the media of atherosclerotic arteries as compared to both normal and intima-thickened arteries. In contrast, PAI-1 staining was elevated in the intima of atherosclerotic arteries as compared to the media. While u-PAR was elevated in the intima of arteries with intimal thickening, staining was weaker in the intima of atherosclerotic arteries, as compared to the intima of normal arteries. These results suggest that both the plasminogen activation system and the MMP system might be involved in the process of atherosclerosis most likely in different steps and stages in this process. (C) 1999 Harcourt Publishers Ltd.","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"259 ","pages":"252-258"},"PeriodicalIF":0.0,"publicationDate":"1999-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91466147","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 2

Regulation of cancer invasion and vascularization by plasminogen activator inhibitor-1 纤溶酶原激活物抑制剂-1对肿瘤侵袭和血管形成的调控

Fibrinolysis and Proteolysis Pub Date : 1999-11-01 DOI: 10.1054/FIPR.2000.0043

A. Noël, K. Bajou, V. Masson, L. Devy, F. Frankenne, J. Rakic, V. Lambert, P. Carmeliet, J. Foidart

引用次数: 18

A link between integrins and MMPs in angiogenesis 血管生成中整合素和MMPs之间的联系

Fibrinolysis and Proteolysis Pub Date : 1999-11-01 DOI: 10.1054/fipr.2000.0042

S. Silletti, D.A. Cheresh

引用次数: 14

Pro-inflammatory effect of oestrogens 雌激素的促炎作用

Fibrinolysis and Proteolysis Pub Date : 1999-11-01 DOI: 10.1054/fipr.2000.0045

C. Kluft

引用次数: 4

Prothrombin promotes the invasiveness of melanoma cells by a different mechanism from thrombin 凝血酶原促进黑色素瘤细胞侵袭的机制与凝血酶不同

Fibrinolysis and Proteolysis Pub Date : 1999-11-01 DOI: 10.1054/fipr.2000.0040

H. Zhou , E.C. Gabazza , T. Sano , Y. Adachi , K. Suzuki

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引用次数: 3