Aminocaproic Acid
Aminocaproates
Antifibrinolytic Agents
Aprotinin
Postoperative Hemorrhage
Effect of phospholipase A2 digestion on the conformation and lysine/fibrinogen binding properties of human lipoprotein[a]. (1/179)
In vitro hydrolysis of human lipoprotein[a] (Lp[a]) by phospholipase A2 (PLA2) decreased the phosphatidylcholine (PC) content by 85%, but increased nonesterified fatty acids 3.2-fold and lysoPC 12.9-fold. PLA2-treated Lp[a] had a decreased molecular weight, increased density, and greater electronegativity on agarose gels. In solution, PLA2-Lp[a] was a monomer, and when assessed by sedimentation velocity it behaved like untreated Lp[a], in that it remained compact in NaCl solutions but assumed the extended form in the presence of 6-amino hexanoic acid, which was shown previously to have an affinity for the apo[a] lysine binding site II (LBS II) comprising kringles IV5-8. We interpreted our findings to indicate that PLA2 digestion had no effect on the reactivity of this site. This conclusion was supported by the results obtained from lysine Sepharose and fibrinogen binding experiments, in the presence and absence of Tween 20, showing that phospholipolysis had no effect on the reactivity of the LBS-II domain. A comparable binding behavior was also exhibited by the free apo[a] derived from each of the two forms of Lp[a]. We did observe a small increase in affinity of PLA2-Lp[a] to lysine Sepharose and attributed it to changes in reactivity of the LBS I domain (kringle IV10) induced by phospholipolysis. In conclusion, the extensive modification of Lp[a] caused by PLA2 digestion had no significant influence on the reactivity of LBS II, which is the domain involved in the binding of apo[a] to fibrinogen and apoB-100. These results also suggest that phospholipids do not play an important role in these interactions. (+info)6-Aminohexanoic acid as a chemical chaperone for apolipoprotein(a). (2/179)
Apolipoprotein (a) (apo(a)) is a component of the atherogenic lipoprotein, Lp(a). The efficiency with which apo(a) escapes the endoplasmic reticulum (ER) and is secreted by the liver is a major determinant of plasma Lp(a) levels. Apo(a) contains a series of domains homologous to plasminogen kringle (K) 4, each of which possesses a potential lysine-binding site. By using primary mouse hepatocytes expressing a 17K4 human apo(a) protein, we found that high concentrations (25-200 mM) of the lysine analog, 6-aminohexanoic acid (6AHA), increased apo(a) secretion 8-14-fold. This was accompanied by a decrease in apo(a) presecretory degradation. 6AHA inhibited accumulation of apo(a) in the ER induced by the proteasome inhibitor, lactacystin. Thus, 6AHA appeared to inhibit degradation by increasing apo(a) export from the ER. Significantly, 6AHA overcame the block in apo(a) secretion induced by the ER glucosidase inhibitor, castanospermine. 6AHA may therefore circumvent the requirement for calnexin and calreticulin interaction in apo(a) secretion. Sucrose gradients and a gel-based folding assay were unable to detect any influence of 6AHA on apo(a) folding. However, non-covalent or small, disulfide-dependent changes in apo(a) conformation would not be detected in these assays. Proline also increased the efficiency of apo(a) secretion. We propose that 6AHA and proline can act as chemical chaperones for apo(a). (+info)Pharmacokinetics of epsilon-aminocaproic acid in patients undergoing aortocoronary bypass surgery. (3/179)
BACKGROUND: Epsilon-aminocaproic acid (EACA) is commonly infused during cardiac surgery using empiric dosing schemes. The authors developed a pharmacokinetic model for EACA elimination in surgical patients, tested whether adjustments for cardiopulmonary bypass (CPB) would improve the model, and then used the model to develop an EACA dosing schedule that would yield nearly constant EACA blood concentrations. METHODS: Consenting patients undergoing elective coronary artery surgery received one of two loading doses of EACA, 30 mg/kg (group I, n = 7) or 100 mg/kg (group II, n = 6) after CPB, or (group III) a 100 mg/kg loading dose before CPB and a 10 mg x kg(-1) x h(-1) maintenance infusion continued for 4 h during and after CPB (n = 7). Two patients with renal failure received EACA in the manner of group III. Blood concentrations of EACA, measured by high-performance liquid chromatography, were subjected to mixed-effects pharmacokinetic modeling. RESULTS: The EACA concentration data were best fit by a model with two compartments and corrections for CPB. The elimination rate constant k10 fell from 0.011 before CPB to 0.0006 during CPB, returning to 0.011 after CPB. V1 increased 3.8 l with CPB and remained at that value thereafter. Cl1 varied from 0.08 l/min before CPB to 0.007 l/min during CPB and 0.13 l/min after CPB. Cl2 increased from 0.09 l/min before CPB to 0.14 l/min during and after CPB. Two patients with renal failure demonstrated markedly reduced clearance. Using their model, the authors predict that an EACA loading infusion of 50 mg/kg given over 20 min and a maintenance infusion of 25 mg x kg(-1) x h(-1) would maintain a nearly constant target concentration of 260 microg/ml. CONCLUSIONS: EACA clearance declines and volume of distribution increases during CPB. The authors' model predicts that more stable perioperative EACA concentrations would be obtained with a smaller loading dose (50 mg/kg given over 20 min) and a more rapid maintenance infusion (25 mg x kg(-1) x h(-1)) than are typically employed. (+info)An integrated study of fibrinogen during blood coagulation. (4/179)
The rate of conversion of fibrinogen (Fg) to the insoluble product fibrin (Fn) is a key factor in hemostasis. We have developed methods to quantitate fibrinopeptides (FPs) and soluble and insoluble Fg/Fn products during the tissue factor induced clotting of whole blood. Significant FPA generation (>50%) occurs prior to visible clotting (4 +/- 0.2 min) coincident with factor XIII activation. At this time Fg is mostly in solution along with high molecular weight cross-linked products. Cross-linking of gamma-chains is virtually complete (5 min) prior to the release of FPB, a process that does not occur until after clot formation. FPB is detected still attached to the beta-chain throughout the time course demonstrating release of only low levels of FPB from the clot. After release of FPB a carboxypeptidase-B-like enzyme removes the carboxyl-terminal arginine resulting exclusively in des-Arg FPB by the 20-min time point. This process is inhibited by epsilon-aminocaproic acid. These results demonstrate that transglutaminase and carboxypeptidase enzymes are activated simultaneously with Fn formation. The initial clot is a composite of Fn I and Fg already displaying gamma-gamma cross-linking prior to the formation of Fn II with Bbeta-chain remaining mostly intact followed by the selective degradation of FPB to des-Arg FPB. (+info)The effect of prophylactic epsilon-aminocaproic acid on bleeding, transfusions, platelet function, and fibrinolysis during coronary artery bypass grafting. (5/179)
BACKGROUND: Antifibrinolytic medications administered before skin incision decrease bleeding after cardiac surgery. Numerous case reports indicate thrombus formation with administration of epsilon-aminocaproic acid (epsilon-ACA). The purpose of this study was to examine the efficacy of epsilon-ACA administered after heparinization but before cardiopulmonary bypass in reducing bleeding and transfusion requirements after primary coronary artery bypass surgery. METHODS: Seventy-four adult patients undergoing primary coronary artery bypass surgery were randomized to receive 125 mg/kg epsilon-ACA followed by an infusion of 12.5 mg x kg(-1) x h(-1) or an equivalent volume of saline. Coagulation studies, thromboelastography, and platelet aggregation tests were performed preoperatively, after bypass, and on the first postoperative day. Mediastinal drainage was recorded during the 24 h after surgery. Homologous blood transfusion triggers were predefined and transfusion amounts were recorded. RESULTS: One patient was excluded for surgical bleeding and five patients were excluded for transfusion against predefined criteria One patient died from a dysrhythmia 2 h postoperatively. Among the remaining 67, the epsilon-ACA group had less mediastinal blood loss during the 24 h after surgery, 529+/-241 ml versus 691+/-286 ml (mean +/- SD), P < 0.05, despite longer cardiopulmonary bypass times and lower platelet counts, P < 0.05. Platelet aggregation was reduced in both groups following cardiopulmonary bypass but did not differ between groups. Homologous blood transfusion was similar between both groups. CONCLUSIONS: Prophylactic administration of epsilon-ACA after heparinization but before cardiopulmonary bypass is of minimal benefit for reducing blood loss postoperatively in patients undergoing primary coronary artery bypass grafting. (+info)The effects of hydrostatic pressure on the conformation of plasminogen. (6/179)
Plasminogen undergoes a large conformational change when it binds 6-aminohexanoate. Using ultraviolet absorption spectroscopy and native PAGE, we show that hydrostatic pressure brings about the same conformational change. The volume change for this conformational change is -33 mL.mol-1. Binding of ligand and hydrostatic pressure both cause the protein to open up to expose surfaces that had previously been buried in the interior. (+info)Intravesicular instillation of E-aminocaproic acid for patients with adenovirus-induced hemorrhagic cystitis. (7/179)
Hemorrhagic cystitis (HC) is a known complication of allogenic BMT. We report a case of a 28-year-old female with CML in chronic phase, which was treated with a matched unrelated donor (MUD) transplant, complicated by hemorrhagic cystitis on day +42 after the transplant. Adenovirus was isolated from the urine and she was treated with ribavirin, 1 g twice a day for 8 days. We report the use of Amicar (E-aminocaproic acid), 2.5 g solution as bladder instillation to treat the intractable hematuria. (+info)Role of the N-terminal region of staphylokinase (SAK): evidence for the participation of the N-terminal region of SAK in the enzyme-substrate complex formation. (8/179)
Staphylokinase (SAK) forms an inactive 1:1 complex with plasminogen (PG), which requires both the conversion of PG to plasmin (Pm) to expose an active site in PG-SAK activator complex and the amino-terminal processing of SAK to expose the positively charged (Lys-11) amino-terminus after removal of the 10 N-terminal amino acid residues from the full length protein. The mechanism by which the N-terminal segment of SAK affects its PG activation capability was investigated by generating SAK mutants, blocked in the native amino-terminal processing site of SAK, and carrying an alteration in the placement of the positively charged amino acid residue, Lys-11, and further studying their interaction with PG, Pm, miniplasmin and kringle structures. A ternary complex formation between PG-SAK PG was observed when an immobilized PG-SAK binary complex interacted with free radiolabelled PG in a sandwich binding experiment. Formation of this ternary complex was inhibited by a lysine analog, 6-aminocaproic acid (EACA), in a concentration dependent manner, suggesting the involvement of lysine binding site(s) in this process. In contrast, EACA did not significantly affect the formation of binary complex formed by native SAK or its mutant derivatives. Furthermore, the binary (activator) complex formed between PG and SAK mutant, PRM3, lacking the N-terminal lysine 11, exhibited 3-4-fold reduced binding with PG, Pm or miniplasmin substrate during ternary complex formation as compared to native SAK. Additionally, activator complex formed with PRM3 failed to activate miniplasminogen and exhibited highly diminished activation of substrate PG. Protein binding studies indicated that it has 3-5-fold reduction in ternary complex formation with miniplasmin but not with the kringle structure. In aggregate, these observations provide experimental evidence for the participation of the N-terminal region of SAK in accession and processing of substrate by the SAK-Pm activator complex to potentiate the PG activation by enhancing and/or stabilizing the interaction of free PG. (+info)In general, surgical blood loss is considered excessive if it exceeds 10-20% of the patient's total blood volume. This can be determined by measuring the patient's hemoglobin levels before and after the procedure. A significant decrease in hemoglobin levels post-procedure may indicate excessive blood loss.
There are several factors that can contribute to surgical blood loss, including:
1. Injury to blood vessels or organs during the surgical procedure
2. Poor surgical technique
3. Use of scalpels or other sharp instruments that can cause bleeding
4. Failure to control bleeding with proper hemostatic techniques
5. Pre-existing medical conditions that increase the risk of bleeding, such as hemophilia or von Willebrand disease.
Excessive surgical blood loss can lead to a number of complications, including:
1. Anemia and low blood counts
2. Hypovolemic shock (a life-threatening condition caused by excessive fluid and blood loss)
3. Infection or sepsis
4. Poor wound healing
5. Reoperation or surgical intervention to control bleeding.
To prevent or minimize surgical blood loss, surgeons may use a variety of techniques, such as:
1. Applying topical hemostatic agents to the surgical site before starting the procedure
2. Using energy-based devices (such as lasers or ultrasonic devices) to seal blood vessels and control bleeding
3. Employing advanced surgical techniques that minimize tissue trauma and reduce the risk of bleeding
4. Monitoring the patient's hemoglobin levels throughout the procedure and taking appropriate action if bleeding becomes excessive.
1. Injury to blood vessels during surgery
2. Poor suturing or stapling techniques
3. Bleeding disorders or use of anticoagulant medications
4. Infection or hematoma (a collection of blood outside the blood vessels)
5. Delayed recovery of blood clotting function
Postoperative hemorrhage can range from mild to severe and life-threatening. Mild bleeding may present as oozing or trickling of blood from the surgical site, while severe bleeding can lead to hypovolemic shock, organ failure, and even death.
To diagnose postoperative hemorrhage, a physical examination and medical history are usually sufficient. Imaging studies such as ultrasound, computed tomography (CT) or magnetic resonance imaging (MRI) may be ordered to evaluate the extent of bleeding and identify any underlying causes.
Treatment of postoperative hemorrhage depends on the severity and location of the bleeding. Mild bleeding may be managed with dressings, compression bandages, and elevation of the affected limb. Severe bleeding may require interventions such as:
1. Surgical exploration to locate and control the source of bleeding
2. Transfusion of blood products or fresh frozen plasma to restore clotting function
3. Use of vasopressors to raise blood pressure and perfuse vital organs
4. Hemostatic agents such as clotting factors, fibrin sealants, or hemostatic powder to promote clot formation
5. In some cases, surgical intervention may be required to repair damaged blood vessels or organs.
Prevention of postoperative hemorrhage is crucial in reducing the risk of complications and improving patient outcomes. Preventive measures include:
1. Proper preoperative evaluation and preparation, including assessment of bleeding risk factors
2. Use of appropriate anesthesia and surgical techniques to minimize tissue trauma
3. Conservative use of hemostatic agents and blood products during surgery
4. Closure of all bleeding sites before completion of the procedure
5. Monitoring of vital signs, including pulse rate and blood pressure, during and after surgery
6. Preoperative and postoperative management of underlying conditions such as hypertension, diabetes, and coagulopathies.
Early recognition and prompt intervention are critical in effectively managing postoperative hemorrhage. In cases of severe bleeding, timely and appropriate interventions can reduce the risk of complications and improve patient outcomes.
Aminocaproic acid
Ion-exchange resin
Utako Okamoto
Antifibrinolytic
Angiodysplasia
Streptokinase
Tissue plasminogen activator
Caprolactam
Panangipalli Venugopal
Exercise-induced pulmonary hemorrhage
Corneal ulcers in animals
Plastic
Coagulation
Tranexamic acid
Fibrinolysis
Yunnan Baiyao
Nylon-eating bacteria
Hyphema
Aprotinin
Angioedema
Complement deficiency
Sickle cell nephropathy
Thromboelastography
Haemophilia
Glanzmann's thrombasthenia
ATC code B02
Elmer Keiser Bolton
C6H13NO2
List of MeSH codes (D02)
Sumire Uesaka
List of MeSH codes (D12.125)
HAL Allergy Group
Cryoprecipitate
Radioimmunoprecipitation assay buffer
Aminocaproic Acid
AMINOCAPROIC ACID INJECTION, USP
DailyMed - AMINOCAPROIC ACID tablet
Aminocaproic Acid: MedlinePlus Drug Information
MedlinePlus - Search Results for: Aminocaproic Acid
Epsilon-aminocaproic acid (EACA) - PubMed
Search of: AMINOCAPROIC ACID AND blood AND surgery AND acid - Results by Topic - ClinicalTrials.gov
Aminocaproic Acid/AE - Search Results - PubMed
ALLANTOIN OR AMINOCAPROIC ACID OR SILICON DIOXIDE - Books - NCBI
Aminocaproic Acid
Hemoglobinopathy Retinopathy Medication: Hemostatic agents, Corticosteroids
Angioedema Medication: Alpha/Beta-Adrenergic Agonists, Antihistamines, 1st-Generation, Antihistamines, 2nd Generation,...
Mixing Aminocaproic Acid and Cocaine | Worlds Best Rehab
Allergic contact dermatitis caused by ϵ-aminocaproic acid in a purified sodium hyaluronate ophthalmic solution. | Contact...
Aminocaproic Acid - Shanghai No.1 Biochem : Uses, Side Effects, Interactions, Dosage / Pillintrip
Community Counts Data Visualization Technical Notes Glossary | CDC
MEDLINE Data Changes - 2014. NLM Technical Bulletin. 2013 Nov-Dec
Cerebral Venous Thrombosis: Background, Etiology, Epidemiology
Lesser Known "A" Herbs For Your Pets | Pet Health | Articles | Magazine
Laboratory measures of hemostasis and fibrinolysis after intravenous administration of epsilon-aminocaproic acid in clinically...
Furosemide (Lasix) | Davis's Drug Guide
Dictionary of Medical Acronyms & Abbreviations
6-aminohexanoic acid - Ontology Report - Rat Genome Database
Overview of Platelet Disorders - Hematology and Oncology - Merck Manuals Professional Edition
Biomarkers Search
Price list for generic name of drugs | A-Z Index Page
Clotting and Bleeding Disorders Social Media Resources | NHLBI, NIH
Ketoconazole Dog Medication (Free Shipping) | Chewy
Epsilon-amin6
- Epsilon-aminocaproic acid (EACA) is a synthetic inhibitor of the plasmin-plasminogen system. (nih.gov)
- Quantitative determination of plasma fibrinolytic activity in patients with ruptured intracranial aneurysms who are receiving epsilon-aminocaproic acid: relationship of possible complications of therapy to the degree of fibrinolytic inhibition. (nih.gov)
- Epsilon-aminocaproic acid myopathy. (nih.gov)
- Laboratory measures of hemostasis and fibrinolysis after intravenous administration of epsilon-aminocaproic acid in clinically normal horses and ponies. (oregonstate.edu)
- To determine whether epsilon-aminocaproic acid (EACA) administered IV affects hemostasis and fibrinolysis in clinically normal horses and ponies. (oregonstate.edu)
- Intravenous antifibrinolytics (e.g., epsilon-aminocaproic acid [EACA] and tranexamic acid) can be used for severe bleeding manifestations, including intracranial hemorrhage (with or without hematoma evacuation). (nih.gov)
Fibrinolysis5
- Aminocaproic Acid is 6-aminohexanoic acid, which acts as an inhibitor of fibrinolysis. (nih.gov)
- The fibrinolysis-inhibitory effects of aminocaproic acid appear to be exerted principally via inhibition of plasminogen activators and to a lesser degree through antiplasmin activity. (nih.gov)
- Aminocaproic Acid Injection is useful in enhancing hemostasis when fibrinolysis contributes to bleeding. (nih.gov)
- When there is uncertainty as to whether the cause of bleeding is primary fibrinolysis or disseminated intravascular coagulation (DIC), this distinction must be made before administering aminocaproic acid. (nih.gov)
- Aminocaproic acid works by inhibiting the process of fibrinolysis (the breakdown of fibrin, a protein needed for proper blood clotting) and can reverse states that are associated with excessive fibrinolysis. (totalhealthmagazine.com)
Tranexamic3
- Antifibrinolytic Use in the Perioperative Setting: Aminocaproic Acid and Tranexamic Acid. (nih.gov)
- this category of treatment products (or medicines) includes aminocaproic acid and tranexamic acid. (cdc.gov)
- Von Willebrand Disease Treatment: Desmopressin Acetate, Factor Replacement Therapy, Hormone Therapy, Aminocaproic Acid & Tranexamic Acid. (nih.gov)
Intravenous administration2
- Aminocaproic Acid Injection, USP, for intravenous administration, is a sterile pyrogen-free solution containing 250 mg/mL of Aminocaproic Acid with Benzyl Alcohol 0.9%, as a preservative, and Water for Injection q.s. (nih.gov)
- Correspondingly, the volume of distribution after intravenous administration has been reported to be 30.0 ± 8.2 L. After prolonged administration, aminocaproic acid has been found to distribute throughout extravascular and intravascular compartments of the body, penetrating human red blood cells as well as other tissue cells. (nih.gov)
Silicon dioxide1
- Each aminocaproic acid Tablet, for oral administration contains 500 mg of aminocaproic acid USP and the following inactive ingredients: colloidal silicon dioxide, crospovidone, magnesium stearate, microcrystalline cellulose, povidone and stearic acid. (nih.gov)
Allergic2
- tell your doctor and pharmacist if you are allergic to aminocaproic acid or any other medications. (medlineplus.gov)
- Allergic contact dermatitis caused by ϵ-aminocaproic acid in a purified sodium hyaluronate ophthalmic solution. (bvsalud.org)
Amino acid4
- Arginine is an essential amino acid found in many foods. (totalhealthmagazine.com)
- Since arginine is an amino acid, supplementation is believed to be safe. (totalhealthmagazine.com)
- An epsilon-amino acid comprising hexanoic acid carrying an amino substituent at position C-6. (mcw.edu)
- Recombinant anthrax toxin protective antigen (rPA) with an amino acid sequence concurring with that from the Bacillus anthracis V770-NP1-R anthrax vaccine strain was obtained from the National Institute of Craniofacial and Dental Research, National Institutes of Health, Bethesda, MD. Antigen was stored frozen at -80°C in small aliquots (10-100 µL, 4.75 mg/mL) in 5 mM Hepes, pH 7.3. (cdc.gov)
Fibrinolytic1
- Some clinicians believe fibrinolytic inhibitors (e.g., aminocaproic acid) may be preferable in children and pregnant women because of hazardous adverse effects. (drugs.com)
Injection1
- Aminocaproic Acid Injection, USP contains benzyl alcohol as a preservative. (nih.gov)
Sodium1
- The pH is adjusted to approximately 6.8 with Hydrochloric Acid and/or Sodium Hydroxide. (nih.gov)
Urine3
- Sixty-five percent of the dose is recovered in the urine as unchanged drug and 11% of the dose appears as the metabolite adipic acid. (nih.gov)
- Aminocaproic acid is also used to control bleeding in the urinary tract (the organs in the body that produce and excrete urine) that may occur after prostate or kidney surgery or in people who have certain types of cancer. (medlineplus.gov)
- Alfalfa can make urine alkaline and is useful in those bladder conditions where a more alkaline urine is needed (likewise, it should not be used in pets whose medical conditions require an acid urine). (totalhealthmagazine.com)
Drugs2
- Aminocaproic Acid and Cocaine Polydrug addiction is a way to counteract the adverse side effects of major drugs. (worldsbest.rehab)
- The screen flagged two drugs for their ability to inhibit RPE atrophy and drusen formation: A protease inhibitor called aminocaproic acid, which likely directly blocks the complement pathway outside cells and a second agent (L745), which stops complement induced inflammation inside the cell indirectly via inactivation of the dopamine pathway. (nih.gov)
Orally1
- Renal excretion is the primary route of elimination, whether aminocaproic acid is administered orally or intravenously. (nih.gov)
Doses1
- Fatty degeneration of the myocardium has been reported in dogs given intravenous doses of aminocaproic acid at 0.8 to 3.3 times the maximum human therapeutic dose and in monkeys given intravenous doses of aminocaproic acid at 6 times the maximum human therapeutic dose. (nih.gov)
Tablet1
- Aminocaproic acid comes as a tablet and a solution (liquid) to take by mouth. (medlineplus.gov)
Pregnant1
- If you become pregnant while taking aminocaproic acid, call your doctor. (medlineplus.gov)
Renal1
- In patients with upper urinary tract bleeding, aminocaproic acid administration has been known to cause intrarenal obstruction in the form of glomerular capillary thrombosis or clots in the renal pelvis and ureters. (nih.gov)
Decrease1
- Your doctor may start you on a high dose of aminocaproic acid and gradually decrease your dose as the bleeding is controlled. (medlineplus.gov)
Treatment2
- Aminocaproic acid should not be used to treat bleeding that is not caused by faster than normal clot breakdown, so your doctor may order tests to find the cause of your bleeding before you begin your treatment. (medlineplus.gov)
- The use of hyaluronic and aminocaproic acid in the treatment of alveolar osteitis. (nih.gov)
DESCRIPTION1
- The description Name of the medicinal product Aminocaproic Acid - Shanghai No.1 Biochem is an automatic translation from the original language. (pillintrip.com)
Blood3
- Aminocaproic acid is used to control bleeding that occurs when blood clots are broken down too quickly. (medlineplus.gov)
- While common, combining cocaine and Aminocaproic Acid together or even hours apart can be extremely risky because it increases heart rate and blood pressure, further increasing the risk of a heart attack. (worldsbest.rehab)
- Exposure to aminocaproic acid in the eye may affect the eye itself and the acid may be absorbed through the tear ducts into the blood. (canada.ca)
Urinary tract1
- For this reason, aminocaproic acid should not be used in hematuria of upper urinary tract origin, unless the possible benefits outweigh the risk. (nih.gov)
Increases2
- Even taking Cocaine without Aminocaproic Acid has a negative effect on the heart, and then taking Aminocaproic Acid with it increases the risk exponentially. (worldsbest.rehab)
- Taking Cocaine and Aminocaproic Acid actually increases the risk of a heart attack. (worldsbest.rehab)
Hours2
- The terminal elimination half-life for aminocaproic acid is approximately 2 hours. (nih.gov)
- When aminocaproic acid is used to treat ongoing bleeding, it is usually taken every 3 to 6 hours. (medlineplus.gov)
Made1
- Aminocaproic acid is made in a 250 mg/ml oral solution. (totalhealthmagazine.com)
Chemical1
- Cocaine and Aminocaproic Acid also react inside the liver to form a chemical known as cocaethylene, which is toxic to the heart, liver, and other organs. (worldsbest.rehab)
Patients1
- 18. Aminocaproic acid use in hospitalized patients with hematological malignancy: a case series. (nih.gov)
Affect1
- When mixed with Aminocaproic Acid, Cocaine can affect the body's ability to keep the correct temperature and heart function. (worldsbest.rehab)
Surgery1
- if you are having surgery, including dental surgery, tell the doctor or dentist that you are taking aminocaproic acid. (medlineplus.gov)
Days1
- This can also happen even if cocaine and Aminocaproic Acid are used separately for several consecutive days. (worldsbest.rehab)
Risk2
- Like death for example, which is always a risk when using Cocaine or mixing Cocaine and Aminocaproic Acid. (worldsbest.rehab)
- The risk associated with mixing Aminocaproic Acid and Cocaine causes cocaethylene to enter the bloodstream and harm the person's health, especially their tissues and organs, causing a euphoric effect as cocaine stimulates the brain. (worldsbest.rehab)