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PubMed2003

Extracorporeal life support for posttraumatic acute respiratory distress syndrome at a children's medical center.

BACKGROUND: Primary traumatic injury was considered previously a contraindication for institution of extracorporeal life support because of high risk for persistent or new bleeding. Published experience in adults suggests that extracorporeal membrane oxygenation (ECMO) can successfully support trauma victims with pulmonary failure. The authors reviewed their experience with the use of ECMO in pediatric and adult trauma patients with acute respiratory distress syndrome (ARDS) at a children's medical center. METHODS: ECMO Center records from 1991 through 2001 (76 children, 8 adults) were reviewed to identify all patients with a primary or secondary ICD-9 diagnostic code of posttraumatic ARDS in addition to documented trauma. RESULTS: Five children and 3 adults with traumatic injury and ARDS received ECMO support. Seven patients were injured in motor vehicle collisions; one patient suffered a gunshot wound to the chest. Patient ages ranged from 21 months to 29 years (pediatric median, 4 years; range, 21 months to 18 years). Four patients had pre-ECMO laparotomies, including 3 who required splenectomy. Four patients had liver lacerations, 3 had pulmonary contusions, and 1 had a renal contusion. Median ventilation before ECMO was 6 days (range, 2 to 10). Seven of 8 patients were placed on venovenous (VV) ECMO. Seven patients had significant bleeding on ECMO. Patients were treated with blood product replacement, epsilon-aminocaproic acid (EACA), and aprotinin infusions. Surgical intervention was not required for bleeding. Six patients received hemofiltration. Median time on ECMO was 653 hours (range, 190 to 921 hours). Six of 8 patients overall survived (75%). Four of 5 pediatric patients survived. CONCLUSIONS: Children and adults with severe posttraumatic ARDS can be treated successfully on VV extracorporeal support. Hemorrhage occurs frequently but is manageable.

Adolescent↗
PubMed1979

Sickle cell trait: forgotten cause of hematuria in white patients.

Extensive evaluations for intermittent gross hematuria, including selective renal arteriograms, failed to reveal the etiology of bleeding in 2 whtie patients. Sickle cell preparation and hemoglobin electrophoresis, obtained as long shot tests, revealed sickle cell trait in both patients. Both patients were treated successfully with low doses of epsilon aminocaproic acid. Sickle cell prepration and hemoglobin electrophoresis should be included in the evaluation of every patient, white or black, with unexplained hematuria.

Adult↗
PubMed2002

Evaluation of progesterone-ovalbumin conjugates with different length linkers in enzyme-linked immunosorbant assay and surface plasmon resonance-based immunoassay.

A series of progesterone-4-ovalbumin (OVA) conjugates with different length linkers (4-, 11-, and 18-atoms long) were synthesized by successive aminocaproic acid homologation of 3-(pregn-4-ene-3,20-dione-4-yl)thiopropanoic acid (1) before conjugation to ovalbumin. The performance studies of these progesterone-4-ovalbumin conjugates showed that the effects of the length of linker on the antibody binding are dependent upon different immunoassay formats. In a rapid flow biosensor surface, on a BIAcore Surface Plasmon Resonance (SPR) instrument, antibody-binding capacities and response rate were dramatically increased for progesterone-4-ovalbumin conjugates when the length of the linker was incremented from 4 atoms to 11 or 18 atoms. Thus, highly sensitive SPR-based immunoassays for progesterone over a range of 0.1-50 ng ml(-1) were developed using biosensor surfaces immobilized with progesterone-ovalbumin conjugates having extended linkers. The SPR-based assays were fully competitive with conventional enzyme-linked immunosorbant assay (ELISA) but much more rapid and simple. However, there were little changes in antibody-binding performance using a conventional ELISA for the same conjugates. The progesterone-4-ovalbumin conjugate (1-OVA) had better antibody binding than its progesterone-7alpha-ovalbumin analog (2-OVA) in the SPR-based assay, but with a conventional ELISA there was no significant difference between these two isomeric conjugates.

Carboxylic Acids↗
PubMed1987

Physiologic regulation and pathologic disorders of fibrinolysis.

Physiologic fibrinolysis is a reparative process that occurs in response to hemostatic plug or thrombus formation. The final enzymatic step, fibrin proteolysis, results from a coordinated interaction of enzymes and inhibitors, which produces effective action at the site of the disease and spares the proteins of the blood or uninvolved parts of the vascular system. The agent of fibrinolysis, the enzyme plasmin, is derived from its zymogen (plasminogen) through limited proteolysis effected by plasminogen activators. They can be grouped according to functional and immunologic properties into the tissue type and urokinase-like plasminogen activators. The ability of alpha 2 antiplasmin to neutralize efficiently free (nonfibrin-bound) plasmin prevents inappropriate systemic activation of fibrinolysis. This control is superseded in certain conditions, such as with the therapeutic administration of plasminogen activators to lyse pathologic thrombi, when plasmin degrades plasma fibrinogen into degradation fragments (X, Y, D, and E). Degradation of cross-linked fibrin results in distinctive products that are characterized by cross-linked (factor XIIIa-induced) derivatives such as D dimer. Disease states resulting from abnormalities in the fibrinolytic system include both hemorrhagic disorders, resulting from excessive fibrinolysis, and thrombosis, as the result of deficient fibrinolysis. Hyperfibrinolysis can result from pharmacologic administration of activators or from defective inhibition produced by alpha 2 antiplasmin deficiency. Hypofibrinolytic thrombosis can result from hereditary defects, for instance of plasminogen or fibrinogen, or from pharmacologic inhibition of fibrinolysis such as with epsilon aminocaproic acid. Laboratory evaluation of fibrinolysis is useful for monitoring fibrinolytic therapy and assessing thrombotic disorders and bleeding; it also includes the specific measurements of plasminogen activator, plasminogen, plasmin, inhibitors and circulating fibrinogen, and cross-linked fibrin degradation products.

Fibrin Fibrinogen Degradation Products↗
PubMed2002

Effect of a synthetic carboxy-terminal peptide of alpha(2)-antiplasmin on urokinase-induced fibrinolysis.

alpha(2)-Antiplasmin (alpha(2)AP) interferes with the binding of plasminogen to fibrin because lysine residues in its carboxy-terminal region compete with those in fibrin, presumably the same way that free lysine or epsilon-aminocaproic acid (EACA) inhibits plasminogen binding to fibrin. While this overall process causes an inhibition of fibrinolysis, the converse was observed with a 26-residue synthetic peptide (AP26) corresponding to the carboxy-terminal region of alpha(2)AP. The AP26 peptide, in fact, accelerated urokinase-induced lysis of (1) fully crosslinked fibrin with complete gamma-dimer and alpha-polymer formation; (2) partially crosslinked fibrin that had undergone only gamma-dimerization; and (3) noncrosslinked fibrin. The AP26 peptide also inhibited factor XIIIa-catalyzed crosslinking of fibrin alpha-chains, and this also accelerated lysis of fibrin. EACA had no effect. In the presence of noncrosslinked fibrin, AP26 promoted plasminogen activation by urokinase and fibrinolysis. EACA only slightly increased the rate of plasminogen activation, and as expected, it inhibited fibrinolysis. Since AP26 peptide enhanced the lysis of partially crosslinked and noncrosslinked fibrin, our results indicate that inhibition of factor XIIIa-catalyzed alpha-polymer formation by AP26, although associated with accelerated fibrinolysis, is not the primary mechanism. Instead, our data support the conclusion that AP26 enhances the conversion of plasminogen to plasmin approximately 5-fold, probably by inducing a conformational change in plasminogen structure just as occurs with low concentrations of lysine or EACA. At higher concentrations, however, AP26 apparently does not approach the avidity or affinity of lysine or EACA for the kringle structures of plasminogen or plasmin so that their binding to fibrin is blocked. Whether AP26 alone, or as part of another molecule, could have potential for enhancing thrombolysis will require further study.

Cross-Linking Reagents↗
PubMed1997

Thrombolysis enhancing activity of a low molecular weight dermatan sulfate (Desmin 370) in experimental pulmonary embolism in rats.

The effect of Desmin 370 (D370), a low molecular weight dermatan sulfate, on the extent of lysis of radiolabelled pulmonary emboli in rats was evaluated. 125I-fibrin labelled blood clots were embolized into the lungs via a jugular vein, and the degree of lysis was calculated, at predetermined intervals, by the residual radioactivity in the lungs. A single i.v. injection of D370 (50 mg/kg) caused a significant increase in the rate of lysis, which was visible at 30 min and persisted for the whole experimental period (2 h). This effect was prevented by epsilon-aminocaproic acid (1 g/kg). At comparable antithrombotic dosages, heparin (2 mg/kg) also produced a significant enhancement of thrombolysis while hirudin (2 mg/kg) was totally ineffective. Heparin, however, produced a much more pronounced anticoagulant effect than D370. No changes in the plasma levels of plasminogen activator and plasminogen activator inhibitor activities were observed after treatment with D370. Moreover, the dermatan sulfate failed to enhance the blood fibrinolytic activity measured by a solid phase 125I-fibrin assay. These results extend previous data indicating that D370 may be efficient also in the therapy of thrombosis and provide direct evidence that this effect occurs, at least in part, via degradation of thrombus associated fibrin.

Animals↗
PubMed2000

The potential mechanism for the effect of heparin on tissue plasminogen activator-mediated plasminogen activation.

The effects and possible role of heparin on tissue plasminogen activator-mediated plasminogen activation was thoroughly investigated. Direct analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated that heparin increased the conversion of plasminogen to plasmin. Experiments by fluorescence quenching suggested that the stimulation of tissue plasminogen activator activity probably was due to a direct binding of heparin to tissue plasminogen activator, causing a conformational change of tissue plasminogen activator and rendering it more accessible to plasminogen interaction. The absence of additive stimulation effects on tissue plasminogen activator-mediated plasminogen activation when both heparin and fibrinogen were present also implied that both compounds interacted with tissue plasminogen activator via the same domain; it appeared to be most likely via the kringle-2 domain in tissue plasminogen activator based on studies using epsilon-aminocaproic acid as an inhibitor. Unlike heparin-induced stimulation of antithrombin-thrombin interaction, the heparin-induced stimulation of tissue plasminogen activator did not seem to follow a template model. Only in the presence of a high plasminogen or a low tissue plasminogen activator concentration, massive stimulation of tissue plasminogen activator activity was observed via a pseudotemplate model. The results suggest that precautions concerning high heparin dose should be given during its conjunctive clinical use with tissue plasminogen activator in thrombolytic therapy to reduce the risk of hemorrhage.

Binding Sites↗
PubMed2000

Interaction of Leishmania mexicana promastigotes with the plasminogen-plasmin system.

The binding of human plasminogen and plasmin to the promastigote form of Leishmania mexicana was investigated. L. mexicana was capable to bind both molecules, the binding being inhibited by epsilon-aminocaproic acid. Scatchard plot analysis revealed a dissociation constant (Kd) value of 2.4+/-0.8 microM and 0.9+/-0.1 x 10(4) binding sites per cell for plasminogen and a Kd value of 1.2+/-0.4 microM and 1.6+/-0.2 x 10(5) binding sites per cell for plasmin. C-terminal lysine residues are involved in plasminogen binding to cells, since carboxypeptidase B treatment reduced this binding by 34%. Ligand blotting analysis showed a group of proteins, with molecular masses between 105 and 115 kDa, capable to interact with plasminogen. Zymogram analysis showed that the protease activity acquired by L. mexicana, due to the interaction with either plasminogen or plasmin, comprises an important fraction of the total protease activity at pH 7.7. Plasminogen activation by tissue-type plasminogen activator (t-PA) was enhanced by the presence of L. mexicana promastigotes. These results raise the question whether the interaction of L. mexicana with components of the fibrinolytic system is involved in the virulence of the parasite.

Animals↗
PubMed1999

Purification and characterization of a new enzyme, N-alkylglycine oxidase from Cladosporium sp. G-10.

A new enzyme, N-alkylglycine oxidase, was isolated from a soil mold, Cladosporium sp. G-10. This protein, which was purified to near homogeneity by ammonium sulfate precipitation followed by successive column chromatography on phenyl-Sepharose, DEAE-Sepharose and Sephadex G-200, was a single polypeptide with a molecular mass of 52,000. In the presence of O2 and H2O, this enzyme acted on some N-alkylglycine derivatives, such as N epsilon-carboxymethyllysine, N-carboxymethyl-6-aminocaproic acid, sarcosine and N-ethylglycine, and produced corresponding N-alkylamine, glyoxylic acid and H2O2. This enzyme had optimum activity at 30 degrees C, pH 8-10, and was most inhibited by ZnSO4, pCMB, iodoacetic acid, and SDS.

Amino Acid Oxidoreductases↗
PubMed1987

Treatment of depressed cutaneous scars with gelatin matrix implant: a multicenter study.

Twenty-two centers participated in a study to determine the efficacy and safety of gelatin matrix implant (GMI; Fibrel) in the elevation of depressed cutaneous scars. Gelatin matrix implant is an implant consisting of absorbable gelatin powder and epsilon-aminocaproic acid, which is reconstituted with the patient's plasma before being injected intradermally beneath the scar. A total of 321 patients were evaluated after a skin sensitivity test; six of the patients (1.9%) had a positive response. After a skin test with negative results, 27 patients dropped out of the study for unrelated reasons. The remaining 288 patients were treated with the implant (total of 840 scars), many of whom have been followed up for more than 1 year. Preliminary results show that approximately half of the treated scars showed improvement of greater than 65%. The current data suggest that the improvement lasts at least up to 1 year. Adverse reactions to gelatin matrix implant injections were local and transient, and none of the patients developed major hypersensitivity responses to the treatment. The data indicate that intradermal injections of gelatin matrix implant are safe and effective in correcting the depressed scars selected for this study.

Cicatrix↗
PubMed1982

Is the formation of fibrin a necessary event for the initiation of angiogenic responses in the chick chorioallantoic membrane?

Millipore filters belong to number of solid materials which interact with the chorioallantoic membrane (CAM) and frequently initiate local edemas sometimes accompanied by vascular responses. We observed that such reactions can completely be prevented by coating Millipore filter pieces with hydrophilic polymers (e.g. polyvinylpyrrolidone dextran) or by hydrophobic substances as liquid paraffin and vaseline. Protease inhibitors (Contrikal, epsilon-aminocaproic acid) did not prevent such reactions but increased the incidence of vascular responses. By assaying several blood components we found a relationship between the initiation of vascular responses in the CAM and the process of blood clotting. If small amounts (5 to 10 microliter) of citrated bovine or human plasma arae dropped on the CAM angiogenic responses occur as good as regularly. They are also initiated if the plasmas are recalified and small fibrin fragments are placed on the CAM. Chicken plasma, however, regularly induced such responses only in combination with bovine serum or following application of (or treatment with) fibrinolysis inhibitors. We conclude that the formation of a stable extravascular plasma clot with reduced susceptibility to fibrinolysis could be the most important precondition for the initiation of vascular responses, and that all materials, substances or biofactors capable of activating the clotting cascade should also have the capacity to induce angiogenic responses.

Allantois↗
PubMed2000

Affinity chromatography for purification of two urokinases from human urine.

A new affinity chromatography (hydrophobic-mediated affinity chromatography), which was characterized by the matrix having both affinity site to urokinase and hydrophobic site, was established for the purification of urokinase from human urine. The hydrophobic affinity matrix (tentatively named PAS in the text) was prepared by immobilizing 6-aminocaproic acid on Sepharose CL-6B, followed by a coupling p-aminobenzamidine to a part of the hydrophobic site on the matrix. The PAS matrix was applied to the purification of urokinase from human urine, and high- and low-molecular weight pure urokinases were efficiently obtained in high yield by the present method.

Chromatography, Affinity↗
PubMed1984

Determination of glycosylated haemoglobin by isoelectric focusing in non-linear pH gradients.

A new isoelectric focusing technique for the separation and quantitation of glycosylated haemoglobin (HbA1c) is described. By using an equimolar mixture of two separators (0.2 M beta-alanine + 0.2 M 6-aminocaproic acid) a 2-pH unit Ampholine range (pH 6-8) is transformed in a shallow, 0.6-pH unit span (pH 6.7-7.3). This brings about an increment of resolution between HbA and HbA1c by a factor of about three, thus allowing proper densitometric evaluation of the trichloroacetic acid-fixed MetHb bands by conventional gel scanners. Excellent agreement is found among microchromatography, isoelectric focusing followed by densitometry in situ, and isoelectric focusing followed by band excision, elution and spectrophotometric determination. The present method also allows full resolution between HbA1c and fetal haemoglobins (F and Fac bands).

Adult↗
PubMed2003

Chiral separation of dioxopromethazine in eye drops by CZE with charged cyclodextrin.

Capillary zone electrophoresis (CZE) with carboxyethyl-beta-cyclodextrin (CE-beta-CD) dissolved in the operating buffer was used for the separation and determination of enantiomers of phenothiazine antihistaminic, dioxopromethazine, in commercial pharmaceutical preparation, eye drops. This chiral selector, negatively charged under given separating conditions (20 mmol/l epsilon -aminocaproic acid, acetic acid, pH 4.5), was effective in enantioresolution of the antihistamine even at its low concentrations (3-6 mg/ml) in the buffer solution. CZE identification and quantitation of the relevant constituents present in the preparation (dioxopromethazine enantiomers, phenylephrine) were based on the response of photometric absorbency detector, operating at a 275 nm detection wavelength. Changes in pH, type and concentration of chiral selector were studied in relation to chiral resolution. Acceptable validation criteria for sensitivity, precision, linearity and repeatability are included.

Cyclodextrins↗
PubMed2004

Domain-dependent action of urokinase on smooth muscle cell responses.

BACKGROUND: Single-chain urokinase-type plasminogen activator (sc-uPA) is one of the key serine proteases involved in modulating cellular and extracellular matrix responses during tissue remodeling. Sc-uPA is composed of three domains: aminoterminal fragment (ATF), kringle domain, and carboxyterminal fragment (CTF). sc-uPA is readily cleaved into these three domain fragments in vitro, each of which is biologically active; however, their roles in the microenvironment of the vessel wall are poorly understood. PURPOSE: The purpose of this study was to determine the role of each domain of sc-uPA on vascular smooth muscle cell (SMC) proliferation and migration. METHODS: SMCs were cultured in vitro. Assays of DNA synthesis, cell proliferation, and migration were performed in response to sc-uPA, ATF, kringle, and CTF in the presence and absence of the plasmin inhibitors epsilon-aminocaproic acid (EACA) and aprotinin, the Galphai inhibitor pertussis toxin, and the mitogen-activated protein kinase 1 (the upstream regulator of the extracellular-signal regulated kinase [ERK]) inhibitor PD98059. RESULTS: sc-uPA produced dose-dependent increases in DNA synthesis and cell proliferation. These responses were dependent on the CTF domain and were sensitive to plasmin inhibitors, pertussis toxin, and PD98059. Sc-uPA also induced SMC migration, which could be elicited by both ATF and kringle. Migration to sc-uPA, ATF, and kringle was both pertussis toxin and PD98059 sensitive, but importantly was plasmin-independent. CONCLUSION: sc-uPA induces SMC proliferation and migration, which are domain-dependent and mediated in part by Galphai-linked, ERK-dependent processes, while only the mitogenic response is protease dependent. These findings suggest that migration is linked to a G-protein coupled nonprotease receptor, while proliferation is associated with a G-protein coupled protease receptor.

Animals↗
PubMed1987

Coronary artery bypass grafting within 24 hours after intracoronary streptokinase thrombolysis.

Little specific information currently exists describing the management of patients with an evolving acute myocardial infarction (AMI) treated with direct intracoronary infusion of streptokinase (SK) followed by emergency coronary artery bypass grafting (CABG). A total of 194 patients with an evolving AMI underwent emergency coronary artery angiography with infusion of SK. Thirty-four of these patients with partial restoration of orthograde blood flow in the infarct-related coronary artery (as determined by clinical and objective evidence of myocardial salvage) were referred for emergency CABG. Problems related to the surgical and anesthetic care of these high-risk patients involved: (1) management of resuscitation of patients with AMI, (2) SK-induced coagulopathy and ongoing thrombolysis, and (3) timely CABG to preserve myocardial salvage. To highlight comparisons of SK-CABG management, data regarding 34 consecutive patients having routine non-SK-CABG surgery were collected simultaneously during the study. Data collected retrospectively included: anesthetic drug summaries, time frame of events from admission to the emergency room until commencing bypass, use of invasive monitoring and hemodynamic assist devices, induction complications, operative complications, coagulation derangements, volume replacement, and blood loss. Results revealed no deaths up to 24 hours postoperatively in the 34 emergency SK-CABG patients, even though complications were frequent intraoperatively. Furthermore, there were no statistically significant differences in SK patients v non-SK patients in blood lost, banked blood and cell saver blood administered, or platelet transfusions. However, in comparison to the non-SK-CABG patients, the SK patients received significantly larger amounts of fresh frozen plasma, cryoprecipitate, and aminocaproic acid.

Aged↗
PubMed1998

Severe urticaria and pregnancy: use of the Internet to aid management.

A case of severe urticaria complicating pregnancy is described. Advice was sought and received from experts in the condition, using the Internet to exchange information. Epsilon-aminocaproic acid (EACA) was used with no apparent adverse effects. This case report highlights some of the problems of management of thi rare condition in pregnancy and obstetric anaesthesia, and the potential benefit of the Internet and its user groups.

Journal Article↗