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PubMed1982

Effect of EACA, PAMBA, AMCA and AMBOCA on fibrinolysis induced by streptokinase, urokinase and tissue activator.

A study is presented in which the inhibiting effects of eACA, PAMBA, AMCA and AMBOCA on fibrinolysis induced by three activators have been compared by a clot lysis method. The order of inhibitory potency was AMBOCA greater than AMCA greater than PAMBA greater than EACA. The activity ratios obtained were found to be influenced by the level of inhibition. At low levels of inhibition the differences between the inhibitory activities are usually more pronounced than at high levels. The degree of inhibition is dependent on the fibrinolytic activator used. The order of sensitivity to the inhibitors was, within the analytical conditions used, found to be: tissue activator greater than streptokinase greater than urokinase. The results are discussed in comparison to the different activity ratios reported by others.

4-Aminobenzoic Acid↗
PubMed1984

Clinical significance of accelerated fibrinolysis in liver disease.

We compared site and severity of bleeding in 46 patients with cirrhosis of the liver and accelerated fibrinolysis (defined as a dilute whole-blood clot lysis time less than 2 h) to 44 patients with cirrhosis of the liver and normal fibrinolysis (dilute whole-blood clot lysis time greater than 4 h). Patients with accelerated fibrinolysis had a significantly higher incidence of severe soft-tissue bleeding after trauma and a trend toward increased intracranial bleeding. Mucosal, postoperative, and gastrointestinal bleeding were equally frequent in the two groups. The median partial thromboplastin time was significantly longer, and the median bilirubin and fibrin/fibrinogen degradation product levels were significantly higher in the group with accelerated fibrinolysis, but median prothrombin time, platelet count, and levels of fibrinogen and serum albumin were comparable. The fibrinolytic inhibitor epsilon-aminocaproic acid successfully controlled bleeding in 4 of 6 cases used. Accelerated fibrinolysis may predispose patients with cirrhosis to soft-tissue and intracranial bleeding.

Bilirubin↗
PubMed1988

Heteroclitic antibodies: differences in fine specificities between monoclonal antibodies directed against dinitrophenyl and trinitrophenyl haptens.

The inhibition of binding of monoclonal antibodies by different haptens was studied using the 50% antibody binding assay. The binding of antidinitrophenyl and antitrinitrophenyl antibodies to dinitrophenylated or trinitrophenylated bovine serum albumin could be inhibited by monovalent dinitrophenyl or trinitrophenyl epsilon-aminocaproic acid. Some of the antibodies could be inhibited to a greater degree with the cross-reacting haptens than with the haptens homologous to the immunizing antigen, therefore these antibodies were heteroclitic.

Animals↗
PubMed2004

Neutrophils stimulated by apolipoprotein(a) generate fragments that are stronger inhibitors of plasmin formation than apo(a).

Apolipoprotein(a), the plasminogen-like component of lipoprotein(a), is transformed into fragments by polymorphonuclear neutrophils (PMNs) elastase. Since stimulated PMNs express urokinase-type plasminogen activator (uPA), we sought to investigate the relevance of apo(a) fragmentation on plasminogen activation by neutrophils. Freshly isolated human PMNs stimulated by a 10 kringle recombinant apo(a), r-apo(a), activate plasminogen in a specific and saturable manner (Km = 476 +/- 42 nM, Vmax = 896 +/- 18 pmol min(-1)). This activation is prevented by amiloride, an inhibitor of u-PA, and epsilon-aminocaproic acid, epsilon-ACA, a lysine analogue that blocks plasminogen binding to PMNs. Stimulation of PMNs by apo(a) results in the formation of elastase-derived apo(a) fragments. These fragments produce a concentration-dependent decrease in the formation of plasmin. Addition of elastase inhibitors to PMNs prevented degradation of apo(a) and partially restored the formation of plasmin. In a similar manner, isolated r-apo(a) fragments were able to produce a 100% decrease in plasmin generation as compared to intact r-apo(a). These data indicate that apo(a) fragments produce a more pronounced inhibition in the generation of cell-bound plasmin by uPA than the parent apo(a). These effects of apo(a) and its fragments were neutralised by a monoclonal antibody directed against the lysine-binding site of apo(a). This mechanism may be of biological relevance to the effects of Lp(a) in conditions where PMNs accumulate and release elastase, i.e. thrombus lysis and inflammatory lesions.

Apolipoproteins A↗
PubMed1998

Sequences within the amino terminus of ApoB100 mediate its noncovalent association with apo(a).

Although sequences within the C terminus of apolipoprotein B (apoB) have been implicated in the formation of covalent lipoprotein(a) [Lp(a)] particles, sequences in apoB that mediate initial noncovalent interaction with apo(a) remain to be characterized. To address this question, we have used an affinity chromatography method in which 2 recombinant forms of apo(a) [r-apo(a); either a 17-kringle form (17K) or a derivative containing apo(a) kringle IV types 5-8] have been immobilized onto Sepharose beads. Conditioned media from rat hepatoma (McA-RH7777) cell lines stably expressing various carboxyl-terminally truncated forms of human apoB (ranging from full-length apoB to apoB15) were applied to the r-apo(a) affinity columns; the columns were subsequently washed and eluted with epsilon-aminocaproic acid (epsilon-ACA). Specific binding was quantified by Western blot analysis of column fractions. Of the apoB truncations examined, apoB94, apoB42, apoB37, and apoB29 exhibited complete specific binding to 17K r-apo(a). Only approximately 50% binding was observed for apoB18, whereas essentially no detectable binding was observed with apoB15. In all cases, similar results were obtained when the r-apo(a) kringle IV types 5-8-Sepharose column was used. Additionally, substitution of proline for epsilon-ACA as the eluent resulted in similar column profiles with either r-apo(a) affinity column. We also demonstrated that apoB48 present in chylomicrons bound completely to the 17K column in an epsilon-ACA-dependent manner. Taken together, these results represent the first demonstration that N-terminal sequences in apoB between amino acid residues 680 (apoB15) and 781 (apoB18) are essential for noncovalent association with apo(a) and that these sequences interact with domain(s) present within apo(a) kringle IV types 5-8.

Amino Acid Sequence↗
PubMed1995

Superficial accumulation of plasminogen during plasma clot lysis.

BACKGROUND: Binding of plasminogen to partially degraded fibrin is an important step in fibrinolysis, influencing its rate and fibrin specificity. Little is known about the spatial distribution of plasminogen and of plasminogen-binding sites inside thrombi during lysis. In the present study, we investigated this problem, which is important for a better understanding of the local regulation of fibrinolysis and the rate-limiting factors of therapeutic thrombolysis. METHODS AND RESULTS: An experimental system was used that allowed continuous visualization and quantification by fluorescence microscopy of the spatial distribution of fluorescein-labeled plasminogen inside and outside model thrombi. Strong superficial accumulation of plasminogen was observed during lysis of a plasma clot induced by tissue-type or urokinase-type plasminogen activators in the surrounding plasma. A distinctly visible plasminogen-accumulating shell moved continuously with the reducing surface of the clot. The accumulation decreased in conditions of exhaustive activation of plasminogen in the outer plasma. It was found in a purified system that a thin superficial layer (approximately 50 microns wide) of a plasmin-treated fibrin clot exposes about 2.5 plasminogen-binding sites per fibrin monomer with a Kd of 2.2 mumol/L. At a physiological concentration of plasminogen (1.5 mumol/L) in the outer medium, plasminogen was concentrated about 10-fold in this layer. The binding was dose-dependently inhibited by epsilon-aminocaproic acid. CONCLUSIONS: We conclude that the generation of potent surface-associated plasminogen-binding sites during thrombolysis results in a strikingly high plasminogen concentration at the dynamically changing surface of a lysing clot. The necessity of a continuous plasminogen supply from the plasma supports the use of fibrin-specific and plasminogen-sparing agents for thrombolytic therapy.

Blood Coagulation↗
PubMed1989

Bleeding diathesis due to decreased functional activity of type 1 plasminogen activator inhibitor.

We evaluated an elderly patient with a lifelong history of severe bleeding after surgery or trauma and with evidence of persistent hyperfibrinolysis. Routine coagulation studies were normal. Serum plasminogen (40%, normal 72-128%) and alpha 2-antiplasmin (55%, normal 70-145%) activities were decreased. Euglobulin clot lysis was abnormally shortened (50 min) and normalized in vitro with epsilon-aminocaproic acid (EACA). The patient was treated with EACA with prompt cessation of bleeding. Patient tissue-plasminogen activator (t-PA) levels in serum were normal (4.7 ng/ml, control 3.5-7.2) as detected by a two-site immunoradiometric assay (IRMA). Patient fibrinolytic inhibitor activities were assessed by incubating 125I-labeled t-PA with either whole blood or serum followed by SDS-PAGE and autoradiography to identify the resultant protease/protease inhibitor complexes. In comparison to blood samples obtained from normal donors, patient plasma and serum demonstrated reduced binding of a fast-acting plasminogen activator inhibitor to 125I-labeled t-PA. Immunoprecipitation experiments indicated diminished complex formation between type 1 plasminogen activator inhibitor (PAI-1) in patient serum and 125I-labeled t-PA. Low patient PAI-1 activity was confirmed in serum (0.36 U/ml, control 0.87-1.81; n = 3) and in platelet lysates using a functional IRMA to quantitate PAI-1 binding to immobilized t-PA. However, patient serum PAI-1 antigen was within the normal range when analyzed by IRMA (31.8 ng/ml, control 19.6-42.2); this result was confirmed in both serum and platelets by Western blot (n = 3). Mixing experiments using purified PAI-1 as well as patient and control sera did not show evidence for an inhibitor against PAI-1. We conclude that this patient's bleeding diathesis was due to hyperfibrinolysis and defective PAI-1. This patient provides the first demonstration of a link between decreased in vivo PAI-1 activity and disordered hemostasis, and supports a role for PAI-1 in control of vivo fibrinolysis.

Aged↗
PubMed1993

The influence of the nature of the asparagine 289-linked oligosaccharide on the activation by urokinase and lysine binding properties of natural and recombinant human plasminogens.

Several strategies have been used to obtain recombinant (r) human plasminogens (HPg) containing different oligosaccharide side chains on its sole N-linked glycosylation site, present at Asn289. The approaches included expression of the cDNA for HPg in insect cell lines under various conditions, addition of glycosidase inhibitors during expression, and purification of specific glycoforms of HPg using affinity chromatography on an insolubilized lectin column. The activation kinetics for urokinase (UK) of each of the purified HPgs, as well as their relative abilities to bind to the ligand, epsilon-aminocaproic acid (EACA), were then determined. Removal of both N- and O-linked oligosaccharide from HPg resulted in a slight increase in the Kcat/Km for its activation, while a glycoform containing tetrasialyl-tetra-antennary complex oligosaccharide on Asn289 was a slightly poorer substrate for UK than plasma HPg, which contains bisialyl-biantennary complex carbohydrate on Asn289. The most dramatic differences were observed for HPgs with high mannose-type glycans on Asn289. (Man9GlcNAc2)-HPg possessed only approximately 6% of the kcat/Km of plasma HPg, whereas (Glc3Man9GlcNAc2)-HPg did not undergo activation at a significant rate by UK. Differences were also found in the relative abilities of the HPg glycoforms to interact with EACA. The most effective interactions were observed with HPgs containing complex-type glycans, and the least effective binding was found for HPgs with high mannose-type oligosaccharides. The full range of the binding effects is represented by a fourfold difference between HPg containing tetrasialyl-tetra-antennary glycan and HPg with (Glc3Man9GlcNAc2) assembled on Asn289. These results clearly demonstrate that the nature of the N-linked glycan assembled on HPg dramatically influences its ability to be activated by UK and to bind to omega-amino acid effector molecules.

Animals↗
PubMed1996

Fibrin deposition in tissues from endotoxin-treated mice correlates with decreases in the expression of urokinase-type but not tissue-type plasminogen activator.

The primary hypothesis of this report is that the formation and subsequent removal of fibrin in specific tissues during pathologic processes reflects temporal changes in the local expression of key procoagulant and fibrinolytic genes. To begin to test this hypothesis, we have used quantitative PCR assays and in situ hybridization analysis to examine the effects of endotoxin on the expression of specific genes in murine tissues, and to relate these changes to fibrin deposition/dissolution using immunohistochemical approaches. Endotoxin caused large increases in plasminogen activator inhibitor-1 mRNA and modest increases in tissue factor mRNA in most tissues examined. However, fibrin was only detected in the kidneys and adrenals of endotoxin-treated mice, and it was transient. Unexpectedly, changes in urokinase-type plasminogen activator mRNA but not tissue-type plasminogen activator mRNA correlated with fibrin deposition/dissolution in these tissues. Pretreatment of mice with the fibrinolytic inhibitor epsilon-aminocaproic acid before endotoxin increased both the number of fibrin-positive tissues and the duration of fibrin deposition in the kidneys and adrenals. These results suggest that the absence of fibrin in some tissues reflects ongoing local fibrinolysis, and that increases in plasminogen activator inhibitory and tissue fac- tor gene expression and decreases in urokinase-type plasminogen activator expression are necessary for tissue-specific fibrin deposition. Changes in tissue-type plasminogen activator gene expression do not appear to be essential for fibrin deposition/dissolution in this murine model of sepsis.

Adrenal Glands↗
PubMed2001

Evaluation of a new point of care heparin test for cardiopulmonary bypass: the TAS heparin management test.

Patients undergoing cardiopulmonary bypass (CPB) require anticoagulation with heparin to avoid thrombosis within the bypass circuit. The common method used to monitor the degree of anticoagulation is the activated clotting time (ACT). We evaluated a novel point of care device, the TAS (Pharmanetics, Raleigh, NC, USA) heparin management test (HMT), for its suitability in monitoring anticoagulation during CPB. In vitro analysis showed a dose-response (r2=0.988) of the HMT from 0.078-10.0 U/ml heparin, covering the range of heparin used during cardiac surgery (2-5 U/ml). Fifty randomly selected patients undergoing CPB were studied. Preheparin clotting times for these patients were 143+/-32 s for the HMT and 146+/-18 s for the ACT; 435+/-60 s HMT and 438+/-39 s ACT during CPB; 145+/-50 s HMT and 128+/-14 s ACT post-protamine (r2=0.797). epsilon-Aminocaproic acid treatment for inhibition of fibrinolysis did not affect the HMT. We conclude that the HMT correlates well with the ACT and may be useful for monitoring heparin during CPB. Advantages of the HMT are small sample volume and good sensitivity to heparin.

Anticoagulants↗
PubMed1988

Fibrin glue: a review of its preparation, efficacy, and adverse effects as a topical hemostat.

Fibrin glue is composed of two separate solutions of fibrinogen and thrombin. When mixed together, these agents mimic the last stages of the clotting cascade to form a fibrin clot. Fibrin glue is available in Europe but is not commercially available in the U.S.; therefore, investigators have extemporaneously compounded their own fibrin glue. Fibrinogen can be obtained from pooled, single-donor, and autologous blood donors and is usually isolated by the process of cryoprecipitation. The thrombin component is generally derived from commercial bovine sources. Some investigators have added calcium chloride and/or antifibrinolytics (i.e., aminocaproic acid, aprotinin) to their preparations. Fibrin glue can be applied using a double-barrel syringe or by spray application. Although fibrin glue has been used in a variety of surgical procedures, it has been especially useful in heparinized patients undergoing cardiovascular procedures requiring extracorporeal circulation, as it does not require an intact hemostatic system to be effective. Fibrin glue also has been evaluated in presealing woven or knitted Dacron vascular grafts. The major drawback to its use is the risk of transmitted serological disease from pooled and single-donor blood donors. The safest preparations use the patient's own blood to prepare fibrin glue. Overall, fibrin glue is a useful adjunct to other methods to control bleeding in selected surgical patients.

Administration, Topical↗
PubMed2004

Menorrhagia due to a qualitative deficiency of plasminogen activator inhibitor-1: case report and literature review.

A case is presented of a 26-year-old woman who was referred to the hematology clinic because of her report of a family history of plasminogen activator inhibitor-1 (PAI-1) deficiency. Since menarche, she had suffered from severe menorrhagia, but she had assumed that this was unrelated to her mother's history of repeated life-threatening bleeding. Her menorraghia was evident by using greater than 100 pads per period, bleeding as long as 4 continuous months, and even bleeding through her clothes despite using both tampons and pads. Evaluation with pelvic examination, endometrial biopsy, and pelvic ultrasound was unremarkable. Medroxyprogesterone acetate treatment for her dysfunctional uterine bleeding was unsuccessful. Laboratory evaluation revealed iron deficiency anemia but otherwise normal platelets, bleeding time, prothrombin time, activated partial thromboplastin time, and vonWillebrand's studies. Despite any preconceptions, examination for a fibrinolytic defect ultimately demonstrated a PAI-1 antigen level of 11.4 ng/mL (4.0-43 ng/mL) and PAI-1 activity less than 5 AU/mL (5-37 AU/mL) and clinically supported a diagnosis of a hereditary, qualitative PAI-1 defect. She was treated with aminocaproic acid with return to relatively normal menses. Future treatment should also prevent excessive bleeding during trauma, surgery, or childbirth. Further evaluation of this patient and her family is planned and may help elucidate the important role of PAI-1 in the complicated balance between hemostasis and hemorrhage.

Adult↗
PubMed1988

Detection of receptors for sulfated polysaccharides in human placenta by biotinylated probes.

Histochemical detection of binding sites for sulfated polysaccharides believed to be important mediators within recognitive interactions was carried out by application of biotinylated probes such as heparin, native and desulfated fucoidan, dermatan sulfate, and two types of carrageenans. The probes were derivatized by mild cyanogen bromide activation and subsequent aminoalkylation to allow incorporation of biotin, inserted with an epsilon-aminocaproic acid spacer to reduce charge-related and steric impediments. Specific labeling could be detected in different cell types of human placenta, dependent on the developmental stage. Sulfated polysaccharides bound predominantly to leucocytes in full-term placenta, whereas demonstration of specific binding sites in decidua, syncytiotrophoblasts, and cytotrophoblasts was restricted primarily to heparin and, less intensely, fucoidan, although not desulfated fucoidan. Heparin binding in the placenta after 8 weeks of gestation was reduced for epithelia that, at this stage of development, revealed carrageenan binding sites. Fucoidan binding was at this developmental stage measurable only for leucocytes. These results provide definite histochemical evidence for the presence and developmental regulation of expression of receptors for sulfated polysaccharides in different cell types of human placenta.

Binding, Competitive↗
PubMed2004

Autologous stem-cell transplantation can be performed safely without the use of blood-product support.

PURPOSE: Autologous stem-cell transplantation has been shown to be a curative procedure for a variety of leukemias and lymphomas. Most transplants require RBC and platelet support. We report the ability to perform autologous transplantation without blood-product support. SUBJECTS AND METHODS: In this study, we treated 26 patients with religious objection to blood products with autologous stem-cell support without the use of any blood products. Patients received a combination of granulocyte colony-stimulating factor (G-CSF), erythropoietin, and interleukin-11 or G-CSF alone to mobilize stem cells. Post-transplant patients received intravenous iron, erythropoietin, G-CSF, and epsilon aminocaproic acid. RESULTS: There were two major bleeding complications (8%), with two treatment-related deaths (8%). There were three minor bleeding complications (12%). The median fall in hemoglobin level was 4.7 g/dL; the median hemoglobin level 30 days after transplantation was 9.2 g/dL. The median total number of days with platelet count less than 10 x 10(9)/L was 4 days; the median days to platelet recovery greater than 20 x 10(9)/L was 12 days. CONCLUSION: Autologous stem-cell transplantation can be performed safely without the use of any blood products.

Adult↗
PubMed1991

Regulation of transepithelial electrical resistance in two-compartment Sertoli cell cultures: in vitro model of the blood-testis barrier.

The effects of FSH, testosterone (T), and incubation temperature on the development of inter-Sertoli cell (Sc) tight junctions were investigated in vitro by using repetitive measurements of transepithelial electrical resistance (TER). Control cultures developed stable TER of 100-145 omega cm2 during the initial 3-4 days of incubation at either 33 or 36.5 C, suggesting the formation of simple but continuous tight junctions. The presence of FSH (200 ng/ml) at 33 C delayed the onset of TER development by 3-5 days. The addition of FSH at the time of stable TER (day 5) resulted in a rapid (24 h) decrease of TER to 35-40 omega cm2, which returned to the control level during the subsequent 5-7 days. T alone (0.001-10 microM) caused an early and dose-dependent increase in TER to 165-240 omega cm2. In mono-layers incubated at 36.5 C, the continuous presence of FSH resulted in a dose-dependent increase in TER, which stabilized at 260-380 omega cm2 after 4-6 days. At this temperature, the addition of FSH on day 5 caused a rapid drop of TER similar to that observed at 33 C. This drop could not be prevented by antiproteases (aprotinin, epsilon-aminocaproic acid, or 10% fetal bovine serum) and was followed by an increase in TER up to 260-300-omega cm2. The Sc monolayers developed FSH-induced TER of 230-280 omega cm2 at 33 C, but only after several days of culture at 36.5 C. The effects of T at 36.5 and 33 C were similar, but the maximal TER values were significantly higher (290-380 omega cm2) at 36.5 C. The concomitant presence of T and FSH at 36.5 C resulted in the highest TER levels (580-1200 omega cm2) within 4-6 days, suggesting the synergistic effect of the two hormones on TER development. Dihydrotestosterone was more effective than T when used together with FSH, whereas estradiol had no effect. The different patterns of TER did not result from differences in Sc number or metabolic activity and probably reflected developmental and/or maturational changes in the inter-Sc tight junctions. It is concluded that FSH, T, and temperature play a role in the development of high TER by Sc monolayers (formation of tight junctions) in vitro. FSH and T appear to regulate TER via separate pathways and to cooperate by a yet unknown synergistic mechanism.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed2006

Successful intraoperative use of recombinant tissue plasminogen activator during liver transplantation complicated by massive intracardiac/pulmonary thrombosis.

During orthotopic liver transplantation a patient received epsilon-aminocaproic acid and clotting factors. Shortly after hepatic artery clamping the patient developed a massive intracardiac/intravascular thrombosis that resulted in cardiac arrest. After diagnosis by transesophageal echocardiography, the patient was treated with recombinant tissue plasminogen activator through a central venous catheter advanced into the right atrium. After treatment with recombinant tissue plasminogen activator, the patient's hemodynamic status improved, permitting the liver transplant to be completed. The patient was ultimately discharged to home. We report the successful intraoperative resuscitation of a patient with acute intracardiac/intravascular thrombosis during an orthotopic liver transplantation using thrombolytic therapy.

Female↗
PubMed1986

External pneumatic calf compression reduces deep venous thrombosis in patients with ruptured intracranial aneurysms.

We evaluated the ability of intermittent external pneumatic calf compression to prevent deep venous thrombosis after subarachnoid hemorrhage from ruptured intracranial aneurysms. Fifty-six subarachnoid hemorrhage patients not given external pneumatic calf compression were compared with 90 patients who had calf compression after their subarachnoid hemorrhages. Both groups of patients were on strict bedrest for 7 to 21 days after aneurysm rupture, and both received epsilon-aminocaproic acid, 30 to 36 g/day intravenously, until operation. The risk factors in the two groups were similar, and the nursing and medical care did not seem to differ. Of patients without external pneumatic compression, 18% had venographically proven deep venous thrombi, which contrasts with 6% of patients receiving calf compression. This was a significant difference (P less than 0.05; chi 2). These retrospective data suggest that external pneumatic calf compression helps to prevent deep venous thrombosis in patients with subarachnoid hemorrhage when delayed operation, bedrest, and antifibrinolytic agents are used.

Adult↗
PubMed1983

Neutrophil behaviour in the presence of protease inhibitors.

Neutrophil leucocytes circulate in plasma, which contains broad-spectrum antiproteases such as alpha-2-macroglobulin and alpha-1-antitrypsin, and move into environments in which antiproteases are present. Plasma antiproteases significantly reduce the adhesiveness of leucocytes in both static and dynamic adhesion assays, although their action does not seem to depend upon their anti-protease capacity. Contrary to expectation, leucocyte movement over surfaces and through both rigid and deformable three-dimensional matrices (micropore filters and collagen gels) is unaffected by antiproteases. This renders the idea that forward movement depends upon the proteolytic cleavage of redundant adhesion sites less probable. Various non-physiological antiproteases (chloromethyl ketones, soya bean trypsin inhibitor, and epsilon-aminocaproic acid are also ineffective in reducing locomotion, although they do cause minor changes in adhesiveness.

Cell Adhesion↗