SEARCH · Search PubMed

Results for “FIBRIN”

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.

SourceResearch connectionFrom yearThrough year

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

At least 1,099 records · Page 61Linked to original sources

PubMedDate not supplied

Use of fibrin sealant as a hemostatic agent after liver biopsy in swine.

PURPOSE: To determine whether fibrin sealant injected into the tract created by liver biopsy can be used to decrease postprocedural bleeding. An innovative delivery system was used to deploy the fibrin sealant. MATERIALS AND METHODS: Fibrin sealant is a hemostatic agent consisting of a suspension of fibrinogen and thrombin. A delivery system was devised whereby fibrin sealant could be injected into the tract created by liver biopsy. Thirty swine were randomized into three groups: control (n = 10), heparin (n = 10), and warfarin (n = 10). Each swine underwent laparotomy and was randomized to undergo three to five open liver biopsies with either a 14-gauge cutting needle in conjunction with the fibrin sealant device or a standard 14-gauge cutting needle alone. Forty-seven biopsy procedures were performed with the device; 64 biopsy procedures were performed without the device. Immediate blood loss per biopsy (mL) was estimated based on the size of the blood stain on a sponge. Specimens were assessed for sample size. RESULTS: Immediate blood loss with and without the device, respectively, was: control, 0.1 mL, 5.4 mL; heparin, 0 mL, 7 mL; warfarin, 0.1 mL, 9.3 mL. These differences were significant (P < .01) for each group of swine. In 43 of 47 biopsies (91%), the device functioned without difficulty. There was no difference in sample size when the device was used. CONCLUSIONS: The fibrin sealant device is effective in reducing bleeding after open liver biopsy in anticoagulated and nonanticoagulated swine. The promising results suggest that a trial of percutaneous liver biopsy in swine should be considered.

Animals↗

PubMedDate not supplied

Limited fibrin specificity of tissue-type plasminogen activator and its potential link to bleeding.

Plasminogen activators initiate the fibrinolytic process by converting plasminogen to plasmin. Though plasminogen activators are effective in the treatment of thrombotic disorders, bleeding complications are associated with their use. The development of plasminogen activators with greater fibrin specificity was expected to reduce the incidence of bleeding complications; however, this has not occurred. In our rabbit model (a) bleeding from standardized ear incisions induced by tissue-type plasminogen activator (t-PA) is attenuated when fibrinogenolysis is reduced by the coadministration of alpha 2-antiplasmin and (b) when used in doses that produce equivalent thrombolysis, vampire bat plasminogen activator (b-PA), an agent that is more fibrin specific than t-PA, causes less bleeding than t-PA. In addition, we have found that the (DD)E complex formed as a result of degradation of crosslinked fibrin is a potent stimulator of t-PA-induced plasminogen activation but has no effect on b-PA. Fragment X, a high-molecular-weight clottable fibrinogen degradation product, accumulates after treatment with t-PA but not with t-PA given with alpha 2-antiplasmin or with b-PA. These findings suggest that there is a link between plasminogen activator-induced fibrinogenolysis and bleeding, and that the composition of fibrin within hemostatic plugs may influence susceptibility to lysis. Whether these results mean that fibrin-specific plasminogen activators like b-PA will have a better risk-to-benefit profile in humans requires rigorous testing in well-designed clinical trials. However, at the very least, our findings suggest that the development of plasminogen activators that are more fibrin specific than t-PA is a worth-while exercise.

Animals↗

PubMed2001

Fibrin sealant reduces the duration and amount of fluid drainage after axillary dissection: a randomized prospective clinical trial.

BACKGROUND: Patients who have axillary dissections during lumpectomy or modified radical mastectomy for breast carcinoma accumulate serosanguinous fluid, potentially resulting in a seroma. Currently accepted practice includes insertion of one or more drains for fluid evacuation. This multicenter, randomized, controlled, phase II study was undertaken to evaluate whether a virally inactivated, investigational fibrin sealant is safe and effective when used as a sealing agent to reduce the duration and volume of serosanguinous fluid drainage and to determine the dose response of this effect. STUDY DESIGN: Patients undergoing lumpectomy or modified radical mastectomy were randomized to treatment with 4, 8, or 16 mL of fibrin sealant or control (no agent) at the axillary dissections site. Patients undergoing modified radical mastectomy also received an additional 4 or 8 mL of fibrin sealant at the skin flap site. Efficacy was evaluated by the number of days required for wound drainage and the volume of fluid drainage compared with control. Safety was confirmed by clinical course, the absence of viral seroconversion, and no major complications attributable to the sealant. RESULTS: The 4-mL axillary dissection dose of fibrin sealant significantly reduced the duration and quantity of fluid drainage from the axilla following lumpectomy (p < or = 0.05). In the modified radical mastectomy patients, a 16-mL axillary dissection dose combined with an 8-mL skin flap dose was significantly effective in reducing the number of days to drain removal (p < or = 0.05) and fluid drainage (p < or = 0.01). There were no fibrin sealant patient viral seroconversions and no major complications attributable to the sealant. A number of wound infections were noted, although this may represent a center-specific effect. CONCLUSIONS: Application of fibrin sealant following axillary dissection at the time of lumpectomy or modified radical mastectomy can significantly decrease the duration and quantity of serosanguinous drainage. The viral safety of the product was also supported.

Axilla↗

PubMed2001

Fibrin induces IL-8 expression from human oral squamous cell carcinoma cells.

In recent studies, we have demonstrated that fibrin is present in association with tumor cells in oral squamous cell carcinoma (OSCC) in vivo. We hypothesized that this fibrin can directly induce the expression of known angiogenic factors from oral tumor cells. Since IL-8 is known to be the major inducer of angiogenesis caused by these cells, we examined the ability of fibrin to stimulate IL-8 expression from OSCC cells in vitro. A physiologically relevant concentration of fibrin was found to cause a dose and time-dependent stimulation of IL-8 expression from oral and pharyngeal tumor cells but not from a non-tumorigenic oral cell line. Fibrinogen, thrombin and collagen were all unable to induce significant IL-8 expression, establishing the specificity of fibrin in causing this response. Gel filtration chromatography confirmed the molecular identity of the IL-8 antigen detected in the ELISA system used. These results suggest that fibrin may promote angiogenesis in oral tumors in vivo by directly upregulating the expression of IL-8 from tumor cells.

Analysis of Variance↗

PubMed2005

Endothelial cells organize fibrin clots into structures that are more resistant to lysis.

Acute myocardial infarction is a major cause of death and disability in the United States. Introducing thrombolytic agents into the clot to dissolve occlusive coronary artery thrombi is one method of treatment. However, despite advances in our knowledge of thrombosis and thrombolysis, survival rates following thrombolytic therapy have not improved substantially. This failure highlights the need for further study of the factors mediating clot stabilization. Using laser scanning confocal microscopy of clots formed from fluorescein-labeled fibrinogen, we investigated what effect binding of fibrin to the endothelial surface has on clot structure and resistance to lysis. Fluorescent fibrin clots were produced over human umbilical vein endothelial cells (HUVEC) and the clot structure analyzed. In the presence of HUVEC, fibrin near the endothelial surface was more organized and occurred in tighter bundles compared to fibrin just 50 microm above. The HUVEC influence on fibrin architecture was blocked by inhibitory concentrations of antibodies to alphaV or beta3 integrin subunits. The regions of the clots associated with endothelial cells were more resistant to lysis than the more homogenous regions distal to endothelium. Thus, our data show that binding of fibrin to integrins on endothelial surfaces produces clots that are more resistant to lysis.

Cells, Cultured↗

PubMed1987

Interaction of one-chain and two-chain tissue plasminogen activator with intact and plasmin-degraded fibrin.

Tissue-type plasminogen activator (t-PA) plays a central role in fibrinolysis in vivo. Although it is known to bind to fibrin, the dissociation constant (Kd) and number of moles bound per mole of fibrin monomer (n) have never been measured directly. In this study, the binding of both the one-chain form and the two-chain form of recombinant, human t-PA to fibrin was measured. Although more one-chain t-PA than two-chain t-PA is bound to fibrin, the Kd's and n's were within experimental error of each other. Significantly more t-PA is bound to clots made from fibrinogen which has been digested with plasmin than to clots made from intact fibrinogen. The additional binding was shown to be due to the formation of new set(s) of binding site(s) with dissociation constants that are 2-4 orders of magnitude tighter than the binding site present on clots made from intact fibrinogen. epsilon-Aminocaproic acid was capable of competing for the loose binding site present on both intact and degraded fibrin but had little effect on the binding of t-PA to the new site(s) formed by plasmin digestion. This increase in binding caused by plasmin-mediated proteolysis of fibrin suggests a possible mechanism for a positive regulation capable of accelerating fibrinolysis.

Fibrin↗

PubMed2004

Factor XIIIa incorporates thymosin beta4 preferentially into the fibrin(ogen) alphaC-domains.

It was shown recently that tissue transglutaminase and presumably plasma transglutaminase, factor XIIIa, can covalently incorporate into fibrin(ogen) a physiologically active peptide, thymosin beta(4) [(Huff et al. (2002) FASEB J. 16, 691-696]. To clarify the mechanism of this incorporation, we studied the interaction of thymosin beta(4) with fibrinogen, fibrin, and their recombinant fragments, the gamma-module (gamma-chain residues 148-411), and the alphaC-domain (Aalpha-chain residues 221-610) and its truncated variants by immunoblot and ELISA. No significant noncovalent interaction between them was detected in the absence of activated factor XIII, while in its presence thymosin beta(4) was effectively incorporated into fibrin and to a lesser extent into fibrinogen. The incorporation at physiological concentrations of fibrin(ogen) and factor XIII was significant with molar incorporation ratios of thymosin beta(4) to fibrinogen and fibrin of 0.2 and 0.4, respectively. Further experiments revealed that although activated factor XIII incorporates thymosin beta(4) into the isolated gamma-module and alphaC-domain, in fibrin the latter serves as the major incorporation site. This site was further localized to the COOH-terminal portion of the alphaC-domain including residues 392-610.

Amino Acid Sequence↗

PubMed2002

Polymerization sites in the D-domain of human fibrin(ogen).

The present work deals with localization of previously unknown polymerization sites of the fibrin DD-fragment. D-dimer we obtained has a pronounced inhibitory effect on fibrin polymerization (IC50 = 0.06 microM). The inhibitory effect of the DD-fragment disappeared after reduction and carboxymethylation. However, polypeptide chains betaDD (Bbeta134-461) and gammagammaDD (gamma63-411)2 of the DD-fragment, isolated by preparative electrophoresis, displayed their inhibitory activity. For instance, the rates of fibrin protofibril lateral association were decreased twice in the presence of betaDD and gammagammaDD chains at their molar ratios to fibrin of 0.40 and 0.15, respectively. The IC50 values for betaDD and gammagammaDD were 0.24 and 0.10 microM, respectively. Highly specific inhibition of protofibril lateral association suggests that the protofibril lateral association sites are located in Bbeta134-461 and gamma63-411 regions of the fibrin D-domain. Our data confirm those reported by Doolittle et al. regarding the gamma-chain and a hypothesis about beta-chain of fibrin D-domain (Yang, Z., Mochalkin, I., and Doolittle, R. F. (2000) Biochemistry, 97, 14156-14161).

Biopolymers↗

PubMed2000

Enzymatic incorporation of bioactive peptides into fibrin matrices enhances neurite extension.

Fibrin plays an important role in wound healing and regeneration, and enjoys widespread use in surgery and tissue engineering. The enzymatic activity of Factor XIIIa was employed to covalently incorporate exogenous bioactive peptides within fibrin during coagulation. Fibrin gels were formed with incorporated peptides from laminin and N-cadherin alone and in combination at concentrations up to 8.2 mol peptide per mole of fibrinogen. Neurite extension in vitro was enhanced when gels were augmented with exogenous peptide, with the maximal improvement reaching 75%. When this particular fibrin derivative was evaluated in rats in the repair of the severed dorsal root within polymeric tubes, the number of regenerated axons was enhanced by 85% relative to animals treated with tubes filled with unmodified fibrin. These results demonstrate that it is possible to enhance the biological activity of fibrin by enzymatically incorporating exogenous oligopeptide domains of morphoregulatory proteins.

Amino Acid Sequence↗

PubMed1997

Expression of tissue type plasminogen activator and type 1 plasminogen activator inhibitor, and persistent fibrin deposition in chronic renal allograft failure.

Persistent fibrin deposition has been observed in kidneys undergoing chronic rejection, and has been suggested to contribute to the obliteration of the vasculature in these grafts. The mechanisms leading to it are not clear. Fibrinolysis, the process to remove fibrin in tissues, is initiated by tissue type plasminogen activator (tPA) and suppressed by type 1 plasminogen activator inhibitor (PAI-1). To investigate their roles in chronic rejection and fibrin deposition, we serially examined the expression of tPA and PAI-1 in an unmodified chronic rejection model, using a Fisher 344 to Lewis rat renal transplant, at 0, 2, 4, 6, 10, 12, 16 and 20 weeks post-transplantation (N = 4 rats/time point in each group). We also analyzed fibrin deposition and the development of chronic changes in the grafts. Our results show that tPA was up-regulated only in the acute phase of rejection (P < 0.05), whereas PAI-1 was induced and persistently expressed during the progressive phase of chronic rejection, together with persistent fibrin deposition in the grafts. Immunohistochemistry showed PAI-1 was mainly localized to the damaged/proliferative vascular intima. The results suggest that persistent induction of PAI-1 may be responsible for the continuance of fibrin deposition, which is associated with irreversible damage and chronic graft loss.

Animals↗

PubMed2003

Thrombin-induced conversion of fibrinogen to fibrin results in rapid platelet trapping which is not dependent on platelet activation or GPIb.

1. Activation of human platelets by thrombin is mediated by the proteolytic cleavage of two G-protein coupled protease-activated receptors, PAR-1 and PAR-4. However, thrombin also binds specifically to the platelet surface glycoprotein GPIb. It has been claimed that thrombin can induce aggregation of platelets via a novel GPIb-mediated pathway, which is independent of PAR activation and fibrinogen binding to alpha(IIb)beta(3) integrin, but dependent upon polymerizing fibrin and the generation of intracellular signals. 2. In the presence of both fibrinogen and the alpha(IIb)beta(3) receptor antagonist lotrafiban, thrombin induced a biphasic platelet aggregation response. The initial primary response was small but consistent and associated with the release of platelet granules. The delayed secondary response was more substantial and was abolished by the fibrin polymerization blocking peptide GPRP. 3. Cleavage of the extracellular portion of GPIb by mocarhagin partially inhibited thrombin-induced alpha(IIb)beta(3)-dependent aggregation and release, but had no effect on the secondary fibrin-dependent response. 4. Fixing of the platelets abolished alpha(IIb)beta(3)-dependent aggregation and release of adenine nucleotides, whereas the fibrin-dependent response remained, indicating that platelet activation and intracellular signalling are not necessary for this secondary 'aggregation'. 5. In conclusion, the secondary fibrin-dependent 'aggregation' response observed in the presence of fibrinogen and lotrafiban is a platelet trapping phenomenon dependent primarily on the conversion of soluble fibrinogen to polymerizing fibrin by thrombin.

Dose-Response Relationship, Drug↗

PubMedDate not supplied

Fibrin sealants and glues.

Fibrin sealants and fibrin glues have become effective instruments in the care of surgical patients. They have been used as an adjunct to hemostasis, wound healing, tissue adhesion, and drug delivery. In cardiac surgery, fibrin glues have emerged as valuable tools to improve hemostasis, decreased blood transfusions, improve tissue handling, and pretreat vascular grafts. Fibrin glues and sealants are now available commercially in the United States. This article will review the history, pharmacology, uses, and toxicity of fibrin sealants and fibrin glues.

Animals↗

PubMed1996

Delayed vasal reanastomosis in rats: comparison of a microsurgical technique and a fibrin-glued procedure.

OBJECTIVES: To compare fibrin-glued vasovasostomy to a conventional microsurgical technique in a protocol of delayed vasovasostomy. MATERIALS AND METHODS: Forty male Sprague-Dawley rats underwent bilateral vasectomy through a midline abdominal incision. Two weeks later all animals underwent a bilateral vasectomy reversal through a bilateral inguino-scrotal incision, following two different protocols. Invariably, the proximal segment had a larger lumen. The control group (20 rats) had a conventional modified one-layer sutured vasal anastomosis with 10/0 nylon. The experimental group (20 rats) underwent vasal anastomosis using fibrin glue and consisting of three transmural sutures with 10/0 nylon followed by the application of fibrin glue circumferentially to seal the anastomosis. The fibrin-tissue adhesive was obtained from pooled donor plasma and was virally inactivated by a solvent-detergent treatment. Seven weeks after surgery all animals were killed and the vasal specimens were evaluated for gross patency and the incidence of sperm granuloma. RESULTS: The control group had a patency rate of 85% and half had sperm granuloma. The experimental group had a patency rate of 92% and 40% had sperm granuloma; neither difference was significant. The mean operative time was significantly shorter for the fibrin glue-assisted vasovasostomy (P < 0.001). CONCLUSION: This study showed that a delayed fibrin-glued vasovasostomy gave a comparable anatomical success and an incidence of sperm granuloma similar to that using a conventional microsurgical technique, but with the advantages of a shorter operative time and a less technically demanding anastomosis.

Anastomosis, Surgical↗

PubMed2000

An immediate, allergic skin reaction to aprotinin after reexposure to fibrin sealant.

BACKGROUND: The safety of fibrin tissue adhesives has been a concern since they entered wide clinical application. Most commercially available kits contain the proteolytic inhibitor, aprotinin, to stabilize the fibrin clot. A bovine protein, this substance has an allergenic potency. CASE REPORT: This case report presents a patient who had a generalized allergic skin reaction, probably triggered by aprotinin upon reexposure to fibrin sealant injected subgaleally to achieve closure of a liquor fistula after neurosurgical treatment. The serologic investigation revealed aprotinin-specific IgE and IgG. From 1990 through 1998, reports of five allergic reactions following 1 million exposures to fibrin sealant were made to the manufacturer. The clinical relevance of allergic reactions to aprotinin contained in fibrin sealants and measures to avoid them are discussed. CONCLUSION: These hypersensitivity reactions are extremely rare (incidence, 0.5/100,000 for all reactions and 0.3/100,000 for serious reactions), but they must be kept in mind as possible adverse events after repeated applications of fibrin sealants within a few weeks.

Antibodies, Anti-Idiotypic↗

PubMedDate not supplied

Direct fibrin injection to promote new collateral growth in hind limb ischemia in a rabbit model.

UNLABELLED: Local stimulation of angiogenesis is a new approach for the treatment of critical limb ischemia. Our investigation tested intramuscular (i.m.) injection of a modified fibrin meshwork in a rabbit model. METHODS: The left external iliac and femoral arteries were excised in 24 rabbits that were divided into four groups: control; i.m. saline injection; fibrin meshwork plus low dose (2.5 mg) fibrinogen i.m.; fibrin meshwork plus high-dose (5.0 mg) fibrinogen i.m. Angiography was performed before surgery, immediately after surgery, and one month postoperatively. Lower limb-calf blood pressure was measured immediately after surgery and at postoperative days 10, 20, and 30. On day 30, conventional indirect immunostaining was performed to determine the percentage of the area occupied by capillaries. RESULTS: Immediately after surgery, in all four groups, the number of contract-opacified arteries (COA) crossing a specific segment of a grid decreased from 5.3 +/- 1.3 to 3.2 +/- 1.0 (p < 0.05); the number of grid intersections decreased from 30.2 +/- 6.5 to 19.3 +/- 4.8 (p < 0.05); and the total number of grids with COA decreased from 18.3 +/- 3.8 to 12.2 +/- 2.5 (p < 0.05). One month after surgery, in the control group, these parameters were 6.2 +/- 1.1, 33.2 +/- 5.7 and 20.3 +/- 1.5, respectively; in the saline-treated group, these parameters were 6.1 +/- 0.8, 28.3 +/- 6.9 and 19.8 +/- 1.1, respectively (p > 0.05 versus control and versus baseline data). When fibrin containing 5.0 mg fibrinogen was used, these parameters increased to 8.5 +/- 0.9, 48.3 +/- 5.1, and 27.1 +/- 0.9, respectively (p < 0.001 versus immediately after surgery and p < 0.05 versus control). In all four series, no Doppler flow signal was detected from the posterior tibial artery by day 10. By day 30, the lower limb-calf blood pressure ratio had improved in all four series, but was significantly improved in only the two groups treated with fibrin sealant (0.3 +/- 0.05 control; 0.3 +/- 0.08 saline; 0.6 +/- 0.06 fibrinogen 2.5; 0.7 +/- 0.05 fibrinogen 5.0). CONCLUSION: Intramuscular injection of a fibrin meshwork considerably increased angiogenesis in the severely ischemic hind limb and may be strongly recommended for clinical use in patients with limb-threatening ischemia.

Animals↗

PubMed1995

[Risk factors, prevention and therapy of fibrin reactions after IOL implantation].

BACKGROUND: Postoperative fibrinous reactions following the small-incision technique seem to be very rare. Problem cases can be treated with tissue Plasmin Activator. METHOD: To investigate the new prophylactic and therapeutic possibilities the last 2,056 cataract procedures with PMMA lens implantation were statistically analyzed. RESULTS: In 152 (7.4%) fibrin cases we observed after ECCE (n = 586) 12.8%, after phacoemulsification (PE) with sutured 6.5-mm corneoscleral incision (n = 546) 7.0% and after PE with clear corneal selfsealing 4.1-mm incision (n = 924) only 3.9% fibrinous reactions (p < 0.01). In case of ECCE the rate of fibrinous reactions amounted to 22.4% following prolonged procedures (< 50 min), while it was low as 9.5% with a short period of time (< 30 min) (p < 0.01). In 8 steroid-resistant cases we applied 25 micrograms Plasmin Activator intraocularly. The injections led to complete dissolution of the fibrinous membranes without complications. CONCLUSION: Postoperative fibrinous reactions can be reduced statistically significantly by application of the corneal small-incision technique. The most efficient therapy is intraocular Plasmin Activator fibrinolysis.

Aged↗

PubMed1994

[Injection therapy of bleeding peptic ulcer with fibrin or polidocanol].

The effectiveness of injecting fibrin (group 1; with adrenalin: n = 11; without adrenalin: n = 29) or polidocanol (with [n = 17] or without adrenalin [n = 8]) or adrenalin alone (n = 15) (group 2) in the arrest of bleeding from peptic ulcers was compared in a prospective randomized study of 80 patients (61 males, 19 females; mean age 66.7 [28-92] years). Both groups were comparable regarding age, sex distribution, ulcer site and haemoglobin concentration. The amount of fibrin injected per patient at the first session averaged 2.9 +/- 1.8 ml, that of polidocanol 3.1 +/- 1.9 ml. The initial injection was successful in all but one patients (40 and 39, respectively). Primary definitive haemostasis was achieved in 59 patients (73.8%), with recurrence of bleeding in 20 (9 and 11: 25%). Recurrent bleeding was always treated with fibrin injection. Definitive haemostasis was achieved by a second application of fibrin in eight patients (10%), so that the definitive haemostasis rate was 83.8%. A second recurrence of bleeding was noted in eight patients, requiring surgical treatment. Four patients died during the second recurrence. It is concluded that injection of fibrin is an effective method of treatment of bleeding ulcer. There was no evidence that fibrin was better than polidocanol with or without adrenaline.

Adult↗

PubMed1987

Fibrin and fibrinogen-related antigens in patients with stable and unstable coronary artery disease.

Coronary-artery thrombosis may be important in the pathogenesis of unstable angina at rest. To study this possibility, we measured the serum concentrations of fibrin-related antigen, D dimer (the principal breakdown fragment of fibrin), and fibrin monomer (an intermediate product of fibrin formation) in the serum of five groups of subjects. These included 10 healthy controls, 10 controls with noncardiac pain, and three groups of 10 patients each with chronic stable angina, unstable angina at rest, or acute myocardial infarction. The concentration of fibrin-related antigen (normal range, 48 to 184 ng per milliliter) was normal in the control patients with noncardiac pain (63 to 202 ng per milliliter) and in patients with chronic stable angina (95 to 186), but it was increased in patients with unstable angina (401 to 2507) or acute myocardial infarction (470 to 1930) (P less than 0.001). D dimer concentrations in patients with unstable angina (178.3 to 310.6 ng per milliliter) or acute myocardial infarction (103.9 to 321.6) were higher than those in patients with chronic stable angina (28.6 to 52.1), in controls with noncardiac pain (44.7 to 53.1), and in healthy controls (40.4 to 50.3) (P less than 0.001). Concentrations of fibrin monomer were highest in patients with acute myocardial infarction (247.5 to 571.3 ng per milliliter) (P less than 0.001), intermediate in those with unstable angina (54.7 to 241.7) (P less than 0.001), and normal (normal range, 14.5 to 19.8 ng per milliliter) in controls with noncardiac pain (12.0 to 18.4). and patients with chronic stable angina (10.7 to 17.6). These findings suggest the presence of an active thrombotic process in patients with unstable angina at rest or acute myocardial infarction. The data do not prove that the coronary arteries were the site of the thrombotic process, but the observations are consistent with the hypothesis that thrombus formation may have an important role in the pathogenesis of these conditions.

Angina Pectoris↗