Effect of liver metastasis from primary rectal adenocarcinoma on activity of tissue plasminogen activators and α2-macroglobulin.

2018 ◽  
Vol 36 (15_suppl) ◽  
pp. e15552-e15552
Author(s):  
Elena Alekseevna Dzhenkova ◽  
Oleg I. Kit ◽  
Elena M. Frantsiyants ◽  
Alexander Vasilievich Shaposhnikov ◽  
Valeria A. Bandovkina ◽  
...  
Keyword(s):  
Liver Metastasis ◽  
Rectal Adenocarcinoma ◽  
Plasminogen Activators ◽  
Α2 Macroglobulin ◽  
Tissue Plasminogen

Differences in plasminogen activation in primary rectal adenocarcinoma with and without liver metastasis.

2017 ◽  
Vol 35 (15_suppl) ◽  
pp. e15111-e15111
Author(s):  
Evgeniy N. Kolesnikov ◽  
Elena Alekseevna Nikipelova ◽  
Elena Mikhaylovna Frantsiyants ◽  
Larisa Kozlova ◽  
Valeria Bandovkina ◽  
...  
Keyword(s):  
Liver Metastasis ◽  
Inhibitory Control ◽  
Rectal Adenocarcinoma ◽  
Plasminogen Activators ◽  
Plasminogen Activation ◽  
Plasminogen Activation System ◽  
Α2 Macroglobulin ◽  
Activation System ◽  
Resection Line ◽  
Metastatic Activity

e15111 Background: Plasminogen activators play a key role in the cascade fibrinolytic system as they catalyze plasmin formation from plasminogen (PG). Plasminogen activators together with plasmin are directly or indirectly involved in tumor growth. The purpose of the study was to compare the plasminogen activation system in primary adenocarcinomas (РА) of the rectum (R) with and without liver metastases (LM). Methods: Tissues of tumors (РА, st. III, G2, 38-74 years) and their perifocal zone (PZ) with LM (T2-3NхM1, n = 24) and without them (T2-3N0M0, n = 32) were studied by ELISA. Results: The studied parameters did not differ in apparently intact R tissues in the resection line (RL) with and without LM. Plasmin-α2-antiplasmin complex (PAP) was 1.4 times higher in PA with LM than without LM (p < 0.05). Prourokinase and urokinase levels (uPA-Ag and uPA-act) were 12.4 and 3.7 higher than in RL. uPA-Ag and uPA-act in PA+LM were higher than without LM by 1.4 and 1.6 times. PG levels and α2-macroglobulin (α2M) activity in PA+LM were lower by 1.5 and 2.7 times than in PA without LM and lower than in RL (p < 0.01). All studied parameters, except α2M, in PA+LM were activated more than in PA without LM. Low α2M content supposed realization of effects of uPA and plasmin in insufficient inhibitory control. Most parameters in PZ+LM were between the levels in PA and RL being significantly different from both and significantly exceeding the values in PZ of PA without LM. α2М was an exception being 1.8 times lower in PZ of PA+LM than in PZ of PA without LM. The results demonstrated higher uPA and РАР levels in PA and its PZ with LM than without them, with increased PG consumption and decreased α2M activity in these parts of the rectum. Activation of plasminogen system in tissues of PA+LM and in PA without LM was unidirectional. Conclusions: Levels of uPA and PAP, as well as low α2M content in PA and PZ with LM can be used as an indicator of tumor metastatic activity.

Inhibitors Interfering with the Quantitative Estimation of Tissue Plasminogen Activator

1975 ◽  
Author(s):  
G. Wijngaards ◽  
A. T. Potjer
Keyword(s):  
Plasminogen Activator ◽  
Tissue Plasminogen Activator ◽  
Human Tissue ◽  
Inhibitory Action ◽  
Human Lung ◽  
Quantitative Estimation ◽  
Plasminogen Activators ◽  
Tissue Extracts ◽  
Tissue Plasminogen ◽  
Inhibitory Components

The commonly used quantitative assay for plasminogen activator in tissues by Astrup and Albrechtsen (1957) was re-evaluated with special reference to the presence of inhibitors in tissue extracts at different stages of the procedure.Human lung, liver, and placenta tissues were chosen for their different activator and inhibitor content. Samples of the extracts were tested for inhibitory capacity against purified human tissue plasminogen activator, urokinase, and plasmin on different kinds of fibrin plates.The procedure for preparing the samples according to Astrup and Albrechtsen did not completely eliminate the inhibitory action against the plasminogen activators added. The presence of inhibitors was partly obscured by 2M KCNS in the sample. In order to quantitate the plasminogen activator content in tissues, the method should be revised with respect to the elimination of inhibiting material.Some interesting aspects of the inhibitory components extracted from liver and placenta were revealed by comparing urokinase inhibition to tissue activator inhibition as to the degree of denaturation during the procedure. It was suggested that, although they have much in common, urokinase and tissue activator inhibitors are separate entities.

Distinction of Plasma Inhibitor of Activator-Induced Clot Lysis from Antiplasmins

1975 ◽  
Author(s):  
N. Aoki ◽  
M. Matsuda ◽  
M. Moroi ◽  
N. Yoshida
Keyword(s):  
Affinity Chromatography ◽  
Human Plasma ◽  
Gel Filtration ◽  
Plasminogen Activators ◽  
Inhibitory Effect ◽  
Clot Lysis ◽  
Plasminogen Activation ◽  
Lysis Time ◽  
Α2 Macroglobulin ◽  
Clot Lysis Time

A fraction of human plasma prolongs the activator-induced clot lysis time and inhibits plasminogen activation by the plasminogen activators derived from various sources (urine and tissues). This fraction, designated as antiactivator fraction, was separatid from antiplasmin fractions (α2-macroglobulin and α1-antitrypsin) by gel filtration and affinity chromatography on Sepharose coupled with IgG of antiserum to α1-antitrypsin. Anti-activator fraction thus obtained exerted little antiplasmin activity but inhibited strongly activator-induced clot lysis.Inhibitory effect of plasma on urokinase-induced clot lysis (antiactivator activity) was assayed in various diseases and compared with antiplasmin activity. No correlation was found between the two activities, and it was concluded that the two activities are independent and are ascribed to two different entities.

Plasminogen Activators in the Intestine of Patients with Inflammatory Bowel Disease

1988 ◽  
Vol 60 (02) ◽  
pp. 262-266 ◽  
Author(s):  
P A F de Bruin ◽  
G Crama-Bohbouth ◽  
H W Verspaget ◽  
J H Verheijen ◽  
G Dooijewaard ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Inflammatory Bowel Disease ◽  
Bowel Disease ◽  
Plasminogen Activators ◽  
Intestinal Tissue ◽  
Colonic Adenomas ◽  
Tissue Plasminogen ◽  
Inflammatory Bowel ◽  
The Difference ◽  
Colorectal Cancer Patients

SummaryPlasminogen activators were determined in intestinal tissue, obtained after surgery from patients with Crohn’s disease and ulcerative colitis, and compared with normal intestinal tissue from colorectal cancer patients.The activity and quantity of tissue-plasminogen activator (t-PA) was found to decrease with the severity of inflammation in the patients with inflammatory bowel disease. Urokinase (u-PA) activity, however, was not changed compared with controls or in relation with severity of inflammation. In contrast, the level of u-PA antigen was found to be increased significantly in the inflammatory bowel disease tissues and was also related with severity of inflammation. The difference between u-PA activity and antigen in inflammatory bowel disease tissue could be attributed to an increase in inactive pro-u-PA and u-PA-inhibitor complexes.This increase in u-PA and the concomitant decrease in t-PA, are similar to those found in premalignant colonic adenomas, and might be related to the known increased cancer risk in inflammatory bowel disease.

Reversible and Irreversible Alterations of Human Plasminogen Indicated by Changes in Susceptibility to Plasminogen Activators and in Response to ∈-Aminocaproic Acid

1974 ◽  
Vol 32 (02/03) ◽  
pp. 325-340 ◽  
Author(s):  
Sixtus Thorsen ◽  
Preben Kok ◽  
Tage Astrup
Keyword(s):  
Ionic Strength ◽  
Aminocaproic Acid ◽  
Plasminogen Activators ◽  
Plasminogen Activation ◽  
Porcine Tissue ◽  
Biphasic Pattern ◽  
Tissue Plasminogen ◽  
Human Plasminogen ◽  
Uniform Manner ◽  
Low Ionic Strength

SummaryIncreasing concentrations of EACA produce a biphasic pattern of inhibition and enhancement of urokinase-induced lysis of bovine fibrin containing bovine plasminogen, while the inhibition of fibrinolysis induced by a porcine tissue plasminogen activator increases uniformly. The biphasic EACA pattern is also observed with human plasminogen in fibrinolytic and caseinolytic assays of urokinase. The biphasic EACA pattern produced with urokinase is related to the presence of a genuine form of plasminogen. The enhancement phase is caused by an increased rate of plasminogen activation in the presence of EACA. A brief treatment of genuine plasminogen with acid at ionic strength 0.15 results in an enhanced susceptibility to plasminogen activators and in a partial abolishment of the biphasic response. These acid-induced alterations of plasminogen seem to be reversed by acid dialysis at low ionic strength. Other preparations of plasminogen with enhanced susceptibility to activators have lost the ability to produce a biphasic pattern of inhibition and enhancement of urokinase-induced plasminogen activation in the presence of EACA and this ability does not return after acid dialysis at low ionic strength. EACA inhibits all plasmin preparations, whether prepared from genuine or altered forms of plasminogen, in the same uniform manner.Our results show that different forms of plasminogen can be identified by differences in the susceptibilities to activators, by their response to EACA, and by the reversibility or irreversibility of the alterations.

scholarly journals Fluorogenic Substrates for the Determination of Plasminogen Activators and Plasmin

1977 ◽  
Author(s):  
W. Nieuwenhuizen ◽  
G. Wijngaards ◽  
E. Groeneveld
Keyword(s):  
Plasminogen Activator ◽  
Enzyme Histochemistry ◽  
Biological Fluids ◽  
Kinetic Studies ◽  
Plasminogen Activators ◽  
Fluorogenic Substrates ◽  
Highly Sensitive ◽  
Tissue Plasminogen ◽  
Hydrolysis Of

Plasminogen activator activities in biological fluids are low and specific for plasminogen. Highly sensitive and accurate assays are needed for direct quantification and for kinetic studies. We therefore, synthesized tripeptide amides i. e., t. BOC. val. gly. arg β-NA (l) and val. gly. arg β-NA (II) from which the fluorescent group β-naphtylamine (β-NA) is released upon enzymatic hydrolysis.Kinetic parameters found for the hydrolysis of these substrates by plasmin, urokinase and tissue plasminogen activator are:*in nmol/CU/min; **in pmol/CTA/minStrikingly, tissue activator is not active on substrate II, allowing discrimination between this activator and other proteases.The sensitivity of the assay is at least ten times higher than that observed for other synthetic substrates available. Moreover, substrates I and II can be used in enzyme histochemistry.

Unilateral orolingual angioedema in a patient with sarcoidosis after intravenous thrombolysis due to acute stroke without improvement after treatment with icatibant

2020 ◽  
Vol 13 (12) ◽  
pp. e236643
Author(s):  
Anna Daniela Wollmach ◽  
Daniel Zehnder ◽  
Markus Schwendinger ◽  
Alexander Andrea Tarnutzer
Keyword(s):  
Risk Factor ◽  
Ischaemic Stroke ◽  
Acute Ischaemic Stroke ◽  
Ace Inhibitors ◽  
Intravenous Thrombolysis ◽  
Plasminogen Activators ◽  
Potential Complication ◽  
Tissue Plasminogen ◽  
History Of ◽  
Complement Pathways

A potential complication after intravenous administration of recombinant tissue plasminogen activators (rtPAs) for thrombolysis in acute ischaemic stroke is orolingual angioedema, with an incidence of 0.4%–7.9%. In the herewith reported case, we discuss potential links between a history of sarcoidosis and the occurrence of orolingual angioedema after rtPA administration. Sarcoidosis is often accompanied by an elevated ACE level. In contrast, low ACE levels appear to play a role in the pathomechanism currently assumed to trigger angioedema, that is, the activation of the bradykinin and complement pathways. Medication with ACE inhibitors is considered a risk factor for angioedema. Based on these considerations, the patient was also treated with icatibant, a bradykinin B2-receptor antagonist, which has been found useful in recent publications on treating orolingual angioedema after intravenous lysis in ischaemic stroke.

Sign in / Sign up

Export Citation Format

Share Document