Raised Plasma Homocysteine: An Emerging Risk Factor for Ischaemic Heart Disease

1970 ◽  
Vol 19 (2) ◽  
pp. 87-93
Author(s):  
MS Kabir ◽  
AAS Majumder ◽  
AW Chowdhury ◽  
SA Haque ◽  
AQM Reza ◽  
...  
Keyword(s):  
Risk Factor ◽  
Heart Disease ◽  
Ischaemic Heart Disease ◽  
Plasminogen Activator ◽  
Research Work ◽  
Vascular Diseases ◽  
Plasminogen Activator Inhibitor ◽  
Plasma Homocysteine ◽  
Type I ◽  
Activator Inhibitor Type

Only one half to two thirds of atherosclerotic vascular diseases can be explained by classical risk factors like smoking, diabetes mellitus, hypertension, dyslipidaemia, family history of premature atherosclerotic vascular diseases, physical inactivity, obesity etc. Some other variables appear to contribute to the development of atherosclerotic vascular diseases which include estrogen deficiency, lipoprotein (a), plasma fibrinogen, plasminogen-activator inhibitor type I, endogenous tissue plasminogen activator (tPA), C-reactive protein and homocysteine. Over the last several years, investigators undertook extensive research work, in home and abroad, to determine the contribution of plasma homocysteine in the pathogenesis of atherosclerotic vascular diseases. So far the research work indicates, raised plasma homocysteine appears to be a potential risk factor for ischaemic heart disease.   doi: 10.3329/taj.v19i2.3158 TAJ 2006; 19(2): 87-93

Plasminogen Activator Inhibitor Type-1 Determines Plasmin Formation in Patients with Ischaemic Heart Disease

1995 ◽  
Vol 73 (05) ◽  
pp. 835-840 ◽  
Author(s):  
Ole Dyg Pedersen ◽  
Jørgen Gram ◽  
Jørgen Jespersen
Keyword(s):  
Heart Disease ◽  
Plasma Concentration ◽  
Ischaemic Heart Disease ◽  
Plasminogen Activator ◽  
Plasma Concentrations ◽  
Plasminogen Activator Inhibitor ◽  
Median Plasma ◽  
Inhibitor Type ◽  
Activator Inhibitor Type ◽  
Pai 1

SummaryThe aim of the present study was to find out whether plasminogen activator inhibitor type-1 (PAI-1) controls the formation of plasmin in patients with ischaemic heart disease.We examined PAI activity, PAI-1 antigen, tissue type plasminogen activator (t-PA) activity, t-PA antigen, plasmin-α2-antiplasmin complex (PAP-complex) and fibrin degradation products D-dimer in 62 patients before (unstimulated) and after infusion of l-desamino-8- D-arginine vasopressin (DDAVP; stimulated). DDAVP was used in a standardized dose to trigger the release of t-PA from the vascular endothelium.We observed that under basal conditions (unstimulated) median plasma t-PA activity for the whole group of patients was 86.5 mlU/ml (0-900), and after stimulation 2550 mlU/ml (0-6800), P <0.0001; median plasma concentration of t-PA antigen was 14.7 ng/ml (7.0-115.5) under basal conditions, and after stimulation 34.1 ng/ml (15.8-58.6), P <0.0001; median plasma PAI activity was 16.9 IU/ml (1.5-144.8) under basal conditions, and after stimulation 3.1 IU/ml (0-118.5), P <0.0001; median plasma concentration of PAI-1 antigen was 21.5 ng/ml (8.1-132.2) under basal conditions, and after stimulation 14.9 ng/ml (4.8-149.0), P <0.0001; the median plasma concentration of PAP-complex was 469.5 ng/ml (185.0-1802.0) under basal conditions, and after stimulation 695.5 (243.0-2292.0), P <0.0001; median plasma concentration of D-dimer was 298.0 ng/ml (103.0-948.0) under basal conditions, and after stimulation 296.5 ng/ml (97.0-917.0), P <0.0008.Under basal conditions plasma PAI activities and plasma concentrations of PAI-1 antigen were both significantly negatively correlated with plasma concentrations of PAP-complex (rs = -0.32; P <0.02 and rs = -0.42; P <0.002, respectively). After stimulation of the fibrinolytic system by infusion of DDAVP, plasma PAI activities and plasma concentrations of PAI-1 antigen were also significantly negatively correlated with plasma concentrations of PAP-complex (rs = -0.41; P <0.002 and rs = - 0.33; P <0.009, respectively).Our results indicate that PAI-1 regulates formation of plasmin in patients with ischaemic heart disease. These observations support that PAI-1 may play a critical role in the evolution of thrombosis.

scholarly journals Epinephrine Exerts Anticoagulant Effects during Human Endotoxemia

1997 ◽  
Vol 185 (6) ◽  
pp. 1143-1148 ◽  
Author(s):  
Tom van der Poll ◽  
Marcel Levi ◽  
Mieke Dentener ◽  
Patty M. Jansen ◽  
Susette M. Coyle ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Plasma Concentrations ◽  
Systemic Infection ◽  
Plasminogen Activator Inhibitor ◽  
Tissue Type ◽  
Coagulation System ◽  
Type I ◽  
Maximal Activation ◽  
Antithrombotic Effects ◽  
Activator Inhibitor Type

To determine the effect of a physiologically relevant elevation in the plasma concentrations of epinephrine on the activation of the hemostatic mechanism during endotoxemia, 17 healthy men were studied after intravenous injection of lipopolysaccharide (LPS, 2 ng/kg), while receiving a continuous infusion of epinephrine (30 ng/kg/min) started either 3 h (n = 5) or 24 h (n = 6) before LPS injection, or an infusion of normal saline (n = 6). Activation of the coagulation system (plasma concentrations of thrombin–antithrombin III complexes and prothrombin fragment F1+2) was significantly attenuated in the groups treated with epinephrine when compared with subjects injected with LPS only (P &lt;0.05). Epinephrine enhanced LPS-induced activation of fibrinolysis (plasma levels of tissue-type plasminogen activator and plasmin-α2–antiplasmin complexes; P &lt;0.05), but did not influence inhibition of fibrinolysis (plasminogen activator inhibitor type I). In subjects infused with epinephrine, the ratio of maximal activation of coagulation and maximal activation of fibrinolysis was reduced by &gt;50%. Hence, epinephrine exerts antithrombotic effects during endotoxemia by concurrent inhibition of coagulation, and stimulation of fibrinolysis. Epinephrine, whether endogenously produced or administered as a component of treatment, may limit the development of disseminated intravascular coagulation during systemic infection.

scholarly journals Plasminogen activator inhibitor type I stabilizes vitronectin-dependent adhesions in HT-1080 cells.

1990 ◽  
Vol 111 (5) ◽  
pp. 2183-2195 ◽  
Author(s):  
G J Ciambrone ◽  
P J McKeown-Longo
Keyword(s):  
Binding Site ◽  
Plasminogen Activator ◽  
Plasminogen Activator Inhibitor ◽  
Type I ◽  
Adherent Cells ◽  
Cell Rounding ◽  
Inhibitor Type ◽  
Activator Inhibitor Type ◽  
Activator Inhibitor ◽  
Pai 1

Polyclonal antibodies against plasminogen activator inhibitor type-I (PAI-1) caused rapid retraction and rounding of substrate-attached HT-1080 cells. The kinetics and extent of antibody-mediated cell rounding were not dependent on either urokinase or plasmin activity. Cells adherent to vitronectin-coated substrates detached within 2 h of antibody addition. Cells adherent to fibronectin were unaffected by the antibodies. Immunoblotting of substrate-attached material indicated that HT-1080 cells deposited PAI-1 into vitronectin, but not fibronectin, dependent contacts. These data suggest that the antibody-mediated cell rounding resulted from a steric disruption of vitronectin-dependent adhesions, indicating that the binding site on vitronectin for PAI-1 is near, but does not overlap, the binding site for vitronectin receptor. The accumulation of PAI-1 into vitronectin-dependent adhesion sites correlated temporally with the preferential degradation of fibronectin from the substrate. HT-1080 cells adherent to either fibronectin or vitronectin were able to activate exogenous plasminogen to plasmin. Plasmin levels were increased 200% on cells adherent to fibronectin and 100% on cells adherent to vitronectin. In the presence of a neutralizing antibody against PAI-1, vitronectin adherent cells activated plasminogen to the same extent as fibronectin adherent cells. Plasmin levels of 200% above baseline were associated with retraction of cells from the substrate. The ability of vitronectin adherent cells to activate exogenous plasmin was completely blocked in the presence of neutralizing antibodies against urokinase. These data represent the first demonstration that vitronectin-associated PAI-1 regulates urokinase in focal contact areas.

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