Fibrinolysis and Proteolysis最新文献

{"title":"Effect of thrombomodulin on plasminogen activation","authors":"H.-S. Han ,&nbsp;H.-L. Wu ,&nbsp;B.-T. Lin ,&nbsp;C.-S. Shi ,&nbsp;G.-Y. Shi","doi":"10.1054/fipr.2000.0059","DOIUrl":"https://doi.org/10.1054/fipr.2000.0059","url":null,"abstract":"<div><p>Thrombomodulin (TM), a thrombin receptor on the endothelial cell surface, plays an important role in the regulation of blood coagulation. In this study, recombinant TM containing six epidermal growth factor-like structures (D2), and serine and threonine (Ser/Thr)-rich domain (D3), TMD23 (corresponding to Ala224-Ser497), was prepared by a recombinant baculovirus expression system and purified to apparent homogeneity by DEAE-Sepharose CL-6B and affinity nickel-chelating column chromatographies. TMD23 in combination with thrombin could effectively activate protein C. TMD23 alone could enhance Glu-plasminogen activation by single-chain urokinase-type plasminogen activator in a dose-dependent manner. The specific binding of plasminogen to TMD23 was also demonstrated and the binding was inhibited by ε-aminocaproic acid. In conclusion, our results suggest that TMD23 could specifically bind to plasminogen and effectively enhance plasminogen activation.</p></div>","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"14 4","pages":"Pages 221-228"},"PeriodicalIF":0.0,"publicationDate":"2000-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1054/fipr.2000.0059","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71825984","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}

{"title":"Effect of thrombomodulin on plasminogen activation","authors":"Huai-Song Han, H.-L. Wu, B.-T. Lin, C.-S. Shi, G. Shi","doi":"10.1054/FIPR.2000.0059","DOIUrl":"https://doi.org/10.1054/FIPR.2000.0059","url":null,"abstract":"Abstract Thrombomodulin (TM), a thrombin receptor on the endothelial cell surface, plays an important role in the regulation of blood coagulation. In this study, recombinant TM containing six epidermal growth factor-like structures (D2), and serine and threonine (Ser/Thr)-rich domain (D3), TMD23 (corresponding to Ala224-Ser497), was prepared by a recombinant baculovirus expression system and purified to apparent homogeneity by DEAE-Sepharose CL-6B and affinity nickel-chelating column chromatographies. TMD23 in combination with thrombin could effectively activate protein C. TMD23 alone could enhance Glu-plasminogen activation by single-chain urokinase-type plasminogen activator in a dose-dependent manner. The specific binding of plasminogen to TMD23 was also demonstrated and the binding was inhibited by e-aminocaproic acid. In conclusion, our results suggest that TMD23 could specifically bind to plasminogen and effectively enhance plasminogen activation.","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"184 1","pages":"221-228"},"PeriodicalIF":0.0,"publicationDate":"2000-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80488180","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}

{"title":"Upregulation of MMP-2 by all-trans retinoic acid is mediated by TGF- β 1 in cultured rat mesangial cell","authors":"Wensheng Lin, N. Zhang, S. Zhang, J. Gu, M. Guo","doi":"10.1054/FIPR.2000.0066","DOIUrl":"https://doi.org/10.1054/FIPR.2000.0066","url":null,"abstract":"Abstract Matrix metalloproteinase-2 (MMP-2) degrades basement membrane collagen and its abnormal expression is associated with glomerulonephritis and glomerulosclerosis. All-trans retinoic acid (ATRA) has been indicated as preventing age-related glomerulosclerosis. The results of our study showed that ATRA upregulated expression of MMP-2 mRNA and secretion of MMP-2 proteins, and increased enzymatic activity of MMP-2 in cultured mesangial cell. In addition, ATRA also caused a dose-dependent increase in the secretion of transforming growth factor-β (TGF-β1) peptides. Since TGF-β1 regulated the expression of MMP-2 in mesangial cell, it is possible that TGF-β1 is involved in ATRA-induced MMP-2 expression. Using antisense TGF-β1 RNA strategy, antisense TGF-β1 construct almost completely blocked secretion of active TGF-β1 peptides in the antisense-bearing transfectants. Northern blot analysis showed that the transfectants treated with 10–6M ATRA for 72 h neither increased nor decreased the levels of MMP-2 messenger ribonucleic acid (mRNA). Moreover, addition of anti-TGF-β1 antibodies to mesangial cell in the presence of 10–6M ATRA reduced ATRA-induced MMP-2 expression dose dependently. These data suggest that TGF-β1 might be involved in ATRA-induced MMP-2 expression.","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"44 2 1","pages":"235-241"},"PeriodicalIF":0.0,"publicationDate":"2000-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85316069","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}

{"title":"An increased thrombin generation is detectable for at least 1 week following elective percutaneous transluminal coronary angioplasty","authors":"D. Prisco ,&nbsp;E. Antonucci ,&nbsp;M. Capanni ,&nbsp;L. Chiarugi ,&nbsp;V. Boddi ,&nbsp;C. Giglioli ,&nbsp;M. Comeglio ,&nbsp;S. Fedi ,&nbsp;G.F. Gensini ,&nbsp;R. Abbate","doi":"10.1054/fipr.2000.0075","DOIUrl":"https://doi.org/10.1054/fipr.2000.0075","url":null,"abstract":"<div><p><em>Objective</em>: The present prospective study was planned to investigate: (1) how long the early haemostatic changes after PTCA last and (2) if some coagulation and/or fibrinolytic parameters assessed during the first month after PTCA may be predictive of subsequent clinical recurrence.</p><p><em>Setting</em>: Istituto di Clinica Medica Generale e Cardiologia, University of Florence, Florence, Italy.</p><p><em>Material and Methods</em>: In 72 patients undergoing PTCA fibrinogen, F1+2, TAT, D-dimer and ELT were evaluated before the procedure (T1) and 2 (T2), 7 (T7) and 30 days (T30) after PTCA; PAI-1 and t-PA were assessed before PTCA and after 7 and 30 days. Follow-up angiography was performed only in patients with recurrence of ischaemia or positive ergometric tests.</p><p><em>Results</em>: F1+2, TAT and fibrinogen were significantly increased at T2 (<em>P</em>&lt;0.005); after a week, F1+2 and fibrinogen were still significantly higher in comparison to baseline values (<em>P</em>&lt;0.005). At T30 these parameters showed significantly lower levels if compared to T1 (<em>P</em>&lt;0.005). Plasma D-dimer concentration significantly increased at T2 and T7 (<em>P</em>&lt;0.001), but no difference was found between baseline values and those at T30. PAI-1 activity significantly decreased at T7 (<em>P</em>&lt;0.001), whereas it was similar to baseline at T30. No significant variations of t-PA levels were observed at the different times. Finally, ELT significantly increased at T2 (<em>P</em>&lt;0.001), but at T7 and T30 the values were similar to baseline values. Clinical recurrence occurred in 19 patients. The values of various parameters investigated were not different at any time considered between the patients with and without subsequent clinical recurrence. Heparin treatment had no significant influence on thrombin generation at different times whereas it had marginal influences on fibrinogen, PAI-1 and t-PA antigen levels.</p><p><em>Conclusion</em>: A number of alterations in haemostasis takes place and persists 2 and 7 days after elective PTCA and heparin treatment is not able to blunt clotting activation. The haemostatic parameters assessed during the first month after PTCA seem not to be predictive of subsequent clinical recurrence.</p></div>","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"14 4","pages":"Pages 253-260"},"PeriodicalIF":0.0,"publicationDate":"2000-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1054/fipr.2000.0075","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71826466","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}

{"title":"Fibrin(ogen) degradation by a 24k-endopeptidase from a Chryseobacterium Sp.","authors":"H.R. Lijnen,&nbsp;B.Van Hoef,&nbsp;I. Roelants,&nbsp;D. Collen","doi":"10.1054/fipr.2000.0076","DOIUrl":"https://doi.org/10.1054/fipr.2000.0076","url":null,"abstract":"<div><p><strong>Summary</strong> A novel 24k-endopeptidase purified from the conditioned medium of a novel species of the <em>Chryseobacterium</em> genus, degraded purified fibrinogen and fibrin. At an enzyme/substrate ratio of 1/200 to 1/1000 rapid degradation of the human fibrinogen α-chain occurred and delayed degradation of the β-chain, whereas the γ-chain was more resistant. Degradation was associated with loss of thrombin-inducible coagulation. Incubation of 24k-endopeptidase (500 nM) in human plasma at 37°C for 3 h resulted in a decrease in fibrinogen to 38 ± 7% of baseline, and an increase of the thrombin time from 21 ± 1 to 52 ± 17 s. Other coagulation factors as well as plasminogen were not significantly affected. Fibrinogen digested with 24k-endopeptidase did not confer anticoagulant properties when added to human plasma.</p><p>In a buffer milieu,¹²⁵I-fibrin labelled matrix was lysed in a time- and concentration-dependent manner by 24k-endopeptidase. Purified¹²⁵I-labelled fibrin clots (65 μl) in a buffer milieu (500 μl) were also efficiently lysed, requiring 50 nM 24k-endopeptidase for 50% lysis in 1 h. The presence of a physiological fibrinogen concentration in this assay did not affect lysis. In contrast, no significant lysis of¹²⁵I-fibrin labelled plasma clots (65 μl) in human plasma (500 μl) was observed upon incubation with 24k-endopeptidase (up to 1 μM) for up to 24 h. Incubation of 24k-endopeptidase with α₂-macroglobulin resulted in formation of a complex with impaired proteolytic activity against fibrinogen. These findings indicate that 24k-endopeptidase may reduce plasma coagulability by degradation of fibrinogen and that its differential action on fibrin in a buffer milieu or in plasma may be due to inhibition by α₂-macroglobulin.</p></div>","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"14 4","pages":"Pages 247-252"},"PeriodicalIF":0.0,"publicationDate":"2000-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1054/fipr.2000.0076","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71826468","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}

{"title":"Overexpression of plasminogen activator inhibitor type-1 in HT-1080 fibrosarcoma cells promotes lung colonization and in vitro cell adhesion","authors":"V. Carroll, J. Mihály, Y. Koshelnick, P. Hufnagl, B. Binder","doi":"10.1054/FIPR.2000.0061","DOIUrl":"https://doi.org/10.1054/FIPR.2000.0061","url":null,"abstract":"Abstract Plasminogen activator inhibitor type 1 (PAI-1) is associated with tumour invasion, angiogenesis and metastatic spread. It is also a strong prognostic factor for relapse in a number of human cancers. This study was designed to investigate the effects of overexpression of PAI-1 on lung colonization by human HT-1080 fibrosarcoma cells. Full length PAI-1 cDNA was transfected in a non-aggressive HT-1080 clonal cell line (1–3C). Stable transfected clones were isolated of which one (3F52) secreted a 29-fold increase in PAI-1 protein levels (29.1±6.5 μg/10 6 cells/24 h) as compared with control mock transfected cells (1.0±0.2 μg/10 6 cells/24 h). 3F52 cells were significantly better able to form lung colonies after i.v. tail vein injection of athymic mice (mean number of colonies±SE 238±105) as compared with control cells (8±7). In addition, PAI-1 overexpressing cells were between 1.5 and 2.5 fold more adhesive to extracellular matrix membrane (ECM) proteins than mock transfected cells in an in vitro cell adhesion assay. These findings provide experimental support that PAI-1 facilitates tumour cell lodgement in vivo and adhesion of HT-1080 cells in vitro.","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"41 1","pages":"215-220"},"PeriodicalIF":0.0,"publicationDate":"2000-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74299616","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}

{"title":"Diabetes mellitus induces decreased plasma fibrinolytic activity and increased tissue synthesis of plasminogen activator inhibitor-1 (PAI-1) in the rat","authors":"A. Pandolfi, A. Giaccari, R. Polishuck, M. Alberta, G. Pellegrini, L. Morviducci, E. Vitacolonna, A. Buongiorno, F. Capani, A. Consoli","doi":"10.1054/FIPR.2000.0083","DOIUrl":"https://doi.org/10.1054/FIPR.2000.0083","url":null,"abstract":"Abstract In diabetes, plasma fibrinolytic activity is decreased while plasma plasminogen activator inhibitor-1 (PAI-1) is increased. Both liver and adipose tissue can synthesize and release PAI-1, but PAI-1 synthesis in these tissues has not been investigated in diabetes. Furthermore, little is known about PAI-1 localization in arterial wall cells of diabetic animals. The aim of this study was to determine the effect of chronic hyperglycemia on plasma fibrinolysis and plasma PAI-1 levels and on liver, adipose tissue and arterial wall PAI-1 content in the rat. We compared plasma fibrinolytic activity (lysis of fibrin plates) and plasma PAI-1 activity (chromogenic assay) in 10 Sprague Dowley 90% pancreatectomized rats (a model of diabetes characterized by normal fasting insulin and the absence of obesity, therefore closely resembling lean type 2 diabetes) and in 15 sham-operated rats. Furthermore, we measured PAI-1-related fluorescence, by immunofluorescent staining and Laser Scanning Confocal Microscopy, in liver, adipose tissue and aortic wall in diabetic and control animals. In the diabetic animals plasma fibrinolytic activity was reduced (lysis areas = 163 ± 23 vs 308 ± 21 mm2, P These data provide evidence that in diabetes mellitus hyperglycemia is associated with increased PAI-1 content in the liver, adipose tissue and in the arterial wall. This suggests that in diabetes the liver and adipose tissue can be important sources for increased plasma PAI-1 and local fibrinolysis can be affected by increased PAI-1 levels in the arterial wall.","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"27 1","pages":"261-267"},"PeriodicalIF":0.0,"publicationDate":"2000-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86888607","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}

{"title":"Controlled evaluation of fibrinolytic response to intraoperative pneumatic intermittent sequential compression of the lower extremities during laparoscopic cholecystectomy","authors":"W. Schwenk ,&nbsp;S. Ziemer ,&nbsp;J. Neudecker ,&nbsp;T. Kuntz ,&nbsp;J.M. Müller","doi":"10.1054/fipr.2000.0058","DOIUrl":"https://doi.org/10.1054/fipr.2000.0058","url":null,"abstract":"<div><p><em>Objective:</em> During a pneumoperitoneum intraoperative intermittent sequential pneumatic compression (ISC) neutralizes venous stasis in the lower extremities and may also have an influence on systemic fibrinolytic activity.</p><p><em>Design</em>: Controlled study to evaluate whether ISC stimulates intravascular fibrinolytic activity.</p><p><em>Setting</em>: University-Hospital.</p><p><em>Materials</em>: 26 patients underwent laparoscopic cholecystectomy with (+ISC, <em>n</em> = 10) or without (–ISC, <em>n</em> = 16) ISC.</p><p><em>Intervention</em>: Intraoperative intermittent sequential compression of the lower extremities.</p><p><em>Main outcome measures</em>: Major endpoint – postoperative plasma activity of tissue-plasminogen-activator (t-PA). Minor endpoints – postoperative plasminogen-activator-inhibitor-1 (PAl-1) activity, plasmin-antiplasmin-complex (PAP) concentration, concentration of total fibrin degradation products (TDP), and D-Dimer concentration.</p><p><em>Results</em>: There was no difference in age, sex, body mass index (BMI), and properative fibrinolytic activity between the groups. Postoperative t-PA-activity (<em>P</em> =0.3), PAI-1-activity (<em>P</em> =0.9), PAP- (<em>P</em> =0.5), TDP-(<em>P</em> =0.2), and D-Dimer-concentrations (<em>P</em> =0.1) were also not different between both groups.</p><p><em>Conclusion</em>: During laparoscopic cholecystectomy intraoperative ISC does not activate systemic intravascular fibrinolysis. Because of the positive hemodynamic effect of ISC during pneumoperitoneum, studies of the antithrombotic efficacy of this tool are needed in the setting of laparoscopic surgery.</p></div>","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"14 4","pages":"Pages 229-234"},"PeriodicalIF":0.0,"publicationDate":"2000-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1054/fipr.2000.0058","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71825988","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}

{"title":"Diabetes mellitus induces decreased plasma fibrinolytic activity and increased tissue synthesis of plasminogen activator inhibitor-1 (PAI-1) in the rat","authors":"A. Pandolfi ,&nbsp;A. Giaccari ,&nbsp;R. Polishuck ,&nbsp;M.M. Alberta ,&nbsp;G. Pellegrini ,&nbsp;L. Morviducci ,&nbsp;E. Vitacolonna ,&nbsp;A.M. Buongiorno ,&nbsp;F. Capani ,&nbsp;A. Consoli","doi":"10.1054/fipr.2000.0083","DOIUrl":"https://doi.org/10.1054/fipr.2000.0083","url":null,"abstract":"<div><p>In diabetes, plasma fibrinolytic activity is decreased while plasma plasminogen activator inhibitor-1 (PAI-1) is increased. Both liver and adipose tissue can synthesize and release PAI-1, but PAI-1 synthesis in these tissues has not been investigated in diabetes. Furthermore, little is known about PAI-1 localization in arterial wall cells of diabetic animals. The aim of this study was to determine the effect of chronic hyperglycemia on plasma fibrinolysis and plasma PAI-1 levels and on liver, adipose tissue and arterial wall PAI-1 content in the rat.</p><p>We compared plasma fibrinolytic activity (lysis of fibrin plates) and plasma PAI-1 activity (chromogenic assay) in 10 Sprague Dowley 90% pancreatectomized rats (a model of diabetes characterized by normal fasting insulin and the absence of obesity, therefore closely resembling lean type 2 diabetes) and in 15 sham-operated rats. Furthermore, we measured PAI-1-related fluorescence, by immunofluorescent staining and Laser Scanning Confocal Microscopy, in liver, adipose tissue and aortic wall in diabetic and control animals.</p><p>In the diabetic animals plasma fibrinolytic activity was reduced (lysis areas = 163 ± 23 vs 308 ± 21 mm², <em>P</em>&lt; 0.001), while plasma PAI-1 activity was increased (4.61 ± 2.01 AU vs 0.70 ± 0.59 AU, <em>P</em>&lt; 0.02). PAI-1 related fluorescence was increased in the liver (754 ± 25 vs 299 ± 14 AFU, <em>P</em>&lt; 0.0001), in the adipose tissue (721 ± 32 vs 248 ± 14 AFU, <em>P</em>&lt; 0.001) and in the aorta wall (339 ± 18 vs 274 ± 9 AFU,<em>P</em> &lt; 0.005) of the diabetic animals.</p><p>These data provide evidence that in diabetes mellitus hyperglycemia is associated with increased PAI-1 content in the liver, adipose tissue and in the arterial wall. This suggests that in diabetes the liver and adipose tissue can be important sources for increased plasma PAI-1 and local fibrinolysis can be affected by increased PAI-1 levels in the arterial wall.</p></div>","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"14 4","pages":"Pages 261-267"},"PeriodicalIF":0.0,"publicationDate":"2000-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1054/fipr.2000.0083","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71826467","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}

{"title":"Does albumin play a role in fibrinolysis by its inhibition of plasminogen activation?","authors":"M.G.M. de Sain-van der Velden ,&nbsp;H.C. Smolders ,&nbsp;H.J.M. van Rijn ,&nbsp;H.A.M. Voorbij","doi":"10.1054/fipr.2000.0067","DOIUrl":"https://doi.org/10.1054/fipr.2000.0067","url":null,"abstract":"<div><p>One of the clinical characteristics of patients with nephrotic syndrome is hypoalbuminemia. The mechanism underlying the susceptibility to thrombosis in this group of patients is not fully understood. The hypoalbuminemia may alter the structure of fibrin clots and affect clot lysis, thereby influencing the coagulolytic balance. In the present study, we investigated the effect of albumin on fibrinolysis. The effect of albumins from several manufacturers and recombinant albumin on the plasminogen activation were tested in an in vitro assay. A chromogenic substrate highly selective for plasmin was used to detect the generation of plasmin. This study revealed a dose-dependent inhibition of plasminogen activation by albumin in a concentration range between 12.5 g/L and 50 g/L. The percentage of inhibition at maximum plasmin activity was different for each albumin, varying from 23% to 90%. Pre-incubation of albumin with fibrinogen enhanced the inhibition, suggesting that by binding to fibrin(ogen) albumin may hinder the formation of the ternary complex and thereby interfere in the fibrinolytic process. This may have consequences for patients with nephrotic syndrome, whose low albumin levels may provide a mechanism partially compensating the well-known hypercoagulability.</p></div>","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"14 4","pages":"Pages 242-246"},"PeriodicalIF":0.0,"publicationDate":"2000-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1054/fipr.2000.0067","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71826464","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}