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Biomedical subjects

E Selmayr

Publications and source records attributed to E Selmayr.

9 recordsLinked to original sources
PubMed1988

Increased blood fibrinolytic activity after physical exercise: comparative study in individuals with different sporting activities and in patients after myocardial infarction taking part in a rehabilitation sports program.

The activation of fibrinolysis during bicycle ergometry was studied in two pairs of age-matched groups. Group A: 18 healthy male competitive athletes (23 +/- 3.5 years of age, mean +/- SD), Group B: 18 healthy male volunteers (25.7 +/- 2.7) not engaged in any sports, Group C: 17 healthy male volunteers (50.6 +/- 7.7) regularly practicing sports, and Group D: 18 male survivors from myocardial infarction (MI-patients, 54.2 +/- 7.9) who took part in a rehabilitation sports program. Before ergometry, healthy participants with regular sporting activities showed significantly lower plasma plasminogen activator inhibitor capacities (PAI cap) than the members of the respective age-matched control groups: Group A 13.9 +/- 2.6 AU/ml, Group B 18.5 +/- 5.5, p less than 0.005; Group C 15.2 +/- 2.9, Group D 20.7 +/- 5.5, p less than 0.05. During ergometry the release of tPA antigen did not differ significantly between the age-matched groups, however, tissue plasminogen activator (tPA) activities after ergometry were higher in groups presenting lower pre-test PAI cap values. Group A 5.5 +/- 6.4 AU/ml, Group B 1.1 +/- 2.9 AU/ml, p less than 0.05; Group C 2.9 +/- 3.3, Group D 0.2 +/- 0.7, p less than 0.05. Levels of the fibrin split product (D-dimer) did not change in any of the groups. This investigation indicates that (1) regular vigorous sporting activities enhance blood fibrinolysis by reducing blood PAI cap in healthy individuals, (2) rehabilitation sport is not capable of reducing blood PAI cap in MI-patients to values measured in age matched healthy individuals regularly practicing sports and (3) the activation of fibrinolysis during physical exercise has no systemic fibrinolytic effect.

Adult↗
PubMed1988

Thrombin-induced fibrinopeptide B release from normal and variant fibrinogens: influence of inhibitors of fibrin polymerization.

Thrombin preferentially cleaves fibrinopeptides A (FPA) from fibrinogen resulting in the formation of desAA-fibrin from which most of the fibrinopeptides B (FPB) are then released with an enhanced rate. Kinetics of fibrinopeptide release from normal and dysfunctional fibrinogens were investigated in order to further characterize the mechanism of accelerated FPB release during desAA-fibrin polymerization. Dysfunctional fibrinogens London I and Ashford, exhibiting primary polymerization abnormalities (i.e., an abnormality present when all fibrinopeptides have been cleaved), which in the case of fibrinogen London I is believed to be caused by a defect in the D-domain, were shown to exhibit a decreased rate of FPB release compared with normal fibrinogen. While Gly-Pro-Arg-Pro, an inhibitor of fibrin polymerization, was shown to decrease the rate of FPB release from normal fibrinogen by a factor of 5, normal fragment D1, although inhibiting clot formation of normal fibrinogen, did not influence the acceleration of FPB release. On the other hand, the presence of fragment D1 did not enhance FPB release from fibrinogen London I, suggesting that interaction of D-domains in functional isolation with desAA-fibrin E-domains is not sufficient to enhance FPB release. Although clot formation was inhibited by the concentrations of fragment D1 used, the formation of small desAA-fibrin oligomers was hardly affected. Thus, small fibrin polymers, but not desAA-fibrin monomers, act as optimal substrates for the release of FPB by thrombin.

Blood Coagulation Disorders↗
PubMed1988

Evidence of increased association of fibrinogen with platelets caused by sodium citrate.

Washed platelet suspensions are almost always prepared from blood anticoagulated with sodium citrate. Because citrate has been reported to affect platelet function, we examined the involvement of citrate on the platelet-fibrinogen interactions. More iodine 125-labeled fibrinogen was bound on washed platelets from citrate-anticoagulated blood (CP) than on washed platelets from non-anticoagulated blood (PNB) obtained by the rapid gel filtration of native blood from the same donor. Scatchard analyses of the equilibrium binding data gave linear plots for PNB indicating a single class of binding sites with 16,480 +/- 2,800 fibrinogen molecules bound per platelet (Kd 5.6 x 10(-7) mol/L); CP gave curvilinear plots that, when resolved into two components assuming two classes of binding sites, gave a high-affinity site (4,950 +/- 970 molecules per platelet; Kd 1.29 x 10(-7) mol/L) and a low-affinity site (25,660 +/- 4,600 molecules per platelet; Kd 1.02 x 10(-6) mol/L). When blood from one donor was collected into 10 mmol/L and 20 mmol/L citrate, increased binding of 125I-fibrinogen was observed on platelets exposed to 20 mmol/L citrate. Exposure of PNB to varying citrate concentrations showed enhanced fibrinogen binding with increasing citrate concentrations; differences in the Kd values between non-citrate-treated PNB and citrate-treated PNB were apparent at about 7.5 mmol/L of citrate. The effects of citrate in increasing the association of fibrinogen with platelets were not caused by variations in the pH; although fibrinogen binding was diminished at low pH of the citrate used, more binding was observed in the presence of citrate than with buffer of the same pH. The effects of citrate appear to be on the platelet fibrinogen receptor because nonspecific binding was not affected by the citrate. Inasmuch as no carbon 14-labeled citric acid binding to platelets was observed, citrate may affect the platelet-fibrinogen interactions without binding to the platelets. We conclude that platelet exposure to citrate increases the fibrinogen binding and may lead to the appearance of curved Scatchard plots.

Blood Platelets↗
PubMed1985

Soluble crosslinked fibrin(ogen) polymers.

The present study is concerned with the formation of fibrin-fibrinogen associations in the presence of FXIIIa while fibrinolysis was inhibited by aprotinin and EACA. SDS agarose-polyacrylamide gel electrophoresis on 2.5% gels under non-reducing conditions and ultracentrifugation of the associations on urea-sucrose density gradients showed the formation of soluble cross-linked high molecular weight (HMW) fibrin-fibrinogen polymers with an estimated molecular size up to 10 times that of fibrinogen. After incubation of a mixture of 131I-fibrinogen (4 mg/ml) and 125I-desAA-fibrin (0.2 mg/ml) with FXIIIa (2 U/ml) for 1 h at 37 degrees C, about 5% of the fibrinogen and 80% of the fibrin was incorporated into the generated soluble HMW polymers. The detection of soluble crosslinked fibrin-fibrinogen polymers could be a useful diagnostic criterion for imminent DIC.

Disseminated Intravascular Coagulation↗
PubMed1985

Crosslinking of fibrinogen to immobilized DesAA-fibrin.

DesAA-fibrin Sepharose was produced by treating fibrinogen-Sepharose with batroxobin. DesAA-fibrin Sepharose was mixed with different concentrations of fibrinogen and at different ratios, and incubated with preactivated FXIII. After 2 hours at 37 degrees C, the Sepharose beads were separated by centrifugation and non-crosslinked fibrinogen was removed by twice times washing with guanidinium chloride, pH 4.1. Under these experimental conditions specific crosslinking of fibrinogen to immobilized desAA-fibrin by FXIIIa was found. These results support the concept of a specific interaction between fibrinogen and fibrin involving polymerization which enables FXIIIa to crosslink fibrin to fibrinogen being in an half-staggered overlap position but not in DD-long contact.

Fibrin↗
PubMed1985

Crosslinking of soluble fibrin and fibrinogen.

Monomeric 125I-desAA-fibrin and 125I-desAABB-fibrin were prepared by treating 125I-fibrinogen with thrombin. Preactivated factor XIII was added to 125I-fibrin/131I-fibrinogen mixtures, and after incubation for 2 and 6 hours, samples were investigated by SDS polyacrylamide gel electrophoresis under reducing conditions. The electrophoresis pattern showed a gamma-gamma band containing both 125I-fibrin and 131I-fibrinogen. These experiments indicate that a fibrin molecule polymerizes with a fibrinogen molecule in a similar way as a fibrin molecule polymerizes to a second fibrin molecule. This type of polymerization results in conformational changes of the molecules involved thus enabling FXIIIa for specific crosslinking reaction. The polymerization of fibrin and fibrinogen molecules as well as the crosslinking of fibrin to fibrinogen molecules seem to represent a mechanism for interrupting the process of further fibrin polymerization.

Blood Coagulation↗
PubMed1985

Influence of fibrinogen on fibrin polymerization. Ultracentrifugation studies.

During the transformation of fibrinogen to fibrin, excess fibrinogen suppresses further polymerization of fibrin, thereby enabling the nascent fibrin to be transported in a soluble form in blood. The question of possible complex formation between fibrin and fibrinogen was addressed by analyzing fibrin/fibrinogen (1:20, mol/mol) mixtures in the presence of calcium ions in stable linear sucrose density gradients by ultracentrifugation at 37 degrees C. During the period of ultracentrifugation in independent experiments, 40% of desAA-fibrin and 30% of desAABB-fibrin, respectively, precipitated without the participation of fibrinogen. The desAABB-fibrin, recovered in the gradient fractions, appeared as high-molecular-weight polymers (22 S), whereas the recovered desAA-fibrin exhibited only a slight increase in molecular weight (9 S) compared to fibrinogen (8 S). In contrast to this finding, both types of fibrin were totally recovered in gradient fractions provided that fibrinogen was present in the gradient at a uniform concentration of 2 mg/ml. In addition, the presence of fibrinogen but not human serum albumin reduced the size of desAABB-fibrin polymers (17 S). However, stable fibrin-fibrinogen complexes could not be demonstrated, since cosedimentation of differently labelled desAABB-fibrin and fibrinogen was not detectable. These studies suggest a specific but weak interaction of the solubilizing fibrinogen with the soluble fibrin polymers as demonstrated by a rapid exchange of both macromolecules.

Centrifugation, Density Gradient↗
PubMedDate not supplied

Fibrinolysis and factor XIII in women with spontaneous abortion.

In the present study, parameters of the fibrinolytic system and factor XIII were determined in 26 women with spontaneous abortion and in 21 women with intact pregnancies to gain insight into the role of fibrinolysis in spontaneous abortion. Both groups of women did not significantly differ from each other in age or weeks of pregnancy. There were no differences in euglobulin lysis time (ELT), tissue plasminogen activator (t-PA) antigen, and plasminogen activator inhibitor type 1 (PAI-1) antigen between the study group and the control group. Factor XIII activity was significantly decreased in patients during abortion. In the present study, changes of fibrinolytic parameters measured in teh cubital vein blood of patients with abortion were not observed although local changes in fibrinolytic activity had been associated with spontaneous abortion. The pathophysiological role of the decrease in factor XIII activity observed in the present study remains to be elucidated.

Abortion, Spontaneous↗