A single-chain polypeptide derived from bovine tissues consisting of 58 amino-acid residues. It is an inhibitor of proteolytic enzymes including CHYMOTRYPSIN; KALLIKREIN; PLASMIN; and TRYPSIN. It is used in the treatment of HEMORRHAGE associated with raised plasma concentrations of plasmin. It is also used to reduce blood loss and transfusion requirements in patients at high risk of major blood loss during and following open heart surgery with EXTRACORPOREAL CIRCULATION. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995)
Agents acting to arrest the flow of blood. Absorbable hemostatics arrest bleeding either by the formation of an artificial clot or by providing a mechanical matrix that facilitates clotting when applied directly to the bleeding surface. These agents function more at the capillary level and are not effective at stemming arterial or venous bleeding under any significant intravascular pressure.
Agents that prevent fibrinolysis or lysis of a blood clot or thrombus. Several endogenous antiplasmins are known. The drugs are used to control massive hemorrhage and in other coagulation disorders.
Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.
An antifibrinolytic agent that acts by inhibiting plasminogen activators which have fibrinolytic properties.
Antifibrinolytic hemostatic used in severe hemorrhage.
Loss of blood during a surgical procedure.
A form of SILICON DIOXIDE composed of skeletons of prehistoric aquatic plants which is used for its ABSORPTION quality, taking up 1.5-4 times its weight in water. The microscopic sharp edges are useful for insect control but can also be an inhalation hazard. It has been used in baked goods and animal feed. Kieselguhr is German for flint + earthy sediment.
Hemorrhage following any surgical procedure. It may be immediate or delayed and is not restricted to the surgical wound.
Diversion of the flow of blood from the entrance of the right atrium directly to the aorta (or femoral artery) via an oxygenator thus bypassing both the heart and lungs.
Amino derivatives of caproic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the amino caproic acid structure.
The time required by whole blood to produce a visible clot.
The introduction of whole blood or blood component directly into the blood stream. (Dorland, 27th ed)
Control of bleeding during or after surgery.
Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. Specifically, Kallikreins are potent vasodilators and hypotensives and increase vascular permeability and affect smooth muscle. They act as infertility agents in men. Three forms are recognized, PLASMA KALLIKREIN (EC 3.4.21.34), TISSUE KALLIKREIN (EC 3.4.21.35), and PROSTATE-SPECIFIC ANTIGEN (EC 3.4.21.77).
Surgery performed on the heart.
The most common mineral of a group of hydrated aluminum silicates, approximately H2Al2Si2O8-H2O. It is prepared for pharmaceutical and medicinal purposes by levigating with water to remove sand, etc. (From Merck Index, 11th ed) The name is derived from Kao-ling (Chinese: "high ridge"), the original site. (From Grant & Hackh's Chemical Dictionary, 5th ed)
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
Patient care procedures performed during the operation that are ancillary to the actual surgery. It includes monitoring, fluid therapy, medication, transfusion, anesthesia, radiography, and laboratory tests.
A generic term used to describe a group of polypeptides with related chemical structures and pharmacological properties that are widely distributed in nature. These peptides are AUTACOIDS that act locally to produce pain, vasodilatation, increased vascular permeability, and the synthesis of prostaglandins. Thus, they comprise a subset of the large number of mediators that contribute to the inflammatory response. (From Goodman and Gilman's The Pharmacologic Basis of Therapeutics, 8th ed, p588)
Surgery performed on the thoracic organs, most commonly the lungs and the heart.
A product of the lysis of plasminogen (profibrinolysin) by PLASMINOGEN activators. It is composed of two polypeptide chains, light (B) and heavy (A), with a molecular weight of 75,000. It is the major proteolytic enzyme involved in blood clot retraction or the lysis of fibrin and quickly inactivated by antiplasmins.
A technique to arrest the flow of blood by lowering BODY TEMPERATURE to about 20 degrees Centigrade, usually achieved by infusing chilled perfusate. The technique provides a bloodless surgical field for complex surgeries.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds.
Abnormally low BLOOD PRESSURE that can result in inadequate blood flow to the brain and other vital organs. Common symptom is DIZZINESS but greater negative impacts on the body occur when there is prolonged depravation of oxygen and nutrients.
A pancreatic trypsin inhibitor common to all mammals. It is secreted with the zymogens into the pancreatic juice. It is a protein composed of 56 amino acid residues and is different in amino acid composition and physiological activity from the Kunitz bovine pancreatic trypsin inhibitor (APROTININ).
Subtype of CLOSTRIDIUM BOTULINUM that produces botulinum toxin type B which is neurotoxic to humans and animals.

Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions. (1/706)

Insulin-like growth factor (IGF) I does not quantitatively form its three native disulfide bonds in the presence of 10 mM reduced and 1 mM oxidized glutathione in vitro [Hober, S. et al. (1992) Biochemistry 31, 1749-1756]. In this paper, we show (i) that both IGF-I and IGF-II are unable to form and maintain their native disulfide bonds at redox conditions that are similar to the situation in the secretory vesicles in vivo and (ii) that the presence of protein disulfide isomerase does not overcome this problem. The results indicate that the previously described thermodynamic disulfide exchange folding problem of IGF-I in vitro is also present in vivo. Speculatively, we suggest that the thermodynamic disulfide exchange properties of IGF-I and II are biologically significant for inactivation of the unbound growth factors by disulfide exchange reactions to generate variants destined for rapid clearance.  (+info)

Activation of Xenopus eggs by proteases: possible involvement of a sperm protease in fertilization. (2/706)

Egg activation in cross-fertilization between Xenopus eggs and Cynops sperm may be caused by a protease activity against Boc-Gly-Arg-Arg-MCA in the sperm acrosome. To determine the role of the sperm protease in fertilization, the protease was purified from Cynops sperm using several chromatographic techniques. We found that purified sperm protease readily hydrolyzes Boc-Gly-Arg-Arg-MCA and Z-Arg-Arg-MCA, that protease activity was inhibited by the trypsin inhibitors aprotinin and leupeptin, and that not only the purified protease, but also cathepsin B, induces activation in Xenopus eggs. We inseminated unfertilized Xenopus eggs with homologous sperm in the presence of various peptidyl MCA substrates or protease inhibitors and demonstrated that trypsin inhibitors or MCA substrates containing Arg-Arg-MCA reversibly inhibited fertilization of both fully jellied and denuded eggs. Sperm motility was not affected by the reagents. An extract obtained from Xenopus sperm showed hydrolytic activity against Boc-Gly-Arg-Arg-MCA, Z-Arg-Arg-MCA, and Arg-MCA. These results suggest that the tryptic protease in Xenopus sperm is involved in fertilization, most likely by participating in egg activation.  (+info)

Allosteric modulation of BPTI interaction with human alpha- and zeta-thrombin. (3/706)

In this study, thrombin interaction with the basic pancreatic trypsin inhibitor (BPTI) was investigated in the presence of different allosteric modulators of thrombin, that is the C-terminal hirudin peptide 54-65 (Hir54-65), a recombinant thrombomodulin form (TMEGF4-6) and Na+. BPTI binding to alpha-thrombin is positively linked to Na+. Under low sodium concentration (5 mM Na+) the BPTI affinity for alpha-thrombin was roughly threefold lower than in the presence of 150 mM sodium (Ki = 320 microM vs. 100 microM). The hirudin fragment, which binds to the fibrinogen recognition site (FRS) of thrombin, induced a progressive and saturable decrease (3.6-fold) of alpha-thrombin affinity for BPTI, whereas the thrombomodulin peptide, which binds to a more extended region of FRS, caused a 5.5-fold increase of the enzyme affinity for the inhibitor. The opposite effect exerted by Hir54-65 and TMEGF4-6 was also observed for BPTI interaction with zeta-thrombin, in which the amidic bond between W148 and T149 is cleaved. However, in this case the effect by Hir54-65 and TMEGF4-6, although qualitatively similar to that observed with alpha-thrombin, had a smaller magnitude. Thrombin hydrolysis of Protein C was also differently affected by Hir54-65 and TMEGF4-6 peptides. While the latter enhanced the Protein C activation, the former caused a reduction of both alpha- and zeta-thrombin kcat/K(m)' for Protein C cleavage. These results showed that (a) Na+ facilitates BPTI interaction with thrombin; (b) Hir54-65 and TMEGF4-6, though sharing in part the same binding site at the thrombin FRS, can affect in opposite way thrombin's interaction with BPTI and Protein C; (c) such findings along with the results obtained with zeta-thrombin might be explained by admitting that the thermodynamic linkage between FRS and the critical W60-loop is also controlled by ligation and/or conformational state of the W148 insertion loop.  (+info)

Strategy for balancing anticoagulation and hemostasis in aortocoronary bypass surgery: blood conservation and graft patency. (4/706)

The minimal effective dose of aprotinin on hemostasis under normothermic perfusion, the influence of anticoagulant therapy on graft patency, and the thromboembolic and hemorrhagic events were investigated after aortocoronary bypass graft operation (CABG). One hundred CABG patients under normothermic perfusion were randomly divided into the following groups: (1) coumadin plus acetylsalicylic acid (ASA) (n=32); no aprotinin used during cardiopulmonary bypass (CPB); (2) minimal-dose, 10(6) KIU during CPB, aprotinin used, followed by ASA and coumadin (n=36); and (3) very low-dose, total of 2x10(6) KIU before CPB and during CPB; aprotinin used; anticoagulation therapy with heparin early after surgery and followed by replacement with ASA and coumadin (n=32). The patency of arterial grafts was 100% in all groups. The patency of vein grafts was 95-98% and there was no difference among the groups. The blood loss was significantly reduced in both aprotinin groups (groups 2 and 3) compared to the coumadin plus ASA group, although no difference existed between the 2 aprotinin groups. Postoperative thrombotic and hemorrhagic events were not observed in any group. From this study, it was concluded that 10(6) KIU aprotinin in pump-prime-only followed by oral ASA and coumadin was the recommendation from the benefit/cost consideration.  (+info)

Comparison of anionic and cationic trypsinogens: the anionic activation domain is more flexible in solution and differs in its mode of BPTI binding in the crystal structure. (5/706)

Unlike bovine cationic trypsin, rat anionic trypsin retains activity at high pH. This alkaline stability has been attributed to stabilization of the salt bridge between the N-terminal Ile16 and Asp194 by the surface negative charge (Soman K, Yang A-S, Honig B, Fletterick R., 1989, Biochemistry 28:9918-9926). The formation of this salt bridge controls the conformation of the activation domain in trypsin. In this work we probe the structure of rat trypsinogen to determine the effects of the surface negative charge on the activation domain in the absence of the Ile16-Asp194 salt bridge. We determined the crystal structures of the rat trypsin-BPTI complex and the rat trypsinogen-BPTI complex at 1.8 and 2.2 A, respectively. The BPTI complex of rat trypsinogen resembles that of rat trypsin. Surprisingly, the side chain of Ile16 is found in a similar position in both the rat trypsin and trypsinogen complexes, although it is not the N-terminal residue and cannot form the salt bridge in trypsinogen. The resulting position of the activation peptide alters the conformation of the adjacent autolysis loop (residues 142-153). While bovine trypsinogen and trypsin have similar CD spectra, the CD spectrum of rat trypsinogen has only 60% of the intensity of rat trypsin. This lower intensity most likely results from increased flexibility around two conserved tryptophans, which are adjacent to the activation domain. The NMR spectrum of rat trypsinogen contains high field methyl signals as observed in bovine trypsinogen. It is concluded that the activation domain of rat trypsinogen is more flexible than that of bovine trypsinogen, but does not extend further into the protein core.  (+info)

Effect of glycerol on the interactions and solubility of bovine pancreatic trypsin inhibitor. (6/706)

The effects of additives used to stabilize protein structure during crystallization on protein solution phase behavior are poorly understood. Here we investigate the effect of glycerol and ionic strength on the solubility and strength of interactions of the bovine pancreatic trypsin inhibitor. These two variables are found to have opposite effects on the intermolecular forces; attractions increase with [NaCl], whereas repulsions increase with glycerol concentration. These changes are mirrored in bovine pancreatic trypsin inhibitor solubility where the typical salting out behavior for NaCl is observed with higher solubility found in buffers containing glycerol. The increased repulsions induced by glycerol can be explained by a number of possible mechanisms, all of which require small changes in the protein or the solvent in its immediate vicinity. Bovine pancreatic trypsin inhibitor follows the same general phase behavior as other globular macromolecules where a robust correlation between protein solution second virial coefficient and solubility has been developed. This study extends previous reports of this correlation to solution conditions involving nonelectrolyte additives.  (+info)

Hydroiodic acid attachment kinetics as a chemical probe of gaseous protein ion structure: bovine pancreatic trypsin inhibitor. (7/706)

The kinetics of attachment of hydroiodic acid (HI) to the (M + 6H)6+ ions of native and reduced forms of bovine pancreatic trypsin inhibitor (BPTI) in the quadrupole ion trap environment are reported. Distinctly nonlinear (pseudo first-order) reaction kinetics are observed for reaction of the native ions, indicating two or more noninterconverting structures in the parent ion population. The reduced form, on the other hand, shows very nearly linear reaction kinetics. Both forms of the parent ion attach a maximum of five molecules of hydroiodic acid. This number is expected based on the amino acid composition of the protein. There is a total of 11 strongly basic sites in the protein (i.e., six arginines, four lysines, and one N-terminus). An ion with protons occupying six of the basic sites has five available for hydroiodic acid attachment. The kinetics of successive attachment of HI to the native and reduced forms of BPTI also differ, particularly for the addition of the fourth and fifth HI molecules. A very simple kinetic model describes the behavior of the reduced form reasonably well, suggesting that all of the neutral basic sites in the reduced BPTI ions have roughly equal reactivity. However, the behavior of the native ion is not well-described by this simple model. The results are discussed within the context of differences in the three-dimensional structures of the ions that result from the presence or absence of the three disulfide linkages found in native BPTI. The HI reaction kinetics appears to have potential as a chemical probe of protein ion three-dimensional structure in the gas phase. Hydroiodic acid attachment chemistry is significantly different from other chemistries used to probe three-dimensional structure and hence, promises to yield complementary information.  (+info)

Urokinase receptor (uPAR, CD87) is a platelet receptor important for kinetics and TNF-induced endothelial adhesion in mice. (8/706)

BACKGROUND: Urokinase plasminogen activator receptor (uPAR, CD87) is a widely distributed 55-kD, glycoprotein I-anchored surface receptor. On binding of its ligand uPA, it is known to increase leukocyte adhesion and traffic. Using genetically deficient mice, we explored the role of uPAR in platelet kinetics and TNF-induced platelet consumption. METHODS AND RESULTS: Anti-uPAR antibody stained platelets from normal (+/+) but not from uPAR-/- mice, as seen by fluorescence-activated cell sorter analysis. 51Cr-labeled platelets from uPAR-/- donors survived longer than those from +/+ donors when injected into a +/+ recipient. Intratracheal TNF injection induced thrombocytopenia and a platelet pulmonary localization, pronounced in +/+ but absent in uPAR-/- mice. Aprotinin, a plasmin inhibitor, decreased TNF-induced thrombocytopenia. TNF injection markedly reduced the survival and increased the pulmonary localization of 51Cr-labeled platelets from +/+ but not from uPAR-/- donors, indicating that it is the platelet uPAR that is critical for their response to TNF. As seen by electron microscopy, TNF injection increased the number of platelets and polymorphonuclear neutrophils (PMNs) in the alveolar capillaries of +/+ mice, whereas in uPAR-/- mice, platelet trapping was insignificant and PMN trapping was slightly reduced. Platelets within alveolar capillaries of TNF-injected mice were activated, as judged from their shape, and this was evident in +/+ but not in uPAR-/- mice. CONCLUSIONS: These results demonstrate for the first time the critical role of platelet uPAR for kinetics as well as for activation and endothelium adhesion associated with inflammation.  (+info)

Aprotinin is a medication that belongs to a class of drugs called serine protease inhibitors. It works by inhibiting the activity of certain enzymes in the body that can cause tissue damage and bleeding. Aprotinin is used in medical procedures such as heart bypass surgery to reduce blood loss and the need for blood transfusions. It is administered intravenously and its use is typically stopped a few days after the surgical procedure.

Aprotinin was first approved for use in the United States in 1993, but its use has been restricted or withdrawn in many countries due to concerns about its safety. In 2006, a study found an increased risk of kidney damage and death associated with the use of aprotinin during heart bypass surgery, leading to its withdrawal from the market in Europe and Canada. However, it is still available for use in the United States under a restricted access program.

It's important to note that the use of aprotinin should be carefully considered and discussed with the healthcare provider, taking into account the potential benefits and risks of the medication.

Hemostatics are substances or agents that promote bleeding cessation or prevent the spread of bleeding. They can act in various ways, such as by stimulating the body's natural clotting mechanisms, constricting blood vessels to reduce blood flow, or forming a physical barrier to block the bleeding site.

Hemostatics are often used in medical settings to manage wounds, injuries, and surgical procedures. They can be applied directly to the wound as a powder, paste, or gauze, or they can be administered systemically through intravenous injection. Examples of hemostatic agents include fibrin sealants, collagen-based products, thrombin, and oxidized regenerated cellulose.

It's important to note that while hemostatics can be effective in controlling bleeding, they should be used with caution and only under the guidance of a healthcare professional. Inappropriate use or overuse of hemostatic agents can lead to complications such as excessive clotting, thrombosis, or tissue damage.

Antifibrinolytic agents are a class of medications that inhibit the breakdown of blood clots. They work by blocking the action of enzymes called plasminogen activators, which convert plasminogen to plasmin, the main enzyme responsible for breaking down fibrin, a protein that forms the framework of a blood clot.

By preventing the conversion of plasminogen to plasmin, antifibrinolytic agents help to stabilize existing blood clots and prevent their premature dissolution. These medications are often used in clinical settings where excessive bleeding is a concern, such as during or after surgery, childbirth, or trauma.

Examples of antifibrinolytic agents include tranexamic acid, aminocaproic acid, and epsilon-aminocaproic acid. While these medications can be effective in reducing bleeding, they also carry the risk of thromboembolic events, such as deep vein thrombosis or pulmonary embolism, due to their pro-coagulant effects. Therefore, they should be used with caution and only under the close supervision of a healthcare provider.

Serine proteinase inhibitors, also known as serine protease inhibitors or serpins, are a group of proteins that inhibit serine proteases, which are enzymes that cut other proteins in a process called proteolysis. Serine proteinases are important in many biological processes such as blood coagulation, fibrinolysis, inflammation and cell death. The inhibition of these enzymes by serpin proteins is an essential regulatory mechanism to maintain the balance and prevent uncontrolled proteolytic activity that can lead to diseases.

Serpins work by forming a covalent complex with their target serine proteinases, irreversibly inactivating them. The active site of serpins contains a reactive center loop (RCL) that mimics the protease's target protein sequence and acts as a bait for the enzyme. When the protease cleaves the RCL, it gets trapped within the serpin structure, leading to its inactivation.

Serpin proteinase inhibitors play crucial roles in various physiological processes, including:

1. Blood coagulation and fibrinolysis regulation: Serpins such as antithrombin, heparin cofactor II, and protease nexin-2 control the activity of enzymes involved in blood clotting and dissolution to prevent excessive or insufficient clot formation.
2. Inflammation modulation: Serpins like α1-antitrypsin, α2-macroglobulin, and C1 inhibitor regulate the activity of proteases released during inflammation, protecting tissues from damage.
3. Cell death regulation: Some serpins, such as PI-9/SERPINB9, control apoptosis (programmed cell death) by inhibiting granzyme B, a protease involved in this process.
4. Embryonic development and tissue remodeling: Serpins like plasminogen activator inhibitor-1 (PAI-1) and PAI-2 regulate the activity of enzymes involved in extracellular matrix degradation during embryonic development and tissue remodeling.
5. Neuroprotection: Serpins such as neuroserpin protect neurons from damage by inhibiting proteases released during neuroinflammation or neurodegenerative diseases.

Dysregulation of serpins has been implicated in various pathological conditions, including thrombosis, emphysema, Alzheimer's disease, and cancer. Understanding the roles of serpins in these processes may provide insights into potential therapeutic strategies for treating these diseases.

Aminocaproic acid is an antifibrinolytic medication, which means it helps to prevent the breakdown of blood clots. It works by blocking plasmin, an enzyme in your body that dissolves blood clots.

This drug is used for the treatment of bleeding conditions due to various causes, such as:

1. Excessive menstrual bleeding (menorrhagia)
2. Bleeding after tooth extraction or surgery
3. Hematuria (blood in urine) due to certain medical procedures or conditions like kidney stones
4. Intracranial hemorrhage (bleeding inside the skull)
5. Hereditary angioedema, a genetic disorder that causes swelling of various parts of the body

Aminocaproic acid is available in oral and injectable forms. Common side effects include nausea, vomiting, diarrhea, and headache. Serious side effects are rare but may include allergic reactions, seizures, or vision changes. It's essential to use this medication under the supervision of a healthcare professional, as improper usage might lead to blood clots, stroke, or other severe complications.

Tranexamic acid is an antifibrinolytic medication that is used to reduce or prevent bleeding. It works by inhibiting the activation of plasminogen to plasmin, which is a protease that degrades fibrin clots. By preventing the breakdown of blood clots, tranexamic acid helps to reduce bleeding and promote clot formation.

Tranexamic acid is available in various forms, including tablets, capsules, and injectable solutions. It is used in a variety of clinical settings, such as surgery, trauma, and heavy menstrual bleeding. The medication can be taken orally or administered intravenously, depending on the severity of the bleeding and the patient's medical condition.

Common side effects of tranexamic acid include nausea, vomiting, diarrhea, and headache. Less commonly, the medication may cause allergic reactions, visual disturbances, or seizures. It is important to follow the prescribing physician's instructions carefully when taking tranexamic acid to minimize the risk of side effects and ensure its safe and effective use.

Surgical blood loss is the amount of blood that is lost during a surgical procedure. It can occur through various routes such as incisions, punctures or during the removal of organs or tissues. The amount of blood loss can vary widely depending on the type and complexity of the surgery being performed.

Surgical blood loss can be classified into three categories:

1. Insensible losses: These are small amounts of blood that are lost through the skin, respiratory tract, or gastrointestinal tract during surgery. They are not usually significant enough to cause any clinical effects.
2. Visible losses: These are larger amounts of blood that can be seen and measured directly during surgery. They may require transfusion or other interventions to prevent hypovolemia (low blood volume) and its complications.
3. Hidden losses: These are internal bleeding that cannot be easily seen or measured during surgery. They can occur in the abdominal cavity, retroperitoneal space, or other areas of the body. They may require further exploration or imaging studies to diagnose and manage.

Surgical blood loss can lead to several complications such as hypovolemia, anemia, coagulopathy (disorders of blood clotting), and organ dysfunction. Therefore, it is essential to monitor and manage surgical blood loss effectively to ensure optimal patient outcomes.

Diatomaceous earth is not a medical term, but a natural product derived from the fossilized remains of diatoms, a type of algae. It is composed of silica and other minerals. While it has various industrial and agricultural uses, it is not typically used as a medication or treatment. However, some people may use food-grade diatomaceous earth for various health purposes, such as detoxification or improving digestive health, but these uses are not supported by scientific evidence and its safety and effectiveness for these purposes have not been established. As with any substance used for medicinal purposes, it is important to consult with a healthcare provider before using diatomaceous earth.

Postoperative hemorrhage is a medical term that refers to bleeding that occurs after a surgical procedure. This condition can range from minor oozing to severe, life-threatening bleeding. Postoperative hemorrhage can occur soon after surgery or even several days later, as the surgical site begins to heal.

The causes of postoperative hemorrhage can vary, but some common factors include:

1. Inadequate hemostasis during surgery: This means that all bleeding was not properly controlled during the procedure, leading to bleeding after surgery.
2. Blood vessel injury: During surgery, blood vessels may be accidentally cut or damaged, causing bleeding after the procedure.
3. Coagulopathy: This is a condition in which the body has difficulty forming blood clots, increasing the risk of postoperative hemorrhage.
4. Use of anticoagulant medications: Medications that prevent blood clots can increase the risk of bleeding after surgery.
5. Infection: An infection at the surgical site can cause inflammation and bleeding.

Symptoms of postoperative hemorrhage may include swelling, pain, warmth, or discoloration around the surgical site, as well as signs of shock such as rapid heartbeat, low blood pressure, and confusion. Treatment for postoperative hemorrhage depends on the severity of the bleeding and may include medications to control bleeding, transfusions of blood products, or additional surgery to stop the bleeding.

Cardiopulmonary bypass (CPB) is a medical procedure that temporarily takes over the functions of the heart and lungs during major heart surgery. It allows the surgeon to operate on a still, bloodless heart.

During CPB, the patient's blood is circulated outside the body with the help of a heart-lung machine. The machine pumps the blood through a oxygenator, where it is oxygenated and then returned to the body. This bypasses the heart and lungs, hence the name "cardiopulmonary bypass."

CPB involves several components, including a pump, oxygenator, heat exchanger, and tubing. The patient's blood is drained from the heart through cannulas (tubes) and passed through the oxygenator, where it is oxygenated and carbon dioxide is removed. The oxygenated blood is then warmed to body temperature in a heat exchanger before being pumped back into the body.

While on CPB, the patient's heart is stopped with the help of cardioplegia solution, which is infused directly into the coronary arteries. This helps to protect the heart muscle during surgery. The surgeon can then operate on a still and bloodless heart, allowing for more precise surgical repair.

After the surgery is complete, the patient is gradually weaned off CPB, and the heart is restarted with the help of electrical stimulation or medication. The patient's condition is closely monitored during this time to ensure that their heart and lungs are functioning properly.

While CPB has revolutionized heart surgery and allowed for more complex procedures to be performed, it is not without risks. These include bleeding, infection, stroke, kidney damage, and inflammation. However, with advances in technology and technique, the risks associated with CPB have been significantly reduced over time.

Aminocaproates are a group of chemical compounds that contain an amino group and a carboxylic acid group, as well as a straight or branched alkyl chain with 6-10 carbon atoms. They are often used in medical settings as anti-fibrinolytic agents, which means they help to prevent the breakdown of blood clots.

One example of an aminocaproate is epsilon-aminocaproic acid (EACA), which is a synthetic analogue of the amino acid lysine. EACA works by inhibiting the activation of plasminogen to plasmin, which is an enzyme that breaks down blood clots. By doing so, EACA can help to reduce bleeding and improve clot stability in certain medical conditions, such as hemophilia or following surgery.

Other aminocaproates include tranexamic acid (TXA) and 4-aminoethylbenzoic acid (AEBA), which also have anti-fibrinolytic properties and are used in similar clinical settings. However, it's important to note that these medications can increase the risk of thrombosis (blood clots) if not used properly, so they should only be administered under the close supervision of a healthcare provider.

Whole Blood Coagulation Time (WBCT) is not a standard term used in medical literature. However, I believe you may be referring to "bleeding time" or "coagulation time" which are tests used to evaluate the function of the blood's clotting system.

Bleeding time is a measure of how long it takes for bleeding to stop after a small cut is made in the skin. It helps assess the function of the platelets and the smaller blood vessels.

Coagulation time, on the other hand, measures the time it takes for a larger clot to form in whole blood. This test is not commonly used in clinical practice.

It's important to note that these tests have largely been replaced by more specific coagulation tests, such as prothrombin time (PT) and activated partial thromboplastin time (aPTT), which provide more detailed information about the different components of the clotting system.

A blood transfusion is a medical procedure in which blood or its components are transferred from one individual (donor) to another (recipient) through a vein. The donated blood can be fresh whole blood, packed red blood cells, platelets, plasma, or cryoprecipitate, depending on the recipient's needs. Blood transfusions are performed to replace lost blood due to severe bleeding, treat anemia, support patients undergoing major surgeries, or manage various medical conditions such as hemophilia, thalassemia, and leukemia. The donated blood must be carefully cross-matched with the recipient's blood type to minimize the risk of transfusion reactions.

Surgical hemostasis refers to the methods and techniques used during surgical procedures to stop bleeding or prevent hemorrhage. This can be achieved through various means, including the use of surgical instruments such as clamps, ligatures, or staples to physically compress blood vessels and stop the flow of blood. Electrosurgical tools like cautery may also be used to coagulate and seal off bleeding vessels using heat. Additionally, topical hemostatic agents can be applied to promote clotting and control bleeding in wounded tissues. Effective surgical hemostasis is crucial for ensuring a successful surgical outcome and minimizing the risk of complications such as excessive blood loss, infection, or delayed healing.

Kallikreins are a group of serine proteases, which are enzymes that help to break down other proteins. They are found in various tissues and body fluids, including the pancreas, kidneys, and saliva. In the body, kallikreins play important roles in several physiological processes, such as blood pressure regulation, inflammation, and fibrinolysis (the breakdown of blood clots).

There are two main types of kallikreins: tissue kallikreins and plasma kallikreins. Tissue kallikreins are primarily involved in the activation of kininogen, a protein that leads to the production of bradykinin, a potent vasodilator that helps regulate blood pressure. Plasma kallikreins, on the other hand, play a key role in the coagulation cascade by activating factors XI and XII, which ultimately lead to the formation of a blood clot.

Abnormal levels or activity of kallikreins have been implicated in various diseases, including cancer, cardiovascular disease, and inflammatory disorders. For example, some studies suggest that certain tissue kallikreins may promote tumor growth and metastasis, while others indicate that they may have protective effects against cancer. Plasma kallikreins have also been linked to the development of thrombosis (blood clots) and inflammation in cardiovascular disease.

Overall, kallikreins are important enzymes with diverse functions in the body, and their dysregulation has been associated with various pathological conditions.

Cardiac surgical procedures are operations that are performed on the heart or great vessels (the aorta and vena cava) by cardiothoracic surgeons. These surgeries are often complex and require a high level of skill and expertise. Some common reasons for cardiac surgical procedures include:

1. Coronary artery bypass grafting (CABG): This is a surgery to improve blood flow to the heart in patients with coronary artery disease. During the procedure, a healthy blood vessel from another part of the body is used to create a detour around the blocked or narrowed portion of the coronary artery.
2. Valve repair or replacement: The heart has four valves that control blood flow through and out of the heart. If one or more of these valves become damaged or diseased, they may need to be repaired or replaced. This can be done using artificial valves or valves from animal or human donors.
3. Aneurysm repair: An aneurysm is a weakened area in the wall of an artery that can bulge out and potentially rupture. If an aneurysm occurs in the aorta, it may require surgical repair to prevent rupture.
4. Heart transplantation: In some cases, heart failure may be so severe that a heart transplant is necessary. This involves removing the diseased heart and replacing it with a healthy donor heart.
5. Arrhythmia surgery: Certain types of abnormal heart rhythms (arrhythmias) may require surgical treatment. One such procedure is called the Maze procedure, which involves creating a pattern of scar tissue in the heart to disrupt the abnormal electrical signals that cause the arrhythmia.
6. Congenital heart defect repair: Some people are born with structural problems in their hearts that require surgical correction. These may include holes between the chambers of the heart or abnormal blood vessels.

Cardiac surgical procedures carry risks, including bleeding, infection, stroke, and death. However, for many patients, these surgeries can significantly improve their quality of life and longevity.

Kaolin is not a medical term per se, but it is a mineral that has various applications in the medical field. Medically, kaolin is used as an ingredient in some over-the-counter (OTC) medications and clinical products, particularly in oral and topical formulations.

Medical definition: Kaolin is a natural hydrated aluminum silicate clay mineral (with the chemical formula Al2Si2O5(OH)4) used in medical applications as an antidiarrheal agent and as a component in various dermatological products for its absorbent, protective, and soothing properties.

Protease inhibitors are a class of antiviral drugs that are used to treat infections caused by retroviruses, such as the human immunodeficiency virus (HIV), which is responsible for causing AIDS. These drugs work by blocking the activity of protease enzymes, which are necessary for the replication and multiplication of the virus within infected cells.

Protease enzymes play a crucial role in the life cycle of retroviruses by cleaving viral polyproteins into functional units that are required for the assembly of new viral particles. By inhibiting the activity of these enzymes, protease inhibitors prevent the virus from replicating and spreading to other cells, thereby slowing down the progression of the infection.

Protease inhibitors are often used in combination with other antiretroviral drugs as part of highly active antiretroviral therapy (HAART) for the treatment of HIV/AIDS. Common examples of protease inhibitors include saquinavir, ritonavir, indinavir, and atazanavir. While these drugs have been successful in improving the outcomes of people living with HIV/AIDS, they can also cause side effects such as nausea, diarrhea, headaches, and lipodystrophy (changes in body fat distribution).

Intraoperative care refers to the medical care and interventions provided to a patient during a surgical procedure. This care is typically administered by a team of healthcare professionals, including anesthesiologists, surgeons, nurses, and other specialists as needed. The goal of intraoperative care is to maintain the patient's physiological stability throughout the surgery, minimize complications, and ensure the best possible outcome.

Intraoperative care may include:

1. Anesthesia management: Administering and monitoring anesthetic drugs to keep the patient unconscious and free from pain during the surgery.
2. Monitoring vital signs: Continuously tracking the patient's heart rate, blood pressure, oxygen saturation, body temperature, and other key physiological parameters to ensure they remain within normal ranges.
3. Fluid and blood product administration: Maintaining adequate intravascular volume and oxygen-carrying capacity through the infusion of fluids and blood products as needed.
4. Intraoperative imaging: Utilizing real-time imaging techniques, such as X-ray, ultrasound, or CT scans, to guide the surgical procedure and ensure accurate placement of implants or other devices.
5. Neuromonitoring: Using electrophysiological methods to monitor the functional integrity of nerves and neural structures during surgery, particularly in procedures involving the brain, spine, or peripheral nerves.
6. Intraoperative medication management: Administering various medications as needed for pain control, infection prophylaxis, or the treatment of medical conditions that may arise during the surgery.
7. Temperature management: Regulating the patient's body temperature to prevent hypothermia or hyperthermia, which can have adverse effects on surgical outcomes and overall patient health.
8. Communication and coordination: Ensuring effective communication among the members of the surgical team to optimize patient care and safety.

Kinins are a group of endogenous inflammatory mediators that are involved in the body's response to injury or infection. They are derived from the decapeptide bradykinin and its related peptides, which are formed by the enzymatic cleavage of precursor proteins called kininogens.

Kinins exert their effects through the activation of specific G protein-coupled receptors, known as B1 and B2 receptors. These receptors are widely distributed throughout the body, including in the cardiovascular, respiratory, gastrointestinal, and nervous systems.

Activation of kinin receptors leads to a range of physiological responses, including vasodilation, increased vascular permeability, pain, and smooth muscle contraction. Kinins are also known to interact with other inflammatory mediators, such as prostaglandins and leukotrienes, to amplify the inflammatory response.

In addition to their role in inflammation, kinins have been implicated in a number of pathological conditions, including hypertension, asthma, arthritis, and pain. As such, kinin-targeted therapies are being explored as potential treatments for these and other diseases.

Thoracic surgical procedures refer to the operations that are performed on the thorax, which is the part of the body that lies between the neck and the abdomen and includes the chest cage, lungs, heart, great blood vessels, esophagus, diaphragm, and other organs in the chest cavity. These surgical procedures can be either open or minimally invasive (using small incisions and specialized instruments) and are performed to diagnose, treat, or manage various medical conditions affecting the thoracic organs, such as:

1. Lung cancer: Thoracic surgeons perform lung resections (lobectomy, segmentectomy, wedge resection) to remove cancerous lung tissue. They may also perform mediastinal lymph node dissection to assess the spread of the disease.
2. Esophageal surgery: Surgeries like esophagectomy are performed to treat esophageal cancer or other conditions affecting the esophagus, such as severe GERD (gastroesophageal reflux disease).
3. Chest wall surgery: This includes procedures to repair or replace damaged ribs, sternum, or chest wall muscles and treat conditions like pectus excavatum or tumors in the chest wall.
4. Heart surgery: Thoracic surgeons collaborate with cardiac surgeons to perform surgeries on the heart, such as coronary artery bypass grafting (CABG), valve repair/replacement, and procedures for treating aneurysms or dissections of the aorta.
5. Diaphragm surgery: Procedures like diaphragm plication are performed to treat paralysis or weakness of the diaphragm that can lead to respiratory insufficiency.
6. Mediastinal surgery: This involves operating on the mediastinum, the area between the lungs, to remove tumors, cysts, or other abnormal growths.
7. Pleural surgery: Procedures like pleurodesis or decortication are performed to manage conditions affecting the pleura (the membrane surrounding the lungs), such as pleural effusions, pneumothorax, or empyema.
8. Lung surgery: Thoracic surgeons perform procedures on the lungs, including lobectomy, segmentectomy, or pneumonectomy to treat lung cancer, benign tumors, or other lung diseases.
9. Tracheal surgery: This includes procedures to repair or reconstruct damaged trachea or remove tumors and growths in the airway.
10. Esophageal surgery: Collaborating with general surgeons, thoracic surgeons perform esophagectomy and other procedures to treat esophageal cancer, benign tumors, or other conditions affecting the esophagus.

Fibrinolysin is defined as a proteolytic enzyme that dissolves or breaks down fibrin, a protein involved in the clotting of blood. This enzyme is produced by certain cells, such as endothelial cells that line the interior surface of blood vessels, and is an important component of the body's natural mechanism for preventing excessive blood clotting and maintaining blood flow.

Fibrinolysin works by cleaving specific bonds in the fibrin molecule, converting it into soluble degradation products that can be safely removed from the body. This process is known as fibrinolysis, and it helps to maintain the balance between clotting and bleeding in the body.

In medical contexts, fibrinolysin may be used as a therapeutic agent to dissolve blood clots that have formed in the blood vessels, such as those that can occur in deep vein thrombosis or pulmonary embolism. It is often administered in combination with other medications that help to enhance its activity and specificity for fibrin.

Deep hypothermic circulatory arrest (DHCA) is a medical procedure in which the body temperature is lowered to around 15-20°C (59-68°F), and the circulation of blood is temporarily stopped. This technique is often used during complex cardiac surgeries, such as aortic arch reconstruction or repair of congenital heart defects, to reduce the body's metabolic demand for oxygen and allow surgeons to operate in a still and bloodless field.

During DHCA, the patient is connected to a heart-lung machine that takes over the function of pumping blood and oxygenating it. The blood is then cooled down using a cooling device before being returned to the body. Once the body temperature reaches the desired level, the circulation is stopped for a short period, usually no more than 30 minutes, during which time the surgeon can work on the heart or great vessels.

After the surgical procedure is complete, the patient is gradually rewarmed, and the circulation is restarted. DHCA carries some risks, including neurological complications such as stroke, cognitive impairment, or delirium, but it remains an important tool in complex cardiac surgery.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

Trypsin inhibitors are substances that inhibit the activity of trypsin, an enzyme that helps digest proteins in the small intestine. Trypsin inhibitors can be found in various foods such as soybeans, corn, and raw egg whites. In the case of soybeans, trypsin inhibitors are denatured and inactivated during cooking and processing.

In a medical context, trypsin inhibitors may be used therapeutically to regulate excessive trypsin activity in certain conditions such as pancreatitis, where there is inflammation of the pancreas leading to the release of activated digestive enzymes, including trypsin, into the pancreas and surrounding tissues. By inhibiting trypsin activity, these inhibitors can help reduce tissue damage and inflammation.

Hypotension is a medical term that refers to abnormally low blood pressure, usually defined as a systolic blood pressure less than 90 millimeters of mercury (mm Hg) or a diastolic blood pressure less than 60 mm Hg. Blood pressure is the force exerted by the blood against the walls of the blood vessels as the heart pumps blood.

Hypotension can cause symptoms such as dizziness, lightheadedness, weakness, and fainting, especially when standing up suddenly. In severe cases, hypotension can lead to shock, which is a life-threatening condition characterized by multiple organ failure due to inadequate blood flow.

Hypotension can be caused by various factors, including certain medications, medical conditions such as heart disease, endocrine disorders, and dehydration. It is important to seek medical attention if you experience symptoms of hypotension, as it can indicate an underlying health issue that requires treatment.

Trypsin Inhibitor, Kazal Pancreatic is a type of protein that is produced in the pancreas and functions as an inhibitor to trypsin, which is a proteolytic enzyme involved in digestion. Specifically, this inhibitor belongs to the Kazal-type serine protease inhibitors. It helps regulate the activity of trypsin within the pancreas, preventing premature activation and potential damage to pancreatic tissue. Any imbalance or deficiency in this inhibitor can lead to pancreatic diseases such as pancreatitis.

'Clostridium botulinum type B' is a gram-positive, spore-forming anaerobic bacterium that produces botulinum neurotoxin type B. This toxin is one of the seven types of botulinum neurotoxins (A-G) produced by various strains of Clostridium botulinum and related species. Botulinum neurotoxin type B is responsible for causing botulism, a rare but serious illness that affects the nervous system and can cause paralysis and even be fatal. The bacterium is commonly found in soil and water and can produce spores that are resistant to heat, which allows them to survive in adverse conditions. Botulinum neurotoxin type B is also used in medical treatments for various neurological disorders, such as cervical dystonia, blepharospasm, and chronic migraine, under the brand name Myobloc or NeuroBloc.

Nordic became distributor of aprotinin in 2012. Aprotinin is a monomeric (single-chain) globular polypeptide derived from ... aprotinin may increase the risk of death. On October 29, 2006 the Food and Drug Administration issued a warning that aprotinin ... 30,000 of whom received aprotinin and the rest other anti-fibrinolytics. The study concluded aprotinin carried greater risks. ... Small amounts of aprotinin can be added to tubes of drawn blood to enable laboratory measurement of certain rapidly degraded ...
"Aprotinin". European Medicines Agency. 17 September 2018. Retrieved 19 January 2023. Antifibrinolytics at the U.S. National ... It is widely agreed that systemic aprotinin use should be minimized due to these concerns. "antifibrinolytic" at Dorland's ... aprotinin, is a naturally-occurring broad-spectrum protease inhibitor; some countries refuse to approve this medication because ...
... improve coronary endothelial function similarly to aprotinin. Unlike aprotinin, at high doses, their anti- ... CU-2010 and CU-2020 have the ability to inhibit plasmin to a similar extent as aprotinin, but they are 100,000 times better at ... CU-2010 and CU-2020 were developed to avoid many issues associated with the use of aprotinin, including the risk of an allergic ... Since the isolation of aprotinin is expensive, a drug with a simpler synthesis was desired. CU-2010 has a molecular weight of ...
Aprotinin and cardiac surgery: a sorry tale of evidence misused". Br J Anaesth. 110 (5): 675-8. doi:10.1093/bja/aet008. PMID ... Trasylol (Aprotinin) Trasylol is a trypsin inhibitor used to control bleeding during major surgery. In a 2006 meeting called by ... Trasylol (aprotinin), used to control bleeding during major surgery, was withdrawn from the market worldwide in 2007 when ... "FDA Revises Labeling for Trasylol (Aprotinin Injection) to Strengthen Safety Warnings and Limit Usage of Drug to Specific ...
"Efficacy of Aprotinin, Epsilon Aminocaproic Acid, or Combination in Cyanotic Heart Disease". Annals of Thoracic Surgery. ...
Paul Hebert discovered that aprotinin is associated with an increased risk of death compared to other drugs routinely used to ... "A comparison of aprotinin and lysine analogues in high-risk cardiac surgery". The New England Journal of Medicine. 358 (22): ...
Formulations from different manufacturers may also contain aprotinin, fibronectin, plasminogen, and factor XIII. Factors that ...
... eglin c and aprotinin". The Biochemical Journal. 313 (2): 555-60. doi:10.1042/bj3130555. PMC 1216943. PMID 8573092. Kikuchi T, ...
Prekallikrein Kinin-kallikrein system Kinin Aprotinin List of cutaneous conditions Raspi G (September 1996). "Kallikrein and ...
In 2004, LSBC announced an agreement with Sigma-Aldritch under which LSB would produce recombinant aprotinin in plants of the ... ProdiGene - was developing several proteins, including aprotinin, trypsin and a veterinary TGE vaccine in corn. Was in process ... Biomanufacturing Press Release Sigma catalog Aprotinin History of bankrupt biotech companies Cordis entry on Novoplant APHIS ... aprotinin, interferon Alpha 2a and 2b, G-CSF, and Hepatitis B vaccine antigens in tobacco. ...
Various serine protease inhibitors (aprotinin, phenylmethyl sulfonyl fluoride, leupeptin, and 4-(2-aminoethyl)-benzenesulfonyl ...
Fergusson, Dean; Glass, Kathleen Cranley; Hutton, Brian; Shapiro, Stan (2016). "Randomized controlled trials of aprotinin in ...
Pandey, R; Deshpande, SB (August 2004). "Protective effects of aprotinin on respiratory and cardiac abnormalities induced by ...
June 2010). "Production of pharmaceutical-grade recombinant aprotinin and a monoclonal antibody product using plant-based ...
APTEM test is an EXTEM based assay in which fibrinolysis is inhibited by aprotinin in the reagent. A significant improvement of ...
0.5 cc of distilled water is then added to the thrombin vial, and the aprotinin is mixed with fibrinogen. Each component is ... aprotinin solution (1,500 KIU in 0.5 ml), one ampoule of sterile water, four 21-gauge needles, two 20-gauge blunt application ...
... fibrinolysis is assessed by comparing the TEM profile in the absence or presence of the fibrinolysis inhibitor aprotinin. ...
Before its withdrawal, aprotinin was used in some forms of major surgery to decrease bleeding risk and the need for blood ...
1-78 Repeatable measurement of local and zonal GFR in the rat kidney with aprotinin (sm.m. O. Tenstad og H. E. Williamson), i ...
... aprotinin, captopril, imidazole or lidocaine.[citation needed] Myocardial+Depressant+Factor at the U.S. National Library of ...
Examples of Kunitz-type protease inhibitors are aprotinin (bovine pancreatic trypsin inhibitor, BPTI), Alzheimer's amyloid ...
Clotting time measurements can be affected by drugs such as warfarin, aprotinin, and GpIIb/IIIa inhibitors, and physiologic ...
... salivary proteins and aprotinin type protease inhibitors". The EMBO Journal. 9 (2): 385-93. doi:10.1002/j.1460-2075.1990. ...
... aprotinin, polysulphated glycosaminoglycan, skin derived fibroblasts etc.) for treating Achilles tendinopathy. As of 2014 there ...
B02AA01 Aminocaproic acid B02AA02 Tranexamic acid B02AA03 Aminomethylbenzoic acid B02AB01 Aprotinin B02AB02 Alfa1 antitrypsin ...
... has been shown to interact with: A2-Macroglobulin, β-amyloid precursor protein, APBB1, APOE, Aprotinin, C1S/C1q inhibitor ...
... aprotinin (INN) aptazapine (INN) aptiganel (INN) aptocaine (INN) (Articles with short description, Short description is ...
Aprotinin Bestatin Calpain inhibitor I and II Chymostatin E-64 Leupeptin (N-acetyl-L-leucyl-L-leucyl-L-argininal) alpha-2- ...
... such as aprotinin SDS is ionic denaturing detergent. Hot SDS buffer is often used when the proteins need to be completely ...
The Importance of Aprotinin and Pentoxifylline in Preventing the Leucocyte Sequestration and Lung İnjury Caused By Protamine at ...
Nordic became distributor of aprotinin in 2012. Aprotinin is a monomeric (single-chain) globular polypeptide derived from ... aprotinin may increase the risk of death. On October 29, 2006 the Food and Drug Administration issued a warning that aprotinin ... 30,000 of whom received aprotinin and the rest other anti-fibrinolytics. The study concluded aprotinin carried greater risks. ... Small amounts of aprotinin can be added to tubes of drawn blood to enable laboratory measurement of certain rapidly degraded ...
Fass environmental information for Artiss (among others aprotinin, bovint, syntetiskt) from Baxter (downloaded 2019-07-10).. ...
... ,Life Sciences Research Products,Native Protein,Peptide&Enzyme ... Bovine Aprotinin General description. Aprotinin is a monomeric globular polypeptide derived from bovine lung tissue. It ... Binding is reversible with most aprotinin-protease complexes dissociating at pH >10 or < 3.. CAS NO.: 9087-70-1. Source:Bovine ... Aprotinin inhibits several serine proteases, specifically trypsin, chymotrypsin, plasmin and kallikrein. Its action on ...
These include aprotinin, epsilon amino caproic acid (epsilon-ACA), and tranexamic acid. [24] Recently, aprotinin has incited ... Aprotinin. Aprotinin is a serine protease inhibitor that prevents the lysis of fibrinogen by inhibiting plasmin, kallikrein, ... However, other studies have not reported a benefit with aprotinin use. Therefore, the precise role of aprotinin remains ... A comparison of aprotinin and lysine analogues in high-risk cardiac surgery. N Engl J Med. 2008 May 29. 358(22):2319-31. [QxMD ...
Pig Aprotinin (AP) ELISA Kit, Cat#EKN43651. Rating Required Select Rating. 1 star (worst). 2 stars. 3 stars (average). 4 stars ... Pig Aprotinin (AP) ELISA Kit for detecting AP in serum, plasma, tissue homogenates, cell lysates, cell culture supernates, ... Pig Aprotinin (AP) ELISA Kit for detecting AP in serum, plasma, tissue homogenates, cell lysates, cell culture supernates, ...
TF, CaCl2, polybrene, aprotinin. Extrinsic and common pathway activation and fibrinolysis inhibition. Hyperfibrinolytic ... aprotinin-test; RVV-test: Russel viper venom test; ECA test: ecarin (saw-scaled viper venom) test [52]. ... aprotinin-test; RVV-test: Russel viper venom test; ECA test: ecarin (saw-scaled viper venom) test [52]. ...
Effects of zinc and aprotinin on the healing of ulnar diaphyseal fractures in rabbits. Celal İzci1, İlhami Çelik2, Muharrem ...
A comparison of aprotinin and lysine analogues in high-risk cardiac surgery. N Engl J Med. 2008 May 29. 358(22):2319-31. [QxMD ... Aprotinin is now only available via a limited-access protocol. Fergusson, et al. reported an increased risk for death compared ... Aprotinin has been documented to decrease blood loss in certain cardiac, orthopedic, and transplant surgeries by inhibiting ... Pharmacologic antifibrinolytics, such as aprotinin, epsilon aminocaproic acid (EACA), and TXA can reduce perioperative blood ...
Alternative perioperative anticoagulation monitoring during cardiopulmonary bypass in aprotinin-treated patients. J ...
Coagulation agents (eg, heparin and aprotinin) * Sugammadex * Induction drugs (eg, opioids, barbiturates, benzodiazepines, and ...
Aktuelle API Auditberichte • GMP-Audits der Herstelung pharmazeutischer Ausgangs- und Wirkstoffe nach ICH Q7 / EU GMP Guide Part II • Diapharm
little ebook dietro limmagine conversazioni sullarte, key aprotinin Ian McIntosh bargained the fans were commonly received by ... the review may add out after 30 slopes of aprotinin. making within the food will rupture your website financial. Educational ...
0.8 μm aprotinin, 0.02 μm leupeptin, 0.04 μm bestain, 0.015 μm pepstatin A, 0.015 μm E-64; Sigma]. After the insoluble material ...
2 mg/mL aprotinin (cat: A1153), 1 mg/mL pepstatin A (cat: 77170), and 2 mg/mL leupeptin (cat: L8511) at a 1:3 dilution, ...
... and aprotinin, all from Sigma-Aldrich). After gentle homogenization, the total amount of protein was quantified using the ...
Drugs that May Enhance the Neuromuscular Blocking Action of Succinylcholine: promazine, oxytocin, aprotinin, certain non- ... Drugs that may enhance the neuromuscular blocking action of succinylcholine include: promazine, oxytocin, aprotinin, certain ...
... aprotinin [1 μg/mL], leupeptin [1 μg/mL], 1mM phenylmethylsulfonyl fluoride, 0.1mM Na3VO4, and 10mM NaF) as described elsewhere ...
Aprotinin. Aprotinin (Trasylol; Bayer Pharmaceutical, West Haven, Connecticut) is an antifibrinolytic serine protease inhibitor ... A comparison of aprotinin and lysine analogues in high-risk cardiac surgery. N Engl J Med. 2008 May 29. 358(22):2319-31. [QxMD ... Aprotinin was approved by the US Food and Drug Administration (FDA) to reduce perioperative blood loss in high-risk patients ... Effect of aprotinin on clinical outcomes in coronary artery bypass graft surgery: a systematic review and meta-analysis of ...
... aprotinin, tranexamic acid), hydroxyurea, ketoconazole, mini-pill (progesterone birth control pills that do not contain ...
2 μg/mL aprotinin, and 0.5 mmol/L phenylmethylsulfonyl fluoride] and incubated on ice for 10 minutes; 10% NP40 (12.5 μL) was ... 2 μg/mL aprotinin, 5 μg/mL benzamidine, 0.5 mmol/L phenylmethylsulfonyl fluoride, and 1% NP40. The lysed cells were centrifuged ... 2 μg/mL aprotinin, and 0.5 mmol/L phenylmethylsulfonyl fluoride], mixed thoroughly, and incubated on ice for 30 minutes. The ...
... and aprotinin (105 U/liter). The slurry was passed twice through a French press at about 2,500 MPa at 0 to 4°C and then ...
... and 10 µg/ml aprotinin. The homogenates were then passed through a 22-gauge needle 30 times and subjected to centrifugation at ...
... aprotinin injection), a Bayer drug used in coronary artery bypass graft (CABG) surgery. ...
... and aprotinin (450 kallikrein-inhibiting units/ml blood), (Bayer, Leverkusen, Germany). The analysis of glucagon concentration ...
Aprotinin/9087-70-1/GT Peptide/Fornitur tal-Peptide. * Ormon tal-paratirojde (1-34) Bovini/12583-68-5/GT.... ...
PMSF and aprotinin) for 30 minutes on ice. Lysate was centrifuged at 12,000 × gfor 5 min at 4°C. Protein concentration was ...
20 μg/mL aprotinin and 10 μg/mL leupeptin). Equal amounts of total protein were separated by SDS-PAGE, transferred to PVDF ...
4 μg/ml aprotinin, 1 μg/ml leupeptin and 1 μg/ml pepstatin. Lysates were centrifuged for 8 minutes at 13,000 g. Supernatants ... 4 μg/ml aprotinin, 1 μg/ml leupeptin and 1 μg/ml pepstatin. Immunoprecipitations were carried out using 1 μg of rabbit anti- ...
  • The drug aprotinin (Trasylol, previously Bayer and now Nordic Group pharmaceuticals), is a small protein bovine pancreatic trypsin inhibitor (BPTI), or basic trypsin inhibitor of bovine pancreas, which is an antifibrinolytic molecule that inhibits trypsin and related proteolytic enzymes. (wikipedia.org)
  • Under the trade name Trasylol, aprotinin was used as a medication administered by injection to reduce bleeding during complex surgery, such as heart and liver surgery. (wikipedia.org)
  • Today, the Cardiovascular and Renal Drugs Advisory Committee and the Drug Safety and Risk Management Advisory Committee to the U.S. Food and Drug Administration (FDA) held a meeting to discuss the risk /benefit profile of Trasylol® (aprotinin injection), a Bayer drug used in coronary artery bypass graft (CABG) surgery. (worldpharmanews.com)
  • citation needed] Aprotinin is a competitive inhibitor of several serine proteases, specifically trypsin, chymotrypsin and plasmin at a concentration of about 125,000 IU/ml, and kallikrein at 300,000 IU/ml. (wikipedia.org)
  • Aprotinin is a monomeric (single-chain) globular polypeptide derived from bovine lung tissue. (wikipedia.org)
  • In September 2006, Bayer A.G. was faulted by the FDA for not revealing during testimony the existence of a commissioned retrospective study of 67,000 patients, 30,000 of whom received aprotinin and the rest other anti-fibrinolytics. (wikipedia.org)
  • Anaphylaxis (a severe allergic reaction) occurs at a rate of 1:200 in first-time use, but serology (measuring antibodies against aprotinin in the blood) is not carried out in practice to predict anaphylaxis risk because the correct interpretation of these tests is difficult. (wikipedia.org)
  • In the Canadian Blood Conservation Using Antifibrinolytics: A Randomized Trial in a Cardiac Surgery Population (BART), which included patients undergoing various types of surgery who were at increased risk for bleeding complications, the apparent aprotinin risk hadn't reached statistical significance but was judged unlikely to improve. (medscape.com)
  • BART had been designed to determine whether aprotinin would be better than either epsilon-aminocaproic acid or tranexamic acid in preventing "massive bleeding" associated with cardiac surgery, the announcement said. (medscape.com)
  • Their search for studies of aprotinin, lysine analogs (such as aminocaproic acid and tranexamic acid) and desmopressin in adult cardiac surgery identified 128 randomized controlled clinical trials. (aafp.org)
  • The risk associated with aprotinin in cardiac surgery. (nih.gov)
  • Studies have variably linked aprotinin administration with both improved as well as adverse cerebral consequences after cardiac surgery. (duke.edu)
  • Aprotinin is a broad spectrum protease inhibitor which modulates the systemic inflammatory response (SIR) associated with cardiopulmonary bypass (CPB) surgery. (nih.gov)
  • Aprotinin, a nonspecific serine protease inhibitor, has been used to decrease bleeding and reduce the systemic inflammatory response after cardiopulmonary bypass (CPB). (duke.edu)
  • Aprotinin is currently approved for preventing perioperative blood loss and cutting the need for transfusions during pump-supported CABG surgery in high-risk patients, according to the agency. (medscape.com)
  • The risk of perioperative myocardial infarction was not increased by use of aprotinin and lysine analogs but was significantly increased in patients receiving desmopressin. (aafp.org)
  • Although the data are based on different dosages of the study drugs and involve patients undergoing surgeries of varying complexity, the authors conclude that aprotinin and lysine analogs decrease perioperative blood loss, mortality and the need for rethoracotomy and blood transfusion. (aafp.org)
  • The physiological renal handling of aprotinin is similar to that of other small proteins, e.g., insulin. (nih.gov)
  • Aprotinin, through its inhibition of multiple mediators [e.g., kallikrein, plasmin] results in the attenuation of inflammatory responses, fibrinolysis, and thrombin generation. (nih.gov)
  • Aprotinin is used in chromogenic assays for the determination of antithrombin III, heparin, α2-macroglobulin, FXa and thrombin to inhibit disturbing kallikrein or plasmin activities. (cryopep.com)
  • The studies comparing the pharmacokinetics of aprotinin in healthy volunteers, cardiac patients undergoing surgery with cardiopulmonary bypass, and women undergoing hysterectomy suggest linear pharmacokinetics over the dose range of 50,000 KIU to 2 million KIU. (nih.gov)
  • Aprotinin improves functional outcome but not cerebral infarct size in an experimental model of stroke during cardiopulmonary bypass. (duke.edu)
  • The effects of aprotinin use in CPB involves a reduction in inflammatory response which translates into a decreased need for allogeneic blood transfusions, reduced bleeding, and decreased mediastinal re-exploration for bleeding. (nih.gov)
  • In this experimental model of stroke occurring during CPB, aprotinin decreased the systemic inflammatory response to CPB. (duke.edu)
  • For now, it said, healthcare providers should be mindful of accumulating data suggesting aprotinin can increase mortality compared with the other antifibrinolytics. (medscape.com)
  • Cite this: Aprotinin-related mortality risk puts brakes on randomized surgery trial - Medscape - Oct 25, 2007. (medscape.com)
  • The trials using aprotinin and lysine analogs showed a significant decrease in mortality. (aafp.org)
  • There was a reduction in systemic inflammation in the aprotinin group compared with the control group, demonstrated by lower levels of IL-1beta (P = 0.035) and IL-6 (P = 0.047). (duke.edu)
  • The bleeding tendency according to high PT and aPTT levels were continued with application of aprotinin while reduction of bleeding was seen. (beun.edu.tr)
  • The announcement closely follows the publication of a massive meta-analysis of randomized trials suggesting that aprotinin does not raise the risk of operative thrombosis or death [ 2 ] and comes on the heels of recommendations from two FDA advisory committees to keep the drug on the market. (medscape.com)
  • After intravenous (IV) injection, rapid distribution of aprotinin occurs into the total extracellular space, leading to a rapid initial decrease in plasma aprotinin concentration. (nih.gov)
  • Aprotinin (molecular weight of 6512 daltons), consists of 58 amino acid residues that are arranged in a single polypeptide chain, cross-linked by three disulfide bridges. (nih.gov)
  • Venous blood samples were collected mined by commercially available radio- using plain tubes for routine tests and chilled immunoassay kits for met-enkephalin, polyethylene tubes containing aprotinin -endorphin and leu-enkephalin (Penin- and/or ethylenediaminetetra-acetic acid sula Laboratories Inc, Division of Bachem, (EDTA). (who.int)
  • In this study, comparison among three agents (Aprotinin, Tranaexaemic Acid & Epsilon Amino Caproic Acid) is done to reduce the peri-operative blood loss in open-heart surgery. (bvsalud.org)
  • Aprotinin, Tranaexaemic acid & EACA respectively. (bvsalud.org)
  • Following a single IV dose of radiolabelled aprotinin, approximately 25-40% of the radioactivity is excreted in the urine over 48 hours. (nih.gov)
  • After a larger dose of 2 million KIU infused over 30 minutes, urinary excretion of unchanged aprotinin accounts for approximately 9% of the dose. (nih.gov)
  • We designed this study to determine whether an antiinflammatory dose of aprotinin could improve the histologic and functional neurologic outcome in a rat model of focal cerebral ischemia during CPB. (duke.edu)
  • Overall, treatment with aprotinin and lysine analogs decreased the rate of surgical re-exploration, but the chance of rethoracotomy varied with the dosage of the drug used and the degree of complexity of the surgery. (aafp.org)
  • After surgical preparation, the animals were randomized into 2 groups: an aprotinin group (60,000 kIU/kg IV) and a control group (0.9% NaCl IV). (duke.edu)
  • Background: The aim of the present study was to test the effectiveness of aprotinin to reduce bleeding in liver resection of guinea pigs with acutely injured hepatocyte using intraperitoneal D(+)Galactosamine. (beun.edu.tr)
  • Animal studies have shown that aprotinin is accumulated primarily in the kidney. (nih.gov)
  • The risk for a fatal reaction appears to be greater upon re-exposure within 12 months of the most recent prior aprotinin exposure. (nih.gov)
  • Aprotinin and lysine analogs reduced the proportion of patients receiving blood transfusion by about 20 percent. (aafp.org)
  • Although there was no difference in the cerebral infarct volume, there was a small improvement in the short-term functional neurologic outcome in the aprotinin group. (duke.edu)
  • Group 4 received 10.000 KIU/kg aprotinin infusion via jugular catheter in 10 min prior to standard liver resection in pretreated animals with D(+)galactosamine. (beun.edu.tr)