Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “PLASMINOGEN”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,405 records · Page 78Linked to original sources
PubMed2001

Deficiency of urokinase-type plasminogen activator-mediated plasmin generation impairs vascular remodeling during hypoxia-induced pulmonary hypertension in mice.

BACKGROUND: Chronic hypoxia results in the development of pulmonary hypertension and subsequent right heart failure. A role of the plasminogen system in the pathogenesis of pulmonary hypertension and pulmonary vascular remodeling has been suggested. METHODS AND RESULTS: Mice with targeted deficiency of the gene encoding tissue-type plasminogen activator (t-PA(-/-)), urokinase-type plasminogen activator (u-PA(-/-)), u-PA receptor (u-PAR(-/-)), or plasminogen (plg(-/-)) were subjected to hypoxic conditions. Hypoxia caused a significant 2.5-fold rise in right ventricular pressure in wild-type mice. Deficiency of u-PA or plasminogen prevented this increase in right ventricular pressure, t-PA(-/-) mice showed changes that were fully comparable with wild-type mice, and u-PAR(-/-) mice showed a partial response. Hypoxia induced an increase in smooth muscle cells within pulmonary arterial walls and a vascular rarefaction in the lungs of wild-type but not of u-PA(-/-) or plg(-/-) mice. Elastic lamina fragmentation, observed in hypoxic wild-type but not in u-PA or plasminogen-deficient mice, suggested that proliferation of vascular smooth muscle cells was dependent on u-PA-mediated elastic membrane degradation. Hypoxia-induced right ventricular remodeling in wild-type mice, characterized by cardiomyocyte hypertrophy and increased collagen contents, was not seen in u-PA(-/-) and plg(-/-) mice. CONCLUSIONS: Loss of the u-PA or plasminogen gene protects against the development of hypoxia-induced pulmonary hypertension and pulmonary vascular remodeling. These observations point to an essential role of u-PA-mediated plasmin generation in the adaptive response to chronic hypoxia and the occurrence of hypoxic pulmonary vascular disease.

Animals↗
PubMed1986

Activation of plasminogen by pro-urokinase. I. Mechanism.

The mechanism of the activation of plasminogen by recombinant pro-urokinase (Rec-pro-UK), obtained by expression of the human pro-urokinase gene in Escherichia coli, was investigated in purified systems. In mixtures of Rec-pro-UK and plasminogen, both active urokinase and plasmin are quickly generated. Addition of plasmin inhibitors (aprotinin or alpha 2-antiplasmin) abolishes the conversion of Rec-pro-UK to urokinase but not the activation of plasminogen to plasmin, suggesting that Rec-pro-UK activates plasminogen directly. Human plasma competitively inhibits the activation of plasminogen by pro-urokinase with a Ki of 0.2% (v/v). This explains the relative stability of Rec-pro-UK in plasma and the lack of activation of the plasma fibrinolytic system in the absence of fibrin. The competitive inhibition by plasma is abolished by the addition of CNBr-digested fibrinogen although Rec-pro-UK has no specific affinity for fibrin. These findings suggest that the fibrin specificity of the activation of plasminogen by pro-urokinase is due to neutralization by fibrin of the competitive inhibition exerted by plasma and not to fibrin-enhanced activation of plasminogen.

Escherichia coli↗
PubMed1983

Plasminogen activator in normal and tumor-bearing mice.

The plasminogen activator levels of a series of murine tumors commonly used in cancer drug screening were determined and compared to the levels found in normal mouse tissues. Tumors high in plasminogen activator included the B16 and colon 26. The Lewis lung and M5076 carcinoma showed an intermediate level of activity, while the plasminogen activator activity in the L1210 leukemia and colon 38 was barely elevated above background. The specific activity of the enzyme (per micrograms protein) in extracts of B16 and colon 26 was three or four times higher than in the most active normal organs surveyed (kidney, lung, brain and intestine). The high level of plasminogen activator activity measured in extracts of the B16 tumor was reflected in a substantial elevation of the levels of fibrin degradation products in the serum of mice carrying this tumor. This result suggests that the tumor-associated plasminogen activator activity is less subject to inhibitory controls in vivo than is the plasminogen activator of most normal tissues, since the total mass of the tumor was far less than the total mass of the fibrinolytically active tissues, and yet the bulk of the fibrin degradation products were caused by the tumor. We conclude that the high levels of plasminogen activator activity which are observed in many human tumors are found only in some of the transplantable murine tumors. Since this enzyme is active at an increased level in vivo in mice carrying the B16 tumor, plasminogen activator may be a suitable target for selective, enzyme-activated chemotherapy with this tumor test system.

Animals↗
PubMed2001

Purification of follicular regulatory protein: possible plasminogen identity.

A partially purified protein (the SR fraction) of porcine and human origin has been extensively characterized as Follicular Regulatory Protein (FRP). In the current study, 1A8D5, one of several monoclonal antibodies raised against FRP, was used to further purify the protein. The monoclonal antibody cross-reacted only with porcine plasminogen, a key fibrinolytic proenzyme. A commercial polyclonal antibody for human plasminogen confirmed the relationship between plasminogen and bands of the SR fraction of the porcine follicular fluid. Sequencing of the N-terminal amino acids (54 kd) of the SR fraction indicated that it shared 100% identity with the short form of porcine plasminogen chain A and 93% identity to human plasminogen. Moreover, we demonstrated that this purified protein from human follicular fluid inhibited aromatase activity of granulosa cells, a key biological property of FRP. Given that plasminogen possesses most of the proposed properties of the protein termed FRP, we conclude that FRP is likely plasminogen itself or a plasminogen-related protein and not a novel protein.

Amino Acid Sequence↗
PubMed2002

Specificity role of the streptokinase C-terminal domain in plasminogen activation.

Several pathogenic bacteria secrete plasminogen activator proteins. Streptokinase (SKe) produced by Streptococcus equisimilis and staphylokinase secreted from Staphylococcus aureus are human plasminogen activators and streptokinase (SKu), produced by Streptococcus uberis, is a bovine plasminogen activator. Thus, the fusion proteins among these activators can explain the function of each domain of SKe. Replacement of the SKalpha domain with staphylokinase donated the staphylokinase-like activation activity to SKe, and the SKbetagamma domain played a role of nonproteolytic activation of plasminogen. Recombinant SKu also activated human plasminogen by staphylokinase-like activation mode. Because SKu has homology with SKe, the bovine plasminogen activation activities of SKe fragments were checked. SKebetagamma among them had activation activity with bovine plasminogen. This means that the C-terminal domain (gamma-domain) of streptokinase determines plasminogen species necessary for activation and converses the ability of substrate recognition to human species.

Animals↗
PubMed2007

Plasminogen and angiostatin interact with heat shock proteins.

Previous studies from this laboratory have demonstrated that plasminogen and angiostatin bind to endothelial cell (EC) surface-associated actin via their kringles in a specific manner. Heat shock proteins (hsps) like hsp 27 are constitutively expressed by vascular ECs and regulate actin polymerization, cell growth, and migration. Since many hsps have also been found to be highly abundant on cell surfaces and there is evidence that bacterial surface hsps may interact with human plasminogen, the purpose of this study was to determine whether human plasminogen and angiostatin would interact with human hsps. ELISAs were developed in our laboratory to assess these interactions. It was observed that plasminogen bound to hsps 27, 60, and 70. In all cases, binding was inhibited (85-90%) by excess (50 mM) lysine indicating kringle involvement. Angiostatin predominantly bound to hsp 27 and to hsp 70 in a concentration- and kringle-dependent manner. As observed previously for actin, there was concentration-dependent inhibition of angiostatin's interaction with hsp 27 by plasminogen. In addition, 30-fold molar excess actin inhibited (up to 50%), the interaction of plasminogen with all hsps. However, 30-fold molar excess actin could only inhibit the interaction of angiostatin with hsp 27 by 15-20%. Collectively, these data indicate that (i) while plasminogen interacts specifically with hsp 27, 60, and 70, angiostatin interacts predominantly with hsp 27 and to some extent with hsp 70; (ii) plasminogen only partially displaces angiostatin's binding to hsp 27 and (iii) actin only partially displaces plasminogen/angiostatin binding to hsps. It is conceivable therefore that surface-associated hsps could mediate the binding of these ligands to cells like ECs.

Actins↗
PubMed1975

The relevance of the structure of lysine bound to Sepharose for the affinity of rabbit plasminogen;.

The features of the structure of lysine, linked to Sepharose by the alpha-amino group, which are important for affinity chromatography of rabbit plasminogem were studied. Nine lysine and lysine-like conjugates, including epsilon-aminohexanoic acid DL-norleucine, DL-alpha-aminoadipic acid, DL-alpha-epsilon-diaminopimelic acid, cadaverine L-ornithine, L-arginine and D-lysine, were prepared; Using labelled rabbit plasminogen added to plasma, the ability of each conjugate to absorb plasminogen and separate the allomeric forms, type I and type II, during epsilon-aminohexanoic acid gradient elution was compared to Sepharose-L-lysine. Plasminogen had no affinity for Sepharose-epsilon-aminohexanoic acid, and was only weakly attracted by Sepharose-norleucine, Sepharose-cadaverine and others. Sepharose-ornithine held a greater attraction to the protein but the strongest binding was obtained with Sepharose-arginine. The affinity of plasminogen type I was always less than type II for the Sepharose-lysine analogues and the recovery of type II greater than type I from Sepharose-ornithine and Sepharose-arginine. Plasminogen affinity was in the order of Sepharose-arginine greater than Sepharose-lysine greater than Sepharose-ornithine. However, because of the present difficulty in recovering plasminogen from Sepharose-arginine the use of Sepharose-lysine in the affinity chromatography of rabbit plasminogen remains unchallenged. It is concluded that binding of rabbit plasminogen to conjugates of lysine and its analogues is determined by the presence of both a free carboxyl and a free amino group and that the distance between these groups is critical.

Animals↗
PubMed1985

Detection of granuloma-associated plasminogen activator in experimental murine schistosomiasis.

Hypersensitivity granulomas induced by infection with Schistosoma mansoni were isolated from the livers of BALB/c mice after 7, 8, 10, and 12 weeks. The parasite egg-granulomas were sequentially extracted with a Tris-buffered saline (soluble fraction) and 2 M KSCN (bound fraction). Fibrinolytic enzyme activity measured with both synthetic substrates and fibrin plates demonstrated an elevated level of plasminogen activator activity in the bound fraction 7-8 weeks after infection when mature granulomas first began to appear, followed by a gradual decrease 10-12 weeks after infection. An electrophoretic enzymography technique revealed multiple molecular species of plasminogen activator at Mr = 95K, 74K, 60K, 45K, and 24K. The bands with Mr = 45K and 24K were found compatible with the electrophoretic pattern of macrophage-plasminogen activator. When the granulomas reached maximum size after 10 to 12 weeks, the plasminogen activator with 45K and 24K diminished, while plasminogen activator activity at Mr = 95K, 74K, and 60K remained unchanged suggesting the presence of both vascular and tissue types of plasminogen activators. There was no urokinase-type plasminogen activator detectable in granulomas at any time. In the soluble fraction no enzymatic activity was found, whereas regulating inhibitor activity for plasminogen activator was consistently detectable.

Animals↗
PubMed1985

Fibrinolysis and plasminogen concentration in aortic intima in relation to death following myocardial infarction.

In samples of human aortic intima fibrin/fibrinogen degradation products (FDP) were assayed by isoelectric focussing/immunoelectrophoresis as a possible measure of endogenous fibrinolysis, and plasminogen concentration was assayed by rocket immunoelectrophoresis as a possible marker for fibrinolytic potential. No consistent differences were found between normal intima and different types of atherosclerotic lesion, but there was marked variation between patients, and multiple samples from the same aorta showed similar levels. There was no significant correlation with age, sex, or time after death. Low concentrations of FDP and failure to recover measureable amounts of plasminogen from intima were highly associated with death in patients who had suffered a recent myocardial infarction. In aortas from which 3 or more samples of intima and lesions were obtained (n = 16), no FDP were found in 3 (total of 12 samples); all of these were from patients who died following myocardial infarction. Low levels were present in the 4th patient with myocardial infarction. No plasminogen was found in 10 of 11 aortas from patients dying after myocardial infarction (total of 46 samples with no plasminogen), but it was present in 10 of 17 aortas from patients dying of other causes (X2 = 7.6, P less than 0.01). Where both were assayed, FDP were not found in any samples which did not contain plasminogen. Low levels of FDP and absence of plasminogen were associated with increased involvement with atherosclerosis. There was no relation between intimal and serum plasminogen levels, and prothrombin and low density lipoprotein were present in all samples from which no plasminogen was recovered. The results indicate that in some patients, particularly those dying after myocardial infarction, there is decreased fibrinolysis and fibrinolytic potential in the arterial intima, and this may result in increased intimal accumulation of fibrin.

Adult↗
PubMed1987

Mini-plasminogen like molecule in septic patients.

Plasma from 7 septic patients with positive blood cultures were studied. None of them presented either clinical or laboratory evidence of Disseminated Intravascular Coagulation. The white cells count varied between 5 and 45 X 10(9)/l. In plasma functional plasminogen levels varied between 25 and 45%, while those of alpha 2-antiplasmin were normal (80-105%). The levels of elastase ranged between 250 and 750 micrograms/ml. Leukocyte elastase digests plasminogen "in vitro" and is able to produce several fragments; one of them called mini-plasminogen lacking lysine binding sites; therefore it does not bind to lysine-Sepharose 4B. Two different behaviors were observed in the plasmatic plasminogen of these patients with respect to their binding capacity to lysine-Sepharose 4 B. 3 patients had plasminogen which did not bind to lysine-Sepharose 4 B; the other 4 had two different components, one of which bound to lysine-Sepharose 4 B and another one which did not bind. Previous studies "in vitro" have shown that leukocyte elastase modifies alpha 2-antiplasmin, initially producing a non-plasminogen binding form. A free alpha 2-antiplasmin (non-plasminogen binding form) was detected in the plasma of these patients with sepsis by crossed immunoelectrophoresis with plasminogen in the first dimension. It seems tenable that high levels of leukocyte elastase could be responsible for these findings although, the possible relationships to leukocyte elastase still remain to be proven but could possibly explain this effect.

Blood Proteins↗
PubMed1992

The compact domain conformation of human Glu-plasminogen in solution.

A complete understanding of the accelerating mechanisms of plasminogen activation and fibrinolysis necessarily requires structural information on the conformational forms of plasminogen. Given the absence of high-resolution structural data on plasminogen the use of lower resolution approaches has been adopted. Two such approaches have previously indicated a compact conformation of Glu-plasminogen (Tranqui, L., Prandini, M., and Chapel, A. (1979) Biol. Cellulaire, 34, 39-42; Bányai, L. and Patthy, L. (1985) Biochim. Biophys. Acta, 832, 224-227) whereas a third has suggested a fairly extended conformation (Mangel, W., Lin, B. and Ramakrishnan, V. (1990) Science, 248, 69-73). Native Glu-plasminogen has been investigated using small-angle X-ray scattering (SAXS) experiments. It is concluded that this molecule in solution is compact (radius of gyration, RG 3.05 +/- 0.02 nm and maximum intramolecular distance, Im 9.1 +/- 0.3 nm) and that the data are consistent with the right-handed spiral structure observed using electron microscopy by Tranqui et al. (1979). A spiral structure of native plasminogen would have important implications for the conformational response of plasminogen to fibrin and concomitant stimulation of plasminogen activation.

Computer Simulation↗
PubMed1990

Modulation of plasminogen activator production by interleukin 1: differential responses of fibroblasts derived from human skin and rheumatoid and non-rheumatoid synovium.

Rheumatoid synovial fibroblasts were treated with purified porcine interleukin 1 alpha and recombinant human interleukin 1B, and the production of secreted and cell-associated plasminogen activator activity was measured. No stimulation of plasminogen activator activity was seen in response to either preparation of interleukin 1, and in more than half of the cell cultures interleukin 1 caused a significant decrease in the secreted levels of PA activity. Increased levels of prostaglandin E were produced in the same experiments, indicating that the cells were responsive to the interleukin 1 preparations. Both retinoic acid and unfractionated monocyte conditioned medium were able to stimulate the production of PA activity by the rheumatoid synovial fibroblast cultures. The rheumatoid synovial fibroblasts produced two species of plasminogen activator as indicated by SDS polyacrylamide gel electrophoresis, with apparent Mr of approx. 50,000 and 100,000. The Mr = 50,000 species co-migrates with urokinase-type plasminogen activator. No species is produced which co-migrates with tissue type plasminogen activator. Studies with antibodies also indicate that the activity produced is urokinase-type plasminogen activator. The Mr = 100,000 species may be an enzyme-inhibitor complex. Two non-rheumatoid synovial fibroblast cultures and two out of six human skin fibroblast cultures did produce elevated levels of plasminogen activator activity in response to recombinant human interleukin 1B. The results suggest that fibroblast populations may differ in their response to interleukin 1, in terms of production of plasminogen activator activity.

Arthritis, Rheumatoid↗
PubMed1983

Serum-dependent induction of plasminogen activator in human fibroblasts by catecholamines and comparison with the effects of prostaglandin E1.

Human foreskin fibroblasts produce the protease plasminogen activator, as shown by the ability of cell extracts to lyse 125I-labelled fibrin in the presence of plasminogen. Cellular plasminogen activator was stimulated up to 3-fold by 0.01-10 microM epinephrine, norepinephrine, or isoproterenol. Increases in plasminogen activator were slow in onset (24 h) and long-lived (greater than 48 h), and were abolished by 10 micrograms/ml of cycloheximide or 1 microgram/ml of actinomycin D, suggesting de novo synthesis of the protease. Stimulation of plasminogen activator by catecholamines was inhibited by 10 microM propranolol but not by 10 microM phentolamine, suggesting the involvement of beta-adrenergic receptors. Catecholamines stimulated plasminogen activator only in the presence of fetal bovine serum; under serum-free conditions they were inhibitory. Serum did not appear to alter the uptake and metabolism of epinephrine during incubation with fibroblasts. The ability of fetal bovine serum to support the induction of plasminogen activator by either 1 microM epinephrine or 3 microM prostaglandin E1 was maintained following dialysis but lost on heating (70 degrees C, 10 min) or acidification (pH 2.5). Human and calf sera supported the stimulatory effects of prostaglandin E1 but not of epinephrine. These results indicate that serum may influence the synthesis of plasminogen activator in cultured cells by modifying their response to vasoactive hormones.

Alprostadil↗
PubMed1992

Development of a procedure for coupling the homing device glu-plasminogen to liposomes.

The aim of this study was to find a suitable way of coupling the homing-device glu-plasminogen to the outside of liposomes. The described procedure is based on the reaction of thiol-groups introduced in the protein with thiol-reactive groups of the liposome. Details on the thiolation of proteins with the reagent succinimidyl-S-acetylthioacetate (SATA) were studied for a model-protein, amylase. Increasing the incubation-ratio SATA: amylase resulted in a gradually growing number of introduced thiol-groups, until a maximum of about 5 mol SH per mol amylase was reached. The enzymatic activity of the derivatized protein was even higher than that of native amylase. The thiol-introduction was then applied to glu-plasminogen itself. After activation with SATA, the protein was incubated with liposomes containing the thiol-reactive anchor maleimido-4-(p-phenylbutyrate)-phosphatidylethanolamine (MPB-PE). Under the chosen conditions, incubation of 0.5-2.5 mg/ml protein with 6.0-7.5 mumol/ml phospholipid for 30-120 min resulted in coupling-ratios of 20 to 94 micrograms glu-plasminogen per mumol phospholipid. This corresponds with about 140 to 660 protein molecules per liposome. SATA-derivatization of glu-plasminogen brought about a loss of its enzymatic activity induced by streptokinase. This activity of liposomally coupled plasminogen was about 52 to 74% of the activity of native glu-plasminogen (depending on the coupling-ratio). Although this may seem a significant loss of activity, it was shown that the capacity of liposomal glu-plasminogen to bind to its target, fibrin, was not reduced but several fold higher under the used conditions than that of the free protein. Therefore, the described method for thiol-introduction is an effective way to thiolate amylase without loss of activity, and to bind the homing-device glu-plasminogen to liposomes without substantially interfering with its fibrin-binding/homing capacity.

Amylases↗
PubMed1986

Species differences in the detection of high molecular weight urinary plasminogen activators.

Urine samples from 10 species of mammals were analyzed by SDS-PAGE followed by zymography for the presence of both plasminogen activators and plasminogen activator binding proteins. In contrast to results obtained with urine from humans (Homo sapiens), and to a lesser extent urine from baboons (Papio cynocephalous), urine from gorillas (Gorilla gorilla) and orangutans (Pongo pygmaeus) did not exhibit either very high molecular weight plasminogen activators or the presence of plasminogen activator binding proteins. Low levels of very high molecular weight plasminogen activators could be detected in concentrates of urine samples from rabbits (Oryctolagus cuniculus), dogs (Canis familiaris) and sheep (Ovis aries). Very high molecular weight plasminogen activators could be detected in unconcentrated guinea-pig (Cavia porcella) urine, concentrated urine samples from rats (Rattus norvegicus), but not in concentrated samples of urine from mice (Mus musculus). These results indicate that considerable variation between species exists at the level of the plasminogen activators present in urine, a finding that may relate to whether plasminogen activator binding proteins are also present in this fluid.

Animals↗
PubMed2004

Plasminogen activities and concentrations in patients with sporadic Creutzfeldt-Jakob disease.

Human plasminogen has been shown to interact with the abnormal disease-specific prion protein. Till now, no data are available for patients with Creutzfeldt-Jakob disease (CJD). Therefore, we compared plasminogen concentrations and plasminogen activities in patients with sporadic CJD and controls with other dementia, which were collected in the framework of the German CJD Surveillance study. Patients with CJD had significantly higher plasminogen concentrations than patients with other forms of dementia and plasminogen specific activities were lower in CJD patients. The reasons for these abnormalities are not clear at the moment. The results may reflect a disease-specific prion protein and plasminogen interaction in patients with CJD. Other possible explanations are plasminogen polymorphisms and genotypes with distinct plasminogen activity levels in CJD than in controls, which should be a subject for further studies.

Aged↗
PubMed2004

Locally delivered plasmin: why should it be superior to plasminogen activators for direct thrombolysis?

With advances in the field of thrombolytic therapy, whereby clots are routinely treated locally via a catheter, traditional systemic thrombolytics such as plasminogen activators might not be the best drugs for this task. Plasmin represents a new class of thrombolytic agents that exhibit direct fibrinolytic activity, without the need for either plasminogen or a plasminogen activator. In contrast to plasminogen activators, this independence from plasminogen allows plasmin to efficiently dissolve long, retracted blood clots that are inherently deficient in plasminogen. Preclinical safety studies in rabbits demonstrate that plasmin, in contrast to tissue-type plasminogen activator, does not cause re-bleeding from preformed hemostatic plugs. These results predict that plasmin will prove to be both superior to, and safer than, plasminogen activators in the dissolution of long, retracted blood clots in humans.

Animals↗
PubMed1987

A multicenter, randomized, placebo-controlled trial of a new form of intravenous recombinant tissue-type plasminogen activator (activase) in acute myocardial infarction.

A new, predominantly single chain preparation of recombinant tissue-type plasminogen activator was evaluated to determine coronary thrombolytic efficacy in 100 patients with acute myocardial infarction. At 3.6 +/- 1.2 hours (mean +/- SD) from symptom onset, patients received either intravenous tissue plasminogen activator (1.25 mg/kg body weight over 3 hours) or placebo on a 3:1 randomized, double-blind basis. Coronary angiography, performed 68 +/- 13 minutes after initiation of the study drug infusion, demonstrated patency of the infarct-related artery in 40 (57%) of 70 patients in the tissue plasminogen activator group compared with 3 (13%) of 23 patients in the placebo group (p less than 0.001). Patients in the placebo group were then eligible to receive intracoronary streptokinase. At 90 minutes the patency was observed in 49 (69%) of 71 tissue plasminogen activator patients compared with 5 (24%) of 21 placebo patients (p less than 0.001). At 120 minutes patency was observed in 59 (79%) of 75 patients of the tissue plasminogen activator group and in 10 (40%) of 25 in the intracoronary streptokinase/placebo group. A nadir value of less than 100 mg/dl fibrinogen occurred in 8 (11%) of 73 patients receiving tissue plasminogen activator versus 8 (40%) of 20 patients treated with intracoronary streptokinase (p = 0.002). Moderate or severe bleeding episodes occurred in 39% of patients treated with tissue plasminogen activator compared with 32% of patients who received placebo/intracoronary streptokinase (p = NS). Thus, this tissue plasminogen activator preparation achieves a high rate of recanalization and, at the doses employed, exhibits increased fibrinogen sparing compared with intracoronary streptokinase.

Angiography↗