Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.5 (thrombin)
 33,306 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mechanisms and biochemical consequences of platelet-neutrophil interactions are well known. In contrast, platelet-eosinophil interactions remain largely unexplored. The aim of this study was to assess whether platelets adhere to eosinophils, and to analyze whether selectin-P would mediate that phenomenon. Eosinophils and platelets were obtained from peripheral blood of healthy volunteers. Eosinophils were isolated using magnetic cell separation method. Platelets were isolated and washed. A number of "rosettes" (an eosinophil with more than 5 adherent platelets) per 100 eosinophils was examined in the eosinophil-platelet suspension. Addition of thrombin stimulated formation of "rosettes". Monoclonal antibodies against selectin-P almost completely prevented thrombin-stimulated formation of "rosettes". In summary, intercellular interaction between platelets and eosinophils are mediated by selectin-P. This phenomenon may be of importance in asthma and other atopic diseases.
Pol J Pharmacol
PMID:Interactions between human platelets and eosinophils are mediated by selectin-P. 1213 13

Surgery is the basic treatment method of cholecystolithiasis. Traditional methods have been replaced laparoscopy. The aim of the study was the evaluation of haemostasis after classical and laparoscopic cholecystectomy. The studies were conducted in 48 patients suffering from chronic cholecystolithiasis--29 of them were operated on by laparoscopy, 19 patients were operated on by classical way. We revealed, that classical and laparoscopic cholecystectomy cause a similar increase of thrombin generating in vascular bed and are risk factors for occurrence of thrombo-embolic complications.
Pol Merkur Lekarski 2002 Aug
PMID:[Antithrombin III, protein C and thrombin/antithrombin III complexes (TAT) in patients suffering from chronic cholecystolithiasis treated by classical and laparoscopic cholecystectomy]. 1242 Mar 41

Cyclosporine A (CsA) has been accepted as one of the most efficient therapies of idiopathic nephrotic syndrome (INS) in children. Despite its beneficial effect on clinical course of the disease, its use has been associated with a number of side-effects. This prompted us to study the influence of cyclosporine A on the coagulation cascade in nephrotic children. We examined thrombinogenesis in 16 children in remission of steroid-dependent idiopathic nephrotic syndrome treated with cyclosporine A. The concentrations of F1 + 2 prothrombin fragments and thrombin-antithrombin complexes were used as markers of coagulation cascade activation. The results were compared between 18 children with INS relapse who had responded to 8-week glucocorticoid treatment (not treated with cyclosporine A) and 20 healthy subjects. We found an increased concentration of F1 + 2 prothrombin fragments in children treated with CsA, while in children after 8 weeks of glicocorticoid therapy the concentration of this marker was comparable to that in the controls. Since we observed similar biochemical disturbances in both INS groups, we suggested that cyclosporine A was able to stimulate coagulation that might lead to an increased risk of thomboembolic events in children with clinical remission of INS.
Pol Merkur Lekarski 2003 Feb
PMID:[Increased thrombin-genesis in cyclosporine A-treated idiopathic nephrotic syndrome in children]. 1272 66

Excessive coagulation and impaired fibrinolysis lead to many hemostatic disorders, which enhance the risk of development of life-threatening cardiovascular diseases such as myocardial infarction, stroke, deep venous thrombosis and pulmonary embolism, belonging to the most important factors influencing morbidity and mortality in civilized societies. The adverse events induced by currently used drugs, the need for regular monitoring of coagulation parameters, inconvenient, in some cases, route of administration stimulate further search for novel, effective and safe methods of therapies of these disorders. In this paper, we describe those new agents which are now under experimental and clinical study, such us prostanoids, nitroaspirin, GP IIb/IIIa receptor antagonists, thienopyridine derivatives, collagen-GPVI and von Willebrand factor-GPIb-IX contact blockers, direct thrombin inhibitors, inhibitors of thrombin-platelet interactions, factor VII inhibitors and tissue factor-factor VII contact blockers. Based on the available literature, we discuss the possible role of these agents in the future prevention and treatment of thromboembolic diseases.
Pol J Pharmacol
PMID:Progress in pharmacotherapy of thrombosis. 1458 10

Patients with end-stage renal disease dialyzed due to diabetic nephropathy are at higher risk of death due to cardiovascular complications than dialyzed non-diabetic patients. Disturbances in hemostasis may play a role in the vascular complications of diabetes mellitus. It has been postulated that TAFI-Thrombin Activatable Fibrinolysis Inhibitor, newly described glycoprotein, couples two opposite systems: coagulation and fibrinolysis. The aim of the work was to study TAFI concentration in hemodialyzed and peritoneally dialyzed diabetic and non-diabetic patients. We assessed: TAFI concentration, markers of ongoing coagulation: thrombin-antithrombin complexes, prothrombin fragments 1 + 2 (markers of TAFI activation), a marker of ongoing fibrinolysis: plasmin-antiplasmin complexes, a marker of TAFI cataliser to TAFIa-thrombomodulin using commercially available kits. All four groups studied did not differ in regard to fibrinogen, thrombomodulin, plasmin-antiplasmin complexes, and TAFI concentration. Both groups of dialyzed diabetic patients have higher concentration of markers of ongoing coagulation when compared to dialyzed non-diabetic patients. Hypercoagulable state observed in dialyzed diabetic patients may contribute to the higher cardiovascular mortality in these population.
Pol Arch Med Wewn 2003 Aug
PMID:[Thrombin activatable fibrinolysis o inhibitor-TAFI- in dialyzed patients with diabetic nephropathy]. 1468 22

Protein Z (PZ) is a 6.2 kDa vitamin K-dependent protein, synthesized in the liver. The gene for human PZ is localized to chromosome 13 at band 34 q. The structure of PZ is very similar to that of factors VII, IX, X and protein C. Very low plasma levels of protein Z were observed under oral anticoagulant treatment. The cause of this phenomenon might be increased protein Z binding on the surface of endothelial cells. Protein Z is consumed during coagulopathy. About 60% of humans suffering from a bleeding tendency of unknown origin presented with decreased plasma levels of protein Z. PZ forms a Ca(2+)-dependent complex with activated factor X (Xa) on phospholipid surfaces, that leads to the inhibition of factor Xa and decrease in thrombin generation. Inhibition of factor Xa may be caused directly by protein Z or indirectly by the activity of protein Z-dependent protease inhibitor (ZPI). ZPI is a 72 kDa member of the serpin family of proteinase inhibitors, synthesized in the liver. ZPI circulates in plasma in complex with protein Z. ZPI in the presence of Ca2+ and phospholipids inhibits factor Xa. The presence of protein Z enhances this process by more than 1000 times. ZPI also inhibits activated factor XI in the absence of protein Z, Ca2+ or phospholipids. Protein Z deficiency may induce bleeding as well as prothrombotic tendencies and might occur as an inherited disorder. Protein Z deficiency may aggravate mild bleeding tendency in subjects with diagnosed borderline decrease in von Willebrand factor and factor VII activity. Patients presenting with factor V Leiden mutation and low protein Z levels show earlier onset and higher frequency of thromboembolic events comparing to patients with normal protein Z levels.
Pol Merkur Lekarski 2003 Dec
PMID:[Protein Z]. 1505 66

Colic in horses very often induces changes in the coagulation system causing the development of disseminated intravascular clotting. It is promoted by blood concentration and an increase in exposition of coagulation activators with a simultaneous decrease in coagulation inhibitors activity, mainly antithrombin III. Progressing blood platelets aggregation supports production of microthromboses and plugging capillary vessels. The progression of this processes causes complications in basic disease and becomes the reason for therapeutic failure. Determination of coagulation system indexes such as the number of platelets, prothrombin time, activated partial thromboplastin time, thrombin time, concentration of fibrinogen and fibrinogen degradation products, and D-dimmer and antithrombin III contents enables diagnosis and facilitates appropriate therapy of colic in horses.
Pol J Vet Sci 2004
PMID:The coagulation system in horses with colic. 1506 86

epsilon-Aminocaproic acid (EACA) is a synthetic low molecular drug with antifibrinolytic activity. However, treatment with this drug can be incidentally associated with an increased thrombotic tendency. The aim of the present work was to test synthetic EACA derivatives for their antiplatelet activities. We investigated the effect of three EACA derivatives with antifibrinolytic activity: I. epsilon-aminocaproyl-L-leucine hydrochloride (HCl*H-EACA-L-Leu-OH), II. epsilon-aminocaproyl-L-(S-benzyl)-cysteine hydrochloride (HCl*H-EACA-L-Cys(S-Bzl)-OH) and III. epsilon-aminocaproyl-L-norleucine (H-EACA-L-Nle-OH) on platelet responses (aggregation and adhesion) and on their integrity. It was found that: 1. as judged by LDH release test, none of the tested compounds, up to 20 mM, was toxic to platelets, 2. in comparison with EACA, all the synthetic derivatives inhibited much stronger the ADP- and collagen-induced aggregation of platelets suspended in plasma (platelet rich plasma) and aggregation of these cells in whole blood, 3. EACA and its derivatives exerted a similar inhibitory effect on the thrombin-induced adhesion of platelets to fibrinogen-coated surfaces. Since platelet activation and blood coagulation are tightly associated processes, the antiplatelet properties of EACA derivatives are expected to indicate reduced thrombotic properties of these derivatives compared to EACA.
Acta Biochim Pol 2004
PMID:The effect of some epsilon-aminocaproic acid derivatives on platelet responses. 1509 27

Desmopressin (DDAVP) action on platelets is associated with the development of procoagulant response but the underlying mechanism of this phenomenon is not known. We investigated whether this effect of DDAVP might be due to activation of plasma membrane Na+/H+ exchanger. The DDAVP-induced platelet procoagulant response, measured as phospholipid-dependent thrombin generation, was dose dependent and significantly weaker than that produced by collagen or monensin (mimics Na+/H+ antiport). Both the DDAVP- and collagen-produced procoagulant responses were less pronounced in the presence of EIPA, an Na+/H+ exchanger inhibitor. Flow cytometry studies revealed that in vitro treatment of platelets with DDAVP or collagen was associated with the appearance of both degranulated (and fragmented) and swollen cells. The DDAVP-evoked rise in size and granularity heterogeneity was similar to that produced by collagen or monensin and was not observed in the presence of EIPA. Using flow cytometry and annexin V-FITC as a probe for phosphatidylserine (PS) we demonstrated increased and uniform binding of this marker to all subsets of DDAVP-treated platelet population. The DDAVP-evoked PS expression was dose dependent, strongly reduced by EIPA and weaker than that caused by monensin or collagen. As judged by optical swelling assay, DDAVP in a dose dependent manner produced a rise in platelet volume. The swelling was inhibited by EIPA and its kinetics was similar to that observed in the presence of monensin. Electronic cell-sizing measurements showed an increase in mean platelet volume and a decrease in platelet count and platelet crit upon treatment with DDAVP. DDAVP elicited a slow (much slower than collagen) alkalinization of platelet cytosol. Altogether the data indicate an involvement of Na+/H+ exchanger in the generation of procoagulant activity in DDAVP-treated platelets.
Acta Biochim Pol 2004
PMID:Involvement of Na+/H+ exchanger in desmopressin-induced platelet procoagulant response. 1544 38

This study was undertaken to determine whether nitric oxide (NO) can affect platelet responses through the inhibition of energy production. It was found that NO donors: S-nitroso-N-acetylpenicyllamine, SNAP, (5-50 microM) and sodium nitroprusside, SNP, (5-100 microM) inhibited collagen- and ADP-induced aggregation of porcine platelets. The corresponding IC50 values for SNAP and SNP varied from 5 to 30 microM and from 9 to 75 microM, respectively. Collagen- and thrombin-induced platelet secretion was inhibited by SNAP (IC50 = 50 microM) and by SNP (IC50 = 100 microM). SNAP (20-100 microM), SNP (10-200 microM) and collagen (20 microg/ml) stimulated glycolysis in intact platelets. The degree of glycolysis stimulation exerted by NO donors was similar to that produced by respiratory chain inhibitors (cyanide and antimycin A) or uncouplers (2,4-dinitrophenol). Neither the NO donors nor the respiratory chain blockers affected glycolysis in platelet homogenate. SNAP (20-100 microM) and SNP (50-200 microM) inhibited oxygen consumption by platelets. The effect of SNP and SNAP on glycolysis and respiration was not reduced by 1H-[1,2,4]oxadiazolo-[4,3-a]quinoxalin-1-one, a selective inhibitor of NO-stimulated guanylate cyclase. SNAP (5-100 microM) and SNP (10-300 microM) inhibited the activity of platelet cytochrome oxidase and had no effect on NADH:ubiquinone oxidoreductase and succinate dehydrogenase. Blocking of the mitochondrial energy production by antimycin A slightly affected collagen-evoked aggregation and strongly inhibited platelet secretion. The results indicate that: 1) in porcine platelets NO is able to diminish mitochondrial energy production through the inhibition of cytochrome oxidase, 2) the inhibitory effect of NO on platelet secretion (but not aggregation) can be attributed to the reduction of mitochondrial energy production.
Acta Biochim Pol 2004
PMID:Nitric oxide and platelet energy metabolism. 1544 39


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>