Fibrinolysis and Proteolysis最新文献

{"title":"Plasma granulocyte elastase levels and its relation to D-dimer in liver cirrhosis","authors":"K. Song, Hong Kyung Kim, Hyon-Suk Kim, Jyewon Song","doi":"10.1054/FIPR.2000.0080","DOIUrl":"https://doi.org/10.1054/FIPR.2000.0080","url":null,"abstract":"Abstract Objective: Do plasma granulocyte elastase levels in liver cirrhosis influence D-dimer levels? Setting: University Hospital. Materials: We investigated plasma granulocyte elastase levels in 65 patients with liver cirrhosis and related it to D-dimer levels determined by enzyme linked immunoassay. Granulocyte elastase was carried out by heterogenous enzyme immunoassay using polymorphonuclear Elastase kit (Diagnostica Merck, Darmstadt, Germany). Results: The mean plasma levels of elastase (175.4 μg/l) and D-dimer (2732.7 μg/l) were significantly increased in patients with cirrhosis as compared to levels of normal subjects (elastase: 22 μg/l; D-dimer: 276 μg/l). There was no significant difference of elastase levels among Child classes ( P =0.010) and etiology of cirrhosis ( P =0.007). D-dimer levels were significantly different among different Child groups ( P =0.020). Plasma elastase levels were positively correlated with D-dimer levels (r=0.437, P Conclusions: We have demonstrated a marked increase of granulocyte elastase and its relation to plasma D-dimer levels in patients with cirrhosis. This findings suggest that accelerated fibrinolysis in cirrhosis may be associated with cellular neutrophil activation and elevated granulocyte elastase level may be partially responsible for elevated D-dimer in cirrhosis.","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"20 1","pages":"300-304"},"PeriodicalIF":0.0,"publicationDate":"2000-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89866617","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":"Atomic force microscopy of fibrin networks and plasma clots during fibrinolysis","authors":"A. Blinc, J. Magdić, J. Frič, I. Muševič","doi":"10.1054/FIPR.2000.0085","DOIUrl":"https://doi.org/10.1054/FIPR.2000.0085","url":null,"abstract":"Abstract We have used atomic force microscopy (AFM) in order to study the ultrastructure of fibrin fibre dissolution in real time. Thin purified fibrin gels and plasma clots were prepared on glass surfaces and overlaid with isotonic saline or heparinized plasma in an AFM fluid-cell. Fibrinolysis was initiated by introducing plasmin or recombinant tissue-type plasminogen activator (rt-PA) into the solution bathing the clots. Microscopy was performed serially in real time on the Nanoscope III Atomic Force Microscope operating in the tapping or contact mode. The acquisition time for a single image was 2–8 min and the clots were imaged for up to 1 h with fields of view ranging from 128 × 128 μm to 0.7 × 0.7 μm with a resolution of 512 × 512 pixels. In the smallest fields of view fibrin fibres were seen to be composed of globules 40–70 nm in diameter. The diameter of composite fibrin fibres in purified gels depended on the concentration of NaCl in the fibrinogen solution: 250 ± 155 nm in 150 mmol/l NaCl vs. 1.42 ± 0.19 μm in 50 mmol/l NaCl. Plasma clots were composed of thick fibres with interspersed thinner fibres. In clots from platelet-rich plasma both the thick and the thin fibres had significantly smaller diameters than the corresponding fibre types in clots from platelet-depleted plasma (620 ± 195 nm vs. 965 ± 200 nm, and 195 ± 30 nm vs. 260 ± 60 nm, P","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"13 1","pages":"288-299"},"PeriodicalIF":0.0,"publicationDate":"2000-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81984646","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":"Plasma granulocyte elastase levels and its relation to D-dimer in liver cirrhosis","authors":"K.S. Song,&nbsp;H.K. Kim,&nbsp;H.S. Kim,&nbsp;J.W. Song","doi":"10.1054/fipr.2000.0080","DOIUrl":"https://doi.org/10.1054/fipr.2000.0080","url":null,"abstract":"<div><p><em>Objective:</em> Do plasma granulocyte elastase levels in liver cirrhosis influence D-dimer levels?</p><p><em>Setting:</em> University Hospital.</p><p><em>Materials:</em> We investigated plasma granulocyte elastase levels in 65 patients with liver cirrhosis and related it to D-dimer levels determined by enzyme linked immunoassay. Granulocyte elastase was carried out by heterogenous enzyme immunoassay using polymorphonuclear Elastase kit (Diagnostica Merck, Darmstadt, Germany).</p><p><em>Results:</em> The mean plasma levels of elastase (175.4 μg/l) and D-dimer (2732.7 μg/l) were significantly increased in patients with cirrhosis as compared to levels of normal subjects (elastase: 22 μg/l; D-dimer: 276 μg/l). There was no significant difference of elastase levels among Child classes (<em>P</em> =0.010) and etiology of cirrhosis (<em>P</em> =0.007). D-dimer levels were significantly different among different Child groups (<em>P</em> =0.020). Plasma elastase levels were positively correlated with D-dimer levels (r=0.437, <em>P</em>&lt; 0.001).</p><p><em>Conclusions:</em> We have demonstrated a marked increase of granulocyte elastase and its relation to plasma D-dimer levels in patients with cirrhosis. This findings suggest that accelerated fibrinolysis in cirrhosis may be associated with cellular neutrophil activation and elevated granulocyte elastase level may be partially responsible for elevated D-dimer in cirrhosis.</p></div>","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"14 5","pages":"Pages 300-304"},"PeriodicalIF":0.0,"publicationDate":"2000-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1054/fipr.2000.0080","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71828585","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":"Age-dependency in molecular markers of haemostasis, fibrinolysis and in soluble adhesion molecules","authors":"S. Szabo,&nbsp;C. Kastner,&nbsp;E. Büttcher,&nbsp;R. Ehlers,&nbsp;S. Kazmaier,&nbsp;U. Helber,&nbsp;M. Pfohl,&nbsp;H.M. Hoffmeister","doi":"10.1054/fipr.2000.0082","DOIUrl":"https://doi.org/10.1054/fipr.2000.0082","url":null,"abstract":"<div><p><em>Objective</em>: Elevation of several molecular markers of the haemostatic/fibrinolytic system and of soluble adhesion molecules has been associated with acute or chronic phases of atherosclerosis. Speculating that markers associated with atherosclerosis would increase with age, we determined the age-dependency of some of these markers in clinically healthy individuals.</p><p><em>Methods</em>: 129 healthy persons were enrolled [division: younger (≤34 years)/older group (&gt;34 years)]. Tissue-type plasminogen activator (t-PA) concentration, plasmin/α2-antiplasmin complex (PAP), D-dimer (DD), prothrombin fragment F1+2 (F1+2), thrombin-antithrombin III complex (TAT), soluble (sICAM-1) intercellular adhesion molecule-1, soluble (sVCAM-1) vascular cell adhesion molecule-1 and sP-selectin were measured with enzyme-linked immuno assays, plasminogen activator inhibitor-1 (PAI-1), plasma kallikrein-like activity (KK), and factor XII (FXII) with chromogenic substrate tests, fibrinogen with the Clauss method.</p><p><em>Results</em>: Fibrinogen (P &lt; 0.01), F1+2 (P&lt;0.01), KK (P&lt;0.05) were significantly higher in the older vs. the younger group and correlated significantly with age (P&lt;0.05, P&lt;0.01). DD showed significantly higher values in the older vs. the younger group, whereas T-PA, PAP, FXII, TAT did not. PAI-1 tended towards higher values in the older vs. the younger persons. T-PA, PAI-1, DD correlated significantly with age P-selectin, sICAM-1, sVCAM-1 did not differ between both groups, nor could a significant age-dependency be found.</p><p><em>Conclusion</em>: This study indicates that plasma levels of several molecular markers of the haemostatic and fibrinolytic system increase with age. The age-dependency of these markers has to be taken into account in respect to their clinical use in order to characterize patients with suspected risk of atherosclerotic events.</p></div>","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"14 5","pages":"Pages 281-287"},"PeriodicalIF":0.0,"publicationDate":"2000-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1054/fipr.2000.0082","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71828140","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":"Fibrinolytic parameters in young adults: the Floren-teen (Florence Teenager) Study","authors":"D. Prisco, S. Fedi, T. Brunelli, L. Chiarugi, R. Gianni, E. Santoro, C. Cappelletti, G. Pepe, G. Gensini, R. Abbate","doi":"10.1054/FIPR.2000.0084","DOIUrl":"https://doi.org/10.1054/FIPR.2000.0084","url":null,"abstract":"Abstract Objective : Determination of fibrinolytic parameters in young adults. Design : Students from a high school of Florence were involved in a longitudinal 5-year study of Preventive Medicine and Education Program. Setting : Istituto Clinica Medica Generale e Cardiologia, University of Florence, and Nuovo Ospedale San Giovanni di Dio, Florence, Italy. Subjects : 144 healthy students (59 males and 85 females) aged 17–19 years. Interventions : Venous blood withdrawal on fasting subjects, after 30 min of resting. Main outcome measures : Euglobulin lysis time (ELT) was measured on acidified plasma. PAI activity (PAI ag) was measured by chromogenic method. PAI-1 antigen (PAI-1 ag) and t-PA ( 1 - 2 I-1PA ag) antigen were measured by enzyme-linked immunosorbent assays (ELISA). Lipid analysis was performed by enzymatic assays. Results : We observed sex-related differences for ELT, which was shorter in males, and PAI-1 ag and t-PA ag levels which were significantly higher in males. No differences in the various parameters were observed according to smoking habits, alcohol consumption or practice of leisure physical activity. A correlation was found between ELT and lipid parameters. PAI-1 ag was correlated to weight, BMI, arterial blood pressure, and lipid parameters. PAI ac was directly related to blood pressure only in females. t-PA ag was correlated to arterial blood pressure and lipid parameters. Direct correlations were observed among ELT, PAI ac, PAI-1 ag, and t-PA ag. Conclusion : The influence of classical risk factors on fibrinolysis-related risk factors takes place early in life.","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"8 1","pages":"275-280"},"PeriodicalIF":0.0,"publicationDate":"2000-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82303062","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":"Fibrinolytic parameters in young adults: the Floren-teen (Florence Teenager) Study","authors":"D. Prisco ,&nbsp;S. Fedi ,&nbsp;T. Brunelli ,&nbsp;L. Chiarugi ,&nbsp;R. Gianni ,&nbsp;E. Santoro ,&nbsp;C. Cappelletti ,&nbsp;G. Pepe ,&nbsp;G.F. Gensini ,&nbsp;R. Abbate","doi":"10.1054/fipr.2000.0084","DOIUrl":"https://doi.org/10.1054/fipr.2000.0084","url":null,"abstract":"<div><p><em>Objective</em>: Determination of fibrinolytic parameters in young adults.</p><p><em>Design</em>: Students from a high school of Florence were involved in a longitudinal 5-year study of Preventive Medicine and Education Program.</p><p><em>Setting</em>: Istituto Clinica Medica Generale e Cardiologia, University of Florence, and Nuovo Ospedale San Giovanni di Dio, Florence, Italy.</p><p><em>Subjects</em>: 144 healthy students (59 males and 85 females) aged 17–19 years.</p><p><em>Interventions</em>: Venous blood withdrawal on fasting subjects, after 30 min of resting.</p><p><em>Main outcome measures</em>: Euglobulin lysis time (ELT) was measured on acidified plasma. PAI activity (PAI ag) was measured by chromogenic method. PAI-1 antigen (PAI-1 ag) and t-PA (¹-₂I-1PA ag) antigen were measured by enzyme-linked immunosorbent assays (ELISA). Lipid analysis was performed by enzymatic assays.</p><p><em>Results</em>: We observed sex-related differences for ELT, which was shorter in males, and PAI-1 ag and t-PA ag levels which were significantly higher in males. No differences in the various parameters were observed according to smoking habits, alcohol consumption or practice of leisure physical activity. A correlation was found between ELT and lipid parameters. PAI-1 ag was correlated to weight, BMI, arterial blood pressure, and lipid parameters. PAI ac was directly related to blood pressure only in females. t-PA ag was correlated to arterial blood pressure and lipid parameters. Direct correlations were observed among ELT, PAI ac, PAI-1 ag, and t-PA ag.</p><p><em>Conclusion</em>: The influence of classical risk factors on fibrinolysis-related risk factors takes place early in life.</p></div>","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"14 5","pages":"Pages 275-280"},"PeriodicalIF":0.0,"publicationDate":"2000-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1054/fipr.2000.0084","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71828139","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":"Vascular and cellular proteolytic activity in mice with α2-antiplasmin gene inactivation","authors":"H. Lijnen, F. Ugwu, E. Maquoi, G. Lemmens, B. Hoef, M. Dewerchin, D. Collen","doi":"10.1054/FIPR.2000.0088","DOIUrl":"https://doi.org/10.1054/FIPR.2000.0088","url":null,"abstract":"Abstract Objective: To study the role of α2-antiplasmin (α2-AP), the main physiological plasmin inhibitor, in controlling vascular and cellular proteolytic activity. Materials: Arteries, organs and cell cultures derived from α2-AP-deficient (α2-AP–/–) mice or from their wild-type littermates (α2-AP+/+). Results: In serum-free conditioned medium of α2-AP+/+or α2-AP–/–skin fibroblasts, the time course (0–72 h) of PAI-1 antigen and of t-PA or u-PA antigen and activity production was similar. Activation of proMMP-9 (gelatinase B) upon addition of plasmin(ogen) to serum-free conditioned medium of fibroblasts was consistently detectable with α2-AP–/–but not with α2-AP+/+cells. In aorta and femoral arterial extracts of α2-AP+/+or α2-AP–/–mice, t-PA and u-PA activity levels were comparable, and fibrin zymography with cryosections did not reveal significant differences in fibrinolytic activity. In liver or kidney extracts of α2-AP+/+or α2-AP–/–mice, t-PA, u-PA, PAI-1 and plasminogen antigen levels were comparable; t-PA or u-PA activity was not detected in liver extracts and was present at comparable levels in kidney extracts. Activation of plasminogen to plasmin in solution by cell-associated plasminogen activator, and activation of cell-bound plasminogen by tcu-PA was comparable for fibroblasts of both genotypes. Conclusions: α2-AP does not play a crucial role in controlling vascular or cellular proteolytic activity in mice.","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"33 1","pages":"322-326"},"PeriodicalIF":0.0,"publicationDate":"2000-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90081735","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":"Atomic force microscopy of fibrin networks and plasma clots during fibrinolysis","authors":"A. Blinc ,&nbsp;J. Magdic ,&nbsp;J. Fric ,&nbsp;I. Musevic","doi":"10.1054/fipr.2000.0085","DOIUrl":"https://doi.org/10.1054/fipr.2000.0085","url":null,"abstract":"<div><p>We have used atomic force microscopy (AFM) in order to study the ultrastructure of fibrin fibre dissolution in real time. Thin purified fibrin gels and plasma clots were prepared on glass surfaces and overlaid with isotonic saline or heparinized plasma in an AFM fluid-cell. Fibrinolysis was initiated by introducing plasmin or recombinant tissue-type plasminogen activator (rt-PA) into the solution bathing the clots. Microscopy was performed serially in real time on the Nanoscope III Atomic Force Microscope operating in the tapping or contact mode. The acquisition time for a single image was 2–8 min and the clots were imaged for up to 1 h with fields of view ranging from 128 × 128 μm to 0.7 × 0.7 μm with a resolution of 512 × 512 pixels. In the smallest fields of view fibrin fibres were seen to be composed of globules 40–70 nm in diameter. The diameter of composite fibrin fibres in purified gels depended on the concentration of NaCl in the fibrinogen solution: 250 ± 155 nm in 150 mmol/l NaCl vs. 1.42 ± 0.19 μm in 50 mmol/l NaCl. Plasma clots were composed of thick fibres with interspersed thinner fibres. In clots from platelet-rich plasma both the thick and the thin fibres had significantly smaller diameters than the corresponding fibre types in clots from platelet-depleted plasma (620 ± 195 nm vs. 965 ± 200 nm, and 195 ± 30 nm vs. 260 ± 60 nm, <em>P</em>&lt; 0.001 for both comparisons). Fibrinolysis of both thick and thin fibres proceeded predominantly by lateral section of the whole fibre thickness at a given site, regardless of whether it was initiated by plasmin or by rt-PA. The time to complete fibre section by 2.5 U/ml of plasmin did not differ between thin and thick fibrin fibres (7.6 ± 3.7 min vs. 6.4 ± 4.2 min). With a low concentration of plasmin (0.17 U/ml) some fibrin fibres became thinner along their entire observed length before they were cleaved. The rate of fibre thinning was 3-times faster in the thicker fibres than in the thinner ones. We conclude that the ‘cut-through’ pattern is the predominant way of fibrinolysis in purified gels and in plasma clots, and that proteolysis leading towards fibre cleavage proceeds more efficiently in thick than in thin composite fibrin fibres.</p></div>","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"14 5","pages":"Pages 288-299"},"PeriodicalIF":0.0,"publicationDate":"2000-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1054/fipr.2000.0085","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71828141","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":"Vascular and cellular proteolytic activity in mice with α2-antiplasmin gene inactivation","authors":"H.R. Lijnen ,&nbsp;F. Ugwu ,&nbsp;E. Maquoi ,&nbsp;G. Lemmens ,&nbsp;B.Van Hoef ,&nbsp;M. Dewerchin ,&nbsp;D. Collen","doi":"10.1054/fipr.2000.0088","DOIUrl":"https://doi.org/10.1054/fipr.2000.0088","url":null,"abstract":"<div><p><em>Objective</em>: To study the role of α₂-antiplasmin (α₂-AP), the main physiological plasmin inhibitor, in controlling vascular and cellular proteolytic activity.</p><p><em>Materials:</em> Arteries, organs and cell cultures derived from α₂-AP-deficient (α₂-AP^–/–) mice or from their wild-type littermates (α₂-AP^+/+).</p><p><em>Results</em>: In serum-free conditioned medium of α₂-AP^+/+or α₂-AP^–/–skin fibroblasts, the time course (0–72 h) of PAI-1 antigen and of t-PA or u-PA antigen and activity production was similar. Activation of proMMP-9 (gelatinase B) upon addition of plasmin(ogen) to serum-free conditioned medium of fibroblasts was consistently detectable with α₂-AP^–/–but not with α₂-AP^+/+cells. In aorta and femoral arterial extracts of α₂-AP^+/+or α₂-AP^–/–mice, t-PA and u-PA activity levels were comparable, and fibrin zymography with cryosections did not reveal significant differences in fibrinolytic activity. In liver or kidney extracts of α₂-AP^+/+or α₂-AP^–/–mice, t-PA, u-PA, PAI-1 and plasminogen antigen levels were comparable; t-PA or u-PA activity was not detected in liver extracts and was present at comparable levels in kidney extracts.</p><p>Activation of plasminogen to plasmin in solution by cell-associated plasminogen activator, and activation of cell-bound plasminogen by tcu-PA was comparable for fibroblasts of both genotypes.</p><p><em>Conclusions</em>: α₂-AP does not play a crucial role in controlling vascular or cellular proteolytic activity in mice.</p></div>","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"14 5","pages":"Pages 322-326"},"PeriodicalIF":0.0,"publicationDate":"2000-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1054/fipr.2000.0088","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71828588","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":"Age-dependency in molecular markers of haemostasis, fibrinolysis and in soluble adhesion molecules","authors":"S. Szabo, C. Kastner, E. Büttcher, R. Ehlers, S. Kazmaier, U. Helber, M. Pfohl, H. Hoffmeister","doi":"10.1054/FIPR.2000.0082","DOIUrl":"https://doi.org/10.1054/FIPR.2000.0082","url":null,"abstract":"Objective: Elevation of several molecular markers of the haemostatic/fibrinolytic system and of soluble adhesion molecules has been associated with acute or chronic phases of atherosclerosis. Speculating that markers associated with atherosclerosis would increase with age, we determined the age-dependency of some of these markers in clinically healthy individuals. \u0000 \u0000Methods: 129 healthy persons were enrolled [division: younger (≤34 years)/older group (>34 years)]. Tissue-type plasminogen activator (t-PA) concentration, plasmin/α2-antiplasmin complex (PAP), D-dimer (DD), prothrombin fragment F1+2 (F1+2), thrombin-antithrombin III complex (TAT), soluble (sICAM-1) intercellular adhesion molecule-1, soluble (sVCAM-1) vascular cell adhesion molecule-1 and sP-selectin were measured with enzyme-linked immuno assays, plasminogen activator inhibitor-1 (PAI-1), plasma kallikrein-like activity (KK), and factor XII (FXII) with chromogenic substrate tests, fibrinogen with the Clauss method. \u0000 \u0000Results: Fibrinogen (P < 0.01), F1+2 (P<0.01), KK (P<0.05) were significantly higher in the older vs. the younger group and correlated significantly with age (P<0.05, P<0.01). DD showed significantly higher values in the older vs. the younger group, whereas T-PA, PAP, FXII, TAT did not. PAI-1 tended towards higher values in the older vs. the younger persons. T-PA, PAI-1, DD correlated significantly with age P-selectin, sICAM-1, sVCAM-1 did not differ between both groups, nor could a significant age-dependency be found. \u0000 \u0000Conclusion: This study indicates that plasma levels of several molecular markers of the haemostatic and fibrinolytic system increase with age. The age-dependency of these markers has to be taken into account in respect to their clinical use in order to characterize patients with suspected risk of atherosclerotic events.","PeriodicalId":100526,"journal":{"name":"Fibrinolysis and Proteolysis","volume":"4 1","pages":"281-287"},"PeriodicalIF":0.0,"publicationDate":"2000-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78308171","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}