query: what is the name of the clotting protein found in plasma

pos: Blood proteins steroid hormones. Globulins make up 38% of blood proteins and transport ions, hormones, and lipids assisting in immune function. Fibrinogen comprises 7% of blood proteins; conversion of fibrinogen to insoluble fibrin is essential for blood clotting. The remainder of the plasma proteins (1%) are regulatory proteins, such as enzymes, proenzymes, and hormones. All blood proteins are synthesized in liver except for the gamma globulins. Separating serum proteins by electrophoresis is a valuable diagnostic tool as well as a way to monitor clinical progress. Current research regarding blood plasma proteins is centered on performing proteomics analyses of serum/plasma in the search

pos: Thrombin time Thrombin time The thrombin time (TT), also known as the thrombin clotting time (TCT) is a blood test that measures the time it takes for a clot to form in the plasma of a blood sample containing anticoagulant, after an excess of thrombin has been added. It is used to diagnose blood coagulation disorders and to assess the effectiveness of fibrinolytic therapy. This test is repeated with pooled plasma from normal patients. The difference in time between the test and the 'normal' indicates an abnormality in the conversion of fibrinogen (a soluble protein) to fibrin, an insoluble protein. The thrombin

pos: Purpura fulminans raised, sometimes with vesicle or blister (bulla) formation. The distribution of purpura fulminans lesions may be different according to the underlying pathogenesis. Purpura fulminans in severe sepsis typically develops in the distal extremities and progresses proximally or appears as a generalised or diffuse rash affecting the whole body surface. In cases of severe inheritable protein C deficiency, purpura fulminans with disseminated intravascular coagulation manifests within a few hours or days after birth. The cardinal features of purpura investigations are the same as those of disseminated intravascular coagulation: prolonged plasma clotting times, thrombocytopenia, reduced plasma fibrinogen concentration, increased plasma fibrin-degradation products

pos: Fibrinogen sequence but is incorrectly glycosylated (i.e. has a wrong amount of sugar residues) added to it during its passage through the Golgi. The incorrectly glycosalated fibrinogen is dysfunctional and may cause pathological episodes of bleeding and/or blood clotting. Other, less well understood, causes are plasma cell dyscrasias and autoimmune disorders in which a circulating abnormal immunoglobulin or other protein interferes with fibrinogen function, and rare cases of cancer and medication (isotretinoin, glucocorticoids, and antileukemic drugs) toxicities. Congenital hypodysfibrinogenemia is a rare inherited disorder in which low levels (i.e. <150 mg/d) of immunologically detected plasma fibrinogen are and composed at least

pos: Blood transfusion developing countries the donor is sometimes specifically recruited by or for the recipient, typically a family member, and the donation occurs immediately before the transfusion. Donated blood is usually subjected to processing after it is collected, to make it suitable for use in specific patient populations. Collected blood is then separated into blood components by centrifugation: red blood cells, plasma, platelets, albumin protein, clotting factor concentrates, cryoprecipitate, fibrinogen concentrate, and immunoglobulins (antibodies). Red cells, plasma and platelets can also be donated individually via a more complex process called apheresis. Before a recipient receives a transfusion, compatibility testing between donor and

pos: Coagulase is called "staphylothrombin", which enables the enzyme protease to convert fibrinogen, a plasma protein produced by the liver, to fibrin. This results in clotting of the blood. Coagulase is tightly bound to the surface of the bacterium "S. aureus" and can coat its surface with fibrin upon contact with blood. The fibrin clot may protect the bacterium from phagocytosis and isolate it from other defenses of the host. The fibrin coat can therefore make the bacteria more virulent. Bound coagulase is part of the larger family of MSCRAMM. The coagulase test has traditionally been used to differentiate "Staphylococcus aureus" from

pos: Hypercoagulability in pregnancy Hypercoagulability in pregnancy Hypercoagulability in pregnancy is the propensity of pregnant women to develop thrombosis (blood clots). Pregnancy itself is a factor of hypercoagulability (pregnancy-induced hypercoagulability), as a physiologically adaptive mechanism to prevent "post partum" bleeding. However, when combined with an additional underlying hypercoagulable states, the risk of thrombosis or embolism may become substantial. Pregnancy-induced hypercoagulability is probably a physiologically adaptive mechanism to prevent "post partum" hemorrhage. Pregnancy changes the plasma levels of many clotting factors, such as fibrinogen, which can rise up to three times its normal value. Thrombin levels increase. Protein S, an anticoagulant, decreases. However, the other

pos: Blood plasma fractionation Blood plasma fractionation Blood plasma fractionation refers to the general processes of separating the various components of blood plasma, which in turn is a component of blood obtained through blood fractionation. Blood plasma is the liquid component of whole blood, and makes up approximately 55% of the total blood volume. It is composed primarily of water with small amounts of minerals, salts, ions, nutrients, and proteins in solution. In whole blood, red blood cells, leukocytes, and platelets are suspended within the plasma. Plasma contains a large variety of proteins including albumin, immunoglobulins, and clotting proteins such as fibrinogen. Albumin constitutes

pos: Blood plasma Blood plasma Blood plasma is a yellowish coloured liquid component of blood that normally holds the blood cells in whole blood in suspension; this makes plasma the extracellular matrix of blood cells. It makes up about 55% of the body's total blood volume. It is the intravascular fluid part of extracellular fluid (all body fluid outside cells). It is mostly water (up to 95% by volume), and contains dissolved proteins (6–8%) (i.e.—serum albumins, globulins, and fibrinogen), glucose, clotting factors, electrolytes (Na, Ca, Mg, HCO, Cl, etc.), hormones, carbon dioxide (plasma being the main medium for excretory product transportation) and oxygen.

pos: Serum protein electrophoresis in hypercholesterolemia. Decreased beta-1 protein occurs in acute or chronic inflammation. Beta-2 comprises C3 (Complement protein 3). It is raised in the acute phase response. Depression of C3 occurs in autoimmune disorders as the complement system is activated and the C3 becomes bound to immune complexes and removed from serum. Fibrinogen, a beta-2 protein, is found in normal plasma but absent in normal serum. Occasionally, blood drawn from heparinized patients does not fully clot, resulting in a visible fibrinogen band between the beta and gamma globulins. C-reactive protein is found in between the beta and gamma zones producing beta/gamma fusion.

neg: Thromboplastin Thromboplastin Thromboplastin or thrombokinase (TPL) is a plasma protein aiding blood coagulation through catalyzing the conversion of prothrombin to thrombin. It is a complex enzyme that is found in brain, lung, and other tissues and especially in blood platelets and that functions in the conversion of prothrombin to thrombin in the clotting of blood—called also thrombokinase. Although sometimes used as a synonym for the protein tissue factor (with its official name "Coagulation factor III [thromboplastin, tissue factor]"), this is a misconception. Historically, thromboplastin was a lab reagent, usually derived from placental sources, used to assay prothrombin times (PT). Thromboplastin, by

neg: Purpura fulminans to complications of fluid overload and death, especially in neonates, such as transfusion-related acute lung injury. Exposure to multiple plasma donors over time increases the cumulative risk for transfusion-associated viral infection and allergic reaction to donor proteins found in fresh frozen plasma. Allergic reactions and alloantibody formation are also potential complications, as with any protein replacement therapy. Concomitant warfarin therapy in subjects with congenital protein C deficiency is associated with an increased risk of warfarin skin necrosis. Early stage sepsis-associated purpura fulminans may be reversible with quick therapeutic intervention. Treatment is mainly removing the underlying cause and degree of clotting

neg: Innate immune system and invertebrates, even though different proteins are used throughout the cascades. In the hemolymph, which makes up the fluid in the circulatory system of arthropods, a gel-like fluid surrounds pathogen invaders, similar to the way blood does in other animals. There are various different proteins and mechanisms that are involved in invertebrate clotting. In crustaceans, transglutaminase from blood cells and mobile plasma proteins make up the clotting system, where the transglutaminase polymerizes 210 kDa subunits of a plasma-clotting protein. On the other hand, in the horseshoe crab species clotting system, components of proteolytic cascades are stored as inactive forms in

neg: Blood donation in England and each donation usually gives two or three adult doses. One adult dose of platelets would otherwise require four whole blood donations. Blood is made in the bone marrow. It is composed of red blood cells, platelets, plasma and white blood cells, collectively referred to as blood components. Donations given at regular blood donation sessions are referred to as "Whole Blood". Platelets are very small cells. They work with the clotting factors in plasma to form a mesh "plug" to stop or prevent bleeding. Plasma is the fluid part of the blood. It contains protein, salts and clotting factors. White

neg: Warfarin necrosis of warfarin, and heparin or its low molecular weight heparin (LMWH) can be used in an attempt to prevent further clotting. None of these suggested therapies have been studied in clinical trials. Heparin and LMWH act by a different mechanism than warfarin, so these drugs can also be used to prevent clotting during the first few days of warfarin therapy and thus prevent warfarin necrosis (this is called 'bridging'). Based on the assumption that low levels of protein C are involved in the underlying mechanism, common treatments in this setting include fresh frozen plasma or pure activated protein C. Since

neg: Blood plasma Plasma also serves as the protein reserve of the human body. It plays a vital role in an intravascular osmotic effect that keeps electrolyte concentration balanced and protects the body from infection and other blood disorders. Blood plasma is separated from the blood by spinning a tube of fresh blood containing an anticoagulant in a centrifuge until the blood cells fall to the bottom of the tube. The blood plasma is then poured or drawn off. Blood plasma has a density of approximately 1025 kg/m, or 1.025 g/ml. Blood serum is blood plasma without clotting factors. Plasmapheresis is a medical

neg: Coagulin 16 half-cystines found in the molecule appear to yield a compact protein stable to acid and heat. Mammalian blood coagulation is based on the proteolytically induced polymerization of fibrinogens. Initially, fibrin monomers noncovalently interact with each other. The resulting homopolymers are further stabilized when the plasma transglutaminase cross-links epsilon-(gamma-glutamyl)lysine bonds between molecules. In crustaceans, hemolymph coagulation depends on the transglutaminase-mediated cross-linking of specific plasma-clotting proteins, but without the proteolytic cascade. In horseshoe crabs, the proteolytic coagulation cascade triggered by lipopolysaccharides and beta-1,3-glucans leads to the conversion of coagulogen into coagulin, resulting in noncovalent coagulin homopolymers through head-to-tail interaction. However, horseshoe

neg: Lupus anticoagulant normal pooled plasma and the clotting is re-assessed. If a clotting inhibitor such as a lupus anticoagulant is present, the inhibitor will interact with the normal pooled plasma and the clotting time will remain abnormal. However, if the clotting time of the mixed plasma corrects towards normal, the presence of an inhibitor such as the lupus anticoagulant is excluded, and instead a deficient quantity of clotting factor (that is replenished by the normal plasma) is likely. If the mixing test indicates an inhibitor, diagnosis of a lupus anticoagulant is then confirmed with prolonged phospholipid-sensitive functional clotting testing, such as the

neg: Clearance (pharmacology) of these equations can be found in e.g Rang and Dale's Pharmacology For substances that exhibit substantial plasma protein binding, clearance is generally dependent on the total concentration (free + protein-bound) and not the free concentration. Most plasma substances have primarily their free concentrations regulated, which thus remains the same, so extensive protein binding increases total plasma concentration (free + protein-bound). This decreases clearance compared to what would have been the case if the substance did not bind to protein. However, the mass removal rate is the same, because it depends only on concentration of free substance, and is independent

neg: Draculin Draculin Draculin (named after Count Dracula) is a glycoprotein found in the saliva of vampire bats. It is composed of 411 amino acids, weighing about 88.5kDa. It functions as an anticoagulant, inhibiting coagulation factors IX (IXa) and X (Xa), thus keeping the blood of the bitten victim from clotting while the bat is drinking. Draculin is a reversible, slow tight binding, noncompetitive inhibitor of FXa. It does not act on thrombin, trypsin or chymotrypsin and does not express fibrinolytic activity. The protein increases the lag phase as well as the height of the peak of thrombin generation when in plasma,

neg: Clinical chemistry the denser blood cells and platelets to the bottom of the centrifuge tube, leaving the liquid serum fraction resting above the packed cells. This initial step before analysis has recently been included in instruments that operate on the "integrated system" principle. Plasma is in essence the same as serum, but is obtained by centrifuging the blood "without" clotting. Plasma is obtained by centrifugation "before" clotting occurs. The type of test required dictates what type of sample is used. A large medical laboratory will accept samples for up to about 700 different kinds of tests. Even the largest of laboratories rarely

neg: Carboxylation to γ-carboxyglutamate, in proteins. It occurs primarily in proteins involved in the blood clotting cascade, specifically factors II, VII, IX, and X, protein C, and protein S, and also in some bone proteins. This modification is required for these proteins to function. Carboxylation occurs in the liver and is performed by γ-glutamyl carboxylase. The carboxylase requires vitamin K as a cofactor and performs the reaction in a processive manner. γ-carboxyglutamate binds calcium, which is essential for its activity. For example, in prothrombin, calcium binding allows the protein to associate with the plasma membrane in platelets, bringing it into close proximity

neg: Kinin–kallikrein system inflammatory mediators that cause dilation of blood vessels and increased vascular permeability. Kinins are small peptides produced from kininogen by kallikrein and are broken down by kininases. They act on phospholipase and increase arachidonic acid release and thus prostaglandin (PGE2) production. C1-inhibitor is a serine protease inhibitor (serpin) protein. C1-INH is the most important physiological inhibitor of plasma kallikrein, fXIa and fXIIa. C1-INH also inhibits proteinases of the fibrinolytic, clotting, and kinin pathways. Deficiency of C1-INH permits plasma kallikrein activation, which leads to the production of the vasoactive peptide bradykinin. Kinin–kallikrein system The kinin–kallikrein system or simply kinin system is

neg: SNED1 extracellular "sticky" protein possibly involved in cell-cell adhesion or in clotting. Protein matches found in Phyre2 comprise an array of proteins with functions of; clotting, hydrolysis, plasminogen activation, hormone/growth factor, protein binding, cell-adhesion, and ECM proteins. Splice variants a, b, and e, in Figures 5 and 6 have >99% structural similarity to the protein neurexin 1-alpha(NRXN1). Neurexins are cell adhesion molecules and often contain EGF binding domains, enhancing intracellular junction forming between cells. NRXN1 is also proposed to play a role in angiogenesis. Alpha-neurexins interact with neurexophilins and possibly function in the synaptic junctions of the vertebrate nervous system. Alpha

neg: Turoctocog alfa whereby expected plasma factor VIII activity levels may not be achieved and thus the bleeding would not be controlled as needed. As cell culture, Chinese hamster ovary cells (CHO) are used in order to acquire proper processing of factor VIII protein, that has demonstrated good efficacy in thrombin generation and clot formation in preclinical evaluations in murine (mouse) and canine (dog) models of hemophilia A and in patient-derived whole blood. Even though both treatments are plasma-derived and recombinant analogues of blood clotting factors, NovoSeven is developed as a congenital FVIIa analogue for hemophilia A and B patients while NovoEight (turoctocog

neg: Kringle domain Kringle domain Kringle Domains are autonomous protein domains that fold into large loops stabilized by 3 disulfide linkages. These are important in protein–protein interactions with blood coagulation factors. The name Kringle comes from the Scandinavian pastry that these structures resemble. Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein(a). Kringles are found throughout the blood clotting and fibrinolytic proteins. Kringle domains are believed to play a role in binding mediators (e.g., membranes, other proteins or phospholipids), and in the regulation of proteolytic activity. Kringle domains are characterised by a triple loop, 3-disulfide bridge structure, whose conformation

neg: Blood type shelf-life, blood banks fractionate some whole blood into several products. The most common of these products are packed RBCs, plasma, platelets, cryoprecipitate, and fresh frozen plasma (FFP). FFP is quick-frozen to retain the labile clotting factors V and VIII, which are usually administered to patients who have a potentially fatal clotting problem caused by a condition such as advanced liver disease, overdose of anticoagulant, or disseminated intravascular coagulation (DIC). Units of packed red cells are made by removing as much of the plasma as possible from whole blood units. Clotting factors synthesized by modern recombinant methods are now in routine

neg: P2Y12 P2Y12 In the field of purinergic signaling, the P2Y protein is found mainly but not exclusively on the surface of blood platelets, and is an important regulator in blood clotting. P2Y belongs to the Gi class of a group of G protein-coupled (GPCR) purinergic receptors and is a chemoreceptor for adenosine diphosphate (ADP). This P2Y receptor family has several receptor subtypes with different pharmacological selectivity, which overlaps in some cases, for various adenosine and uridine nucleotides. The P2Y12 receptor is involved in platelet aggregation and is thus a biological target for the treatment of thromboembolisms and other clotting disorders. Two

neg: Biofluid dynamics clotting. In addition to these 55 to 60 percent of blood by volume consists of plasma. Plasma is the transparent, amber-colored liquid in which the cellular components of blood are suspended. Plasma contains constituents such as proteins, electrolytes, hormones, and nutrients. The serum is blood plasma from which clotting factors have been removed.Blood accounts for 6 to 8 percent of body weight in normal, healthy humans. The density of blood is slightly greater than the density of water at approximately 1060 kg/m3. The increased density comes from the increased density of a red blood cell compared with the density of

neg: Kaolin clotting time of cell fragments and plasma lipids to provide the phospholipid surface required for coagulation. Therefore, the sample quality is important for the validity of the test. The test combines a test plasma with kaolin, and the time the clot (in seconds) is measured. If the KCT is less than 60 seconds, this suggests that the normal control plasma is contaminated with platelet fragments; therefore, the test is not valid. The KCT test/control ratio of greater than or equal to 1.2 indicates an inhibitor is present. If the test/control ratio is between 1.1 and 1.2, the test is equivocal. Kaolin clotting

neg: Dilute Russell's viper venom time the test sensitive to the presence of lupus anticoagulants, because these antibodies interfere with the clot-promoting role of phospholipid "in vitro", and their presence results in a prolonged clotting time. A mixing study is then performed, which consists of adding an equal volume of the patient's plasma to normal plasma; in this study, one would expect the clotting time to return to the normal range if there was only a deficiency of coagulation factors alone. A prolonged clotting time of 30 seconds or greater that does not correct despite the mixing study suggests the presence of a lupus anticoagulant. An

neg: Sulfatide in the peripheral nervous system. However, sulfatide is also present on the extracellular leaflet of the plasma membrane of many cells in eukaryotic organisms. Since sulfatide is a multifunctional molecule, it can be used in multiple biological areas. Aside from being a membrane component, sulfatide functions in protein trafficking, cell aggregation and adhesion, neural plasticity, memory, and glial-axon interactions. Sulfatide also plays a role in several physiological processes and systems, including the nervous system, the immune system, insulin secretion, blood clotting, viral infection, and bacterial infection. As a result, sulfatide is associated with, able to bind to, and/or is present

neg: Surfactant protein B surfactant proteins. It is smaller, only 35 amino acids long, and is found embedded in lipid structures much like SP-B. SP-A and SP-D, known together as colletins, are more distinct from SP-B than SP-C. They are hydrophilic, so they are found in the solution, and function in immune response instead of lipid arrangement and surface tension reduction. SP-A is actually a name for two very similar proteins, SP-A1 and SP-A2. Along with SP-A, B, C, and D, blood plasma proteins are found in very small quantities in surfactant as well. Surfactant protein B Surfactant protein B is an essential lipid-associated

neg: Extracellular fluid of the protein is altered. The normal shape, and therefore function of very many of the extracellular proteins, as well as the extracellular portions of the cell membrane proteins is dependent on a very precise ionized calcium concentration in the ECF. The proteins that are particularly sensitive to changes in the ECF ionized calcium concentration are several of the clotting factors in the blood plasma, which are functionless in the absence of calcium ions, but become fully functional on the addition of the correct concentration of calcium salts. The voltage gated sodium ion channels in the cell membranes of nerves

neg: Coagulation space initiates two processes: changes in platelets, and the exposure of subendothelial tissue factor to plasma Factor VII, which ultimately leads to fibrin formation. Platelets immediately form a plug at the site of injury; this is called "primary hemostasis". "Secondary hemostasis" occurs simultaneously: Additional coagulation factors or clotting factors beyond Factor VII (listed below) respond in a complex cascade to form fibrin strands, which strengthen the platelet plug. Coagulation is highly conserved throughout biology; in all mammals, coagulation involves both a cellular (platelet) and a protein (coagulation factor) component. The system in humans has been the most extensively researched and

neg: Protein C inhibitor Protein C inhibitor Protein C inhibitor (PCI, SERPINA5) is a serine protease inhibitor (serpin) which limits the activity of protein C (an anticoagulant). An N-terminal fragment of PCI is a possible serum biomarker for prostate cancer. Protein C inhibitor is activated by heparin against thrombin. Protein C inhibitor (PCI) is serine protease inhibitor of serpin type that is found in most tissues and fluids, including blood plasma, seminal plasma and urine of human. It is a 52kD glycoprotein and belongs to serine protease inhibitor ( Serpin) super family of protein. In the beginning protein C Inhibitor (PCI) was identified as

neg: ADAMTS13 ADAMTS13 ADAMTS13 (a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13)—also known as "von Willebrand factor-cleaving protease" (VWFCP)—is a zinc-containing metalloprotease enzyme that cleaves von Willebrand factor (vWf), a large protein involved in blood clotting. It is secreted in blood and degrades large vWf multimers, decreasing their activity. The "ADAMTS13" gene maps to the ninth chromosome (9q34). Since 1982 it had been known that thrombotic thrombocytopenic purpura (TTP), one of the microangiopathic hemolytic anemias (see below), was characterized in its familial form by the presence in plasma of unusually large von Willebrand factor multimers (ULVWF). In 1994,

neg: EGF-like domain the second cbEGF module and thereby aligns both modules. Thus, domain-domain interactions (partially facilitated by calcium coordination) are crucial for the catalytic activity of proteins involved in the blood-clotting cascade. Below is a list of human proteins containing the EGF-like domain: EGF-like domain The EGF-like domain is an evolutionary conserved protein domain, which derives its name from the epidermal growth factor where it was first described. It comprises about 30 to 40 amino-acid residues and has been found in a large number of mostly animal proteins. Most occurrences of the EGF-like domain are found in the extracellular domain of membrane-bound

neg: SNED1 to SNED1, with protein abundance found in blood plasma, platelets, and liver. All of the interacting proteins described are expressed in these three common areas. SNED1 is ubiquitously expressed at intermediate levels, making it unclear from RNA expression profiles, which cells are secreting SNED1. The protein expression profiles of SNED1 predicted with MOPED-Multi-Omics Profiling Expression Database and PaxB-Protein Abundance Across Organisms database indicate that the protein is found in blood serum, blood plasma, blood T-lymphocytes, platelets, kidney Hek-293 cells, liver, and low levels in the brain. The program Aceview was used to predict transcript variants, shown in Figure 6. There

neg: Hypoprothrombinemia Non-inheritance and other factors: There are two types of prothrombin deficiencies that occur depending on the mutation: Type I (true deficiency), includes a missense or nonsense mutation, essentially decreasing prothrombin production. This is associated with bleeding from birth. Here, plasma levels of prothrombin are typically less than 10% of normal levels. Type II, known as dysprothrombinemia, includes a missense mutation at specific Xa factor cleavage sites and serine protease prothrombin regions. Type II deficiency creates a dysfunctional protein with decreased activity and usually normal or low-normal antigen levels. A vitamin K-dependent clotting factor is seldom seen as a contributor to

neg: SNAP29 SNAP29 Synaptosomal-associated protein 29 is a protein that in humans is encoded by the "SNAP29" gene. This gene, a member of the SNAP25 gene family, encodes a protein involved in multiple membrane trafficking steps. Two other members of this gene family, SNAP23 and SNAP25, encode proteins that bind a syntaxin protein and mediate synaptic vesicle membrane docking and fusion to the plasma membrane. The protein encoded by this gene binds tightly to multiple syntaxins and is localized to intracellular membrane structures rather than to the plasma membrane. While the protein is mostly membrane-bound, a significant fraction of it is found

neg: EPB41L1 interact with: EPB41L1 Band 4.1-like protein 1 is a protein that in humans is encoded by the "EPB41L1" gene. Erythrocyte membrane protein band 4.1 (EPB41) is a multifunctional protein that mediates interactions between the erythrocyte cytoskeleton and the overlying plasma membrane. The protein encoded by this gene is a neuronally-enriched protein that is structurally similar to EPB41. The encoded protein binds and stabilizes D2 and D3 dopamine receptors at the neuronal plasma membrane. Multiple transcript variants encoding different isoforms have been found for this gene, but the full-length nature of only two of them has been determined. EPB41L1 has been

neg: EPB41L1 EPB41L1 Band 4.1-like protein 1 is a protein that in humans is encoded by the "EPB41L1" gene. Erythrocyte membrane protein band 4.1 (EPB41) is a multifunctional protein that mediates interactions between the erythrocyte cytoskeleton and the overlying plasma membrane. The protein encoded by this gene is a neuronally-enriched protein that is structurally similar to EPB41. The encoded protein binds and stabilizes D2 and D3 dopamine receptors at the neuronal plasma membrane. Multiple transcript variants encoding different isoforms have been found for this gene, but the full-length nature of only two of them has been determined. EPB41L1 has been shown to

neg: Plasma cell dyscrasia kinds of mutations that lead to the production of an IgM myeloma protein. Overproduction of this myeloma protein may progress to a different form of plasma cell/lymphoplasmacytoid cell malignancy, Waldenström macroglobulinaemia. Genetic mutations thought to be involved in the development and/or progression of the latter disease include the L265P mutation in the "MYD88" gene found in >90% of Waldenström macroglobulinaemia patients as well as various mutations in the "CXCR" gene found in 27% to 40% of Waldenström macroglobulinaemia patiens. The clonal plasma cells involved in plasma cell dyscrasias exhibit a high degree of genetic instability. For example, the clonal plasma

neg: FERM domain FERM domain In molecular biology, the FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain is located at the N terminus in the majority of proteins in which it is found. Ezrin, moesin, and radixin are highly related proteins (ERM protein family), but the other proteins in which the FERM domain is

neg: Protein C is present in normal adult human blood plasma at concentrations between 65–135 IU/dL. Activated protein C is found at levels approximately 2000 times lower than this. Mild protein C deficiency corresponds to plasma levels above 20 IU/dL, but below the normal range. Moderately severe deficiencies describe blood concentrations between 1 and 20 IU/dL; severe deficiencies yield levels of protein C that are below 1 IU/dL or are undetectable. Protein C levels in a healthy term infant average 40 IU/dL. The concentration of protein C increases until six months, when the mean level is 60 IU/dL; the level stays low through

neg: VP40 VP40 In molecular biology, VP40 is the name of a Viral matrix protein. Most commonly it is found in the "Ebola virus" (EBOV), a type of non-segmented, negative-strand RNA virus. Ebola virus causes a severe and often fatal haemorrhagic fever in humans, known as Ebola virus disease. The virus matrix protein VP40 is a major structural protein that plays a central role in virus assembly and budding at the plasma membrane of infected cells. VP40 proteins work by associating with cellular membranes, interacting with the cytoplasmic tails of glycoproteins and binding to the ribonucleoprotein complex. The VP40 monomer consists of

neg: Lupus anticoagulant and aggregation of platelets, which accounts for the in vivo prothrombotic characteristics. The condition was first described by hematologist C. Lockard Conley. Both words in the term "lupus anticoagulant" can be misleading: The presence of prolonged clotting times on a routine plasma test often triggers functional testing of the blood clotting function, as well as serological testing to identify common autoantibodies such as antiphospholipid antibodies. These antibodies tend to delay in-vitro coagulation in phospholipid-dependent laboratory tests such as the partial thromboplastin time. The initial workup of a prolonged PTT is a mixing test whereby the patient's plasma is mixed with

neg: Protein S deficiency cofactor of APC both work to degrade factor V and factor VIII. It has been suggested that Zn2+ might be necessary for Protein S binding to factor Xa. Mutations in this condition change amino acids, which in turn disrupts blood clotting. Functional protein S is lacking, which normally "turns off" clotting proteins, this increases risk of blood clots. The diagnosis for deficiency of protein S can be done via reviewing family history of condition and genetic testing, as well as the following: Among the possibilities for differential diagnosis of protein S deficiency are- Antiphospholipid syndrome, disseminated intravascular coagulation and antithrombin

neg: Cetirizine there is no accumulation of the drug with chronic administration. Following once-daily administration of 10 mg cetirizine for 10 days, the mean C was 311 ng/mL. The mean plasma protein binding of cetirizine has been found to be 93 to 96% across a range of 25 to 1,000 ng/mL independent of concentration. Plasma protein binding of 88 to 96% has also been reported across multiple studies. The drug is bound to albumin with high affinity, while α-acid glycoprotein and lipoproteins contribute much less to total plasma protein binding. The unbound or free fraction of levocetirizine has been reported to be

neg: VAPB VAPB has arisen because mutations in this protein are associated with rare, familial forms of Motor Neurone Disease (also called Amyotrophic Lateral Sclerosis and Lou Gehrig's disease). VAPB Vesicle-associated membrane protein-associated protein B/C is a protein that in humans is encoded by the "VAPB" gene. The VAPB gene is found on the 20th human chromosome. Together with VAPA, it forms the VAP protein family. The protein encoded by this gene is a type IV membrane protein found in plasma and intracellular vesicle membranes. The encoded protein is found as a homodimer and as a heterodimer with VAPA. This protein also

neg: Carboxyglutamic acid Carboxyglutamic acid Carboxyglutamic acid (or the conjugate base, carboxyglutamate), is an uncommon amino acid introduced into proteins by a post-translational carboxylation of glutamic acid residues. This modification is found, for example, in clotting factors and other proteins of the coagulation cascade. This modification introduces an affinity for calcium ions. In the blood coagulation cascade, vitamin K is required to introduce gamma-carboxylation of clotting factors II, VII, IX, X and protein Z. In the biosynthesis of formula_1-carboxyglutamic acid, the formula_1-proton on glutamic acid is abstracted, and CO is subsequently added. The reaction intermediate is a formula_1-glutamyl carbanion. This reaction is catalyzed

neg: Factor V Leiden Factor V Leiden Factor V Leiden (rs6025) is a variant (mutated form) of human factor V (one of several substances that helps blood clot), which causes an increase in blood clotting (hypercoagulability). With this mutation, protein C, an anticoagulant protein (which normally inhibits the pro-clotting activity of factor V), is not able to bind normally to Factor V, leading to a hypercoagulable state, i.e., an increased tendency for the patient to form abnormal and potentially harmful blood clots. Factor V Leiden is the most common hereditary hypercoagulability (prone to clotting) disorder amongst ethnic Europeans. It is named after the Dutch

neg: Protein C However, a 2012 Cochrane review found that its use cannot be recommended as it does not improve survival and increases bleeding risk. In October 2011 Xigris was withdrawn from the market by Eli Lilly due to a higher mortality in a trial among adults. Protein C's anticoagulant role in the human body was first noted by Seegers "et al." in 1960, who gave protein C its original name, "autoprothrombin II-a". Protein C was first isolated by Johan Stenflo from bovine plasma in 1976, and Stenflo determined it to be a vitamin K-dependent protein. He named it protein "C" because it

neg: Warfarin clotting factors II, VII, IX and X, as well as the regulatory factors protein C, protein S, and protein Z. Other proteins not involved in blood clotting, such as osteocalcin, or matrix Gla protein, may also be affected. The precursors of these factors require gamma carboxylation of their glutamic acid residues to allow the coagulation factors to bind to phospholipid surfaces inside blood vessels, on the vascular endothelium. The enzyme that carries out the carboxylation of glutamic acid is gamma-glutamyl carboxylase. The carboxylation reaction will proceed only if the carboxylase enzyme is able to convert a reduced form of vitamin

neg: Protein C either of these two proteins is absent in murine specimens, the mouse dies from excessive blood-clotting while still in an embryonic state. On the endothelium, APC performs a major role in regulating blood clotting, inflammation, and cell death (apoptosis). Because of the accelerating effect of thrombomodulin on the activation of protein C, the protein may be said to be activated not by thrombin but the thrombin–thrombomodulin (or even thrombin–thrombomodulin–EPCR) complex. Once in active form, APC may or may not remain bound to EPCR, to which it has approximately the same affinity as the protein zymogen. Protein C in zymogen form

neg: VAPB VAPB Vesicle-associated membrane protein-associated protein B/C is a protein that in humans is encoded by the "VAPB" gene. The VAPB gene is found on the 20th human chromosome. Together with VAPA, it forms the VAP protein family. The protein encoded by this gene is a type IV membrane protein found in plasma and intracellular vesicle membranes. The encoded protein is found as a homodimer and as a heterodimer with VAPA. This protein also can interact with VAMP1 and VAMP2 and may be involved in vesicle trafficking. Like VAPA, VAPB binds to proteins that contain a FFAT motif. Considerable interest in

neg: Lower gastrointestinal bleeding blood should be immediately corrected if possible. Platelets should be maintained above 50,000/mL and clotting abnormalities should be corrected with vitamin K or fresh frozen plasma. Vitamin K should be taken orally unless the patient has cirrhosis or biliary obstruction, in which case it should be administered subcutaneously. The full effect of vitamin K is not obtained for 12–24 hours, unlike fresh frozen plasma which immediately reverses clotting abnormalities. The intravenous formulation of vitamin K reverses coagulopathy more quickly and may be used in cases of severe bleeding, however, patients should be monitored for anaphylaxis. The effects of fresh frozen

neg: VEK-30 protein domain to Pg-K5), of which the first three make the protein angiostatin. VEK-30 is a protein domain of the group A streptococcal protein PAM. It binds to Pg-K2 domain of angiostatin and activates the molecule to mediate its anti-angiogenic effects. VEK-30 binds to angiostatin via a C-terminal lysine with argininyl and glutamyl side chain residues known as a 'through space isostere'. Since VEK-30 binds to Pg-K2 domain of angiostatin, its function is crucial to blood clotting, and in lower organisms increase their pathogenicity. In solution, it has been found that VEK-30, exhibited the canonical fold of a kringle domain, including a

neg: LCCL domain protein Lgl1, contains two tandem copies of the LCCL domain. LCCL domain In molecular biology, the LCCL domain is a protein domain which has been named after several well-characterised proteins that were found to contain it, namely Limulus clotting factor C, Coch-5b2 (Cochlin) and Lgl1. It is an about 100 amino acids domain whose C-terminal part contains a highly conserved histidine in a conserved motif YxxxSxxCxAAVHxGVI. The LCCL module is thought to be an autonomously folding domain that has been used for the construction of various modular proteins through exon-shuffling. It has been found in various metazoan proteins in association

neg: Kringle domain is defined by a number of hydrogen bonds and small pieces of anti-parallel beta-sheet. They are found in a varying number of copies in some plasma proteins including prothrombin and urokinase-type plasminogen activator, which are serine proteases belonging to MEROPS peptidase family S1A. ATF; F12; F2; HABP2; HGF; HGFAC; KREMEN1; KREMEN2; LPA; LPAL2; MST1; PIK3IP1; PLAT; PLAU; PLG; PRSS12; ROR1; ROR2; Kringle domain Kringle Domains are autonomous protein domains that fold into large loops stabilized by 3 disulfide linkages. These are important in protein–protein interactions with blood coagulation factors. The name Kringle comes from the Scandinavian pastry that these structures

neg: VKORC1 VKORC1 The human gene "VKORC1" encodes for the enzyme, Vitamin K epOxide Reductase Complex (VKORC) subunit 1. This enzymatic protein complex is responsible for reducing vitamin K 2,3-epoxide to its active form, which is important for effective clotting. In humans, mutations in this gene can be associated with deficiencies in vitamin-K-dependent clotting factors. The VKORC1 protein is a key enzyme in the vitamin K cycle. VKORC1 is a 163 amino acid integral membrane protein associated with the endoplasmic reticulum and VKORC1 mRNA is broadly expressed in many different tissues. VKORC1 is involved in the vitamin K cycle by reduction of

neg: TMEM156 protein that is found in the cytoplasm. The k-NN tool suggests the location of TMEM156 in the Endoplasmic Reticulum of the cell with 44.4% certainty. The following locations were all predicted with 11.1% certainty: vacuolar, vesicles of secretory system, extracellular, plasma membrane, and mitochondrial. TMEM156 is expressed in several tissues including ascites, bone marrow, salivary glands, and vascular to name a few. It should be noted this gene is not ubiquitously expressed, but is still evident in many tissues. This gene is predominately expressed in adults but there is a bit of expression in fetuses. Transmembrane protein 156 has one

neg: Clearance (pharmacology) on plasma protein binding, even with the fact that plasma proteins increase in concentration in the distal renal glomerulus as plasma is filtered into Bowman's capsule, because the relative increases in concentrations of substance-protein and non-occupied protein are equal and therefore give no net binding or dissociation of substances from plasma proteins, thus giving a constant plasma concentration of free substance throughout the glomerulus, which also would have been the case without any plasma protein binding. In other sites than the kidneys, however, where clearance is made by membrane transport proteins rather than filtration, extensive plasma protein binding may increase

neg: Ecarin clotting time the measurement of all direct thrombin inhibitors. Ecarin clotting time Ecarin clotting time (ECT) is a laboratory test used to monitor anticoagulation during treatment with hirudin, an anticoagulant medication which was originally isolated from leech saliva. Ecarin, the primary reagent in this assay, is derived from the venom of the saw-scaled viper, "Echis carinatus". In the clinical assay, a known quantity of ecarin is added to the plasma of a patient treated with hirudin. Ecarin activates prothrombin through a specific proteolytic cleavage, which produces meizothrombin, a prothrombin-thrombin intermediate which retains the full molecular weight of prothrombin, but possesses a low

neg: Ecarin clotting time Ecarin clotting time Ecarin clotting time (ECT) is a laboratory test used to monitor anticoagulation during treatment with hirudin, an anticoagulant medication which was originally isolated from leech saliva. Ecarin, the primary reagent in this assay, is derived from the venom of the saw-scaled viper, "Echis carinatus". In the clinical assay, a known quantity of ecarin is added to the plasma of a patient treated with hirudin. Ecarin activates prothrombin through a specific proteolytic cleavage, which produces meizothrombin, a prothrombin-thrombin intermediate which retains the full molecular weight of prothrombin, but possesses a low level of procoagulant enzymatic activity. Crucially, this

neg: Warfarin and purple toes syndrome. Use is not recommended during pregnancy. It is recommended that the effects of warfarin typically be monitored by checking prothrombin time (INR) every one to four weeks. Many other medications and dietary factors can interact with warfarin, either increasing or decreasing its effectiveness. The effects of warfarin may be reversed with phytonadione (vitamin K1), fresh frozen plasma, or prothrombin complex concentrate. Warfarin decreases blood clotting by blocking an enzyme called vitamin K epoxide reductase that reactivates vitamin K. Without sufficient active vitamin K, clotting factors II, VII, IX, and X have decreased clotting ability. The anticlotting

neg: Amoxapine to norepinephrine transporter blockade. Amoxapine is metabolised into two main active metabolites: 7-hydroxyamoxapine and 8-hydroxyamoxapine. Where: - t is the elimination half life of the compound. - t is the time to peak plasma levels after oral administration of amoxapine. - C is the steady state plasma concentration. - protein binding is the extent of plasma protein binding. - V is the volume of distribution of the compound. Brand names for amoxapine include (where † denotes discontinued brands): Amoxapine Amoxapine, sold under the brand name Asendin among others, is a tricyclic antidepressant (TCA). It is the N-demethylated metabolite of loxapine.

neg: Teniposide The enzyme inducers phenobarbital and phenytoin have been found to lower its blood plasma concentrations. Theoretically possible interactions include increased plasma concentrations when combined with sodium salicylate, sulfamethizole or tolbutamide, which displace teniposide from plasma protein binding, at least "in vitro". Teniposide causes dose-dependent single- and double-stranded breaks in DNA and DNA-protein cross-links. The substance has been found to act as an inhibitor of topoisomerase II (an enzyme that aids in DNA unwinding), since it does not intercalate into DNA or bind strongly to DNA. The cytotoxic effects of teniposide are related to the relative number of double-stranded DNA breaks

neg: GPR158 GPR158 Probable G-protein coupled receptor 158 is a protein that in humans is encoded by the "GPR158" gene. This protein is an orphan class C GPCR. It is highly expressed in the brain, where it binds to RGS7, an inhibitor of G-coupled GPCR signaling, localizing it to the plasma membrane. It is expressed at lower levels in other organs and shows an unusual subcellular localization pattern, being found at both the plasma membrane and in the nucleus. GPR158 in the medial prefrontal cortex (mPFC) has been shown to regulate stress-induced depression in a mouse model of depression and has been

neg: Antiphospholipid syndrome does not correct in an 80:20 mixture with normal human plasma (50:50 mixes with normal plasma are insensitive to all but the highest antibody levels). The APTT (plus 80:20 mix), dilute Russell's viper venom time (DRVVT), kaolin clotting time (KCT), dilute thromboplastin time (TDT/DTT), silica clotting time (SCT) and prothrombin time (using a lupus sensitive thromboplastin) are the principal tests used for the detection of lupus anticoagulant. These tests must be carried out on a minimum of two occasions at least 6 weeks apart and be positive on each occasion, demonstrating persistent positivity, to allow a diagnosis of antiphospholipid syndrome.

neg: Unconventional protein secretion Unconventional protein secretion Unconventional protein secretion (known as ER/Golgi-independent protein secretion or nonclassical protein export ) represents a manner in which the proteins are delivered to the surface of plasma membrane or extracellular matrix independent of the Endoplasmic reticulum or Golgi apparatus. This includes cytokines and mitogens with crucial function in complex processes such as inflammatory response or tumor-induced angiogenesis. Most of these proteins are involved in processes in higher eukaryotes, however an unconventional export mechanism was found in lower eukaryotes too. Even proteins folded in their correct conformation can pass plasma membrane this way, unlike proteins transported via ER/Golgi

neg: Platelet-rich plasma Platelet-rich plasma Platelet-rich plasma (PRP), also known as autologous conditioned plasma, is a concentrate of platelet-rich plasma protein derived from whole blood, centrifuged to remove red blood cells. Evidence for benefit is poor. As a concentrated source of blood plasma and autologous conditioned plasma, PRP contains several different growth factors and other cytokines. PRP has been investigated and used for chronic tendinitis, osteoarthritis, in oral surgery, and in plastic surgery. A 2015 meta-analysis on PRP for osteoarthritis (OA) of the knee and found that nine were worth considering and concluded that with respect to short term outcomes, PRP was no

neg: Fresh frozen plasma Fresh frozen plasma Fresh frozen plasma (FFP) is a blood product made from the liquid portion of whole blood. It is used to treat conditions in which there are low blood clotting factors (INR>1.5) or low levels of other blood proteins. It is also used as part of plasma exchange. The specific batch typically needs to be tested for compatibility before it is given. Use as a volume expander is not recommended. It is given by injection into a vein. Side effects include nausea and itchiness. Rarely there may be allergic reactions, blood clots, or infections. It is unclear if

neg: EGF-like domain O-linked fucose at Ser60. Multiple cbEGF domains are often connected by one or two amino acids to form larger, repetitive arrays, here referred to as 'cbEGF modules'. In the blood-clotting cascade, coagulation factors VII, IX and X and protein C contain a tandem of two cbEGF modules, whereas protein S has four. Impressively, in fibrillin-1 and fibrillin-2, 43 cbEGF modules have been found. The modularity of these proteins adds complexity to protein-protein but also module-module interaction. In factors VII, IX and X, the two cbEGF modules are preceded by an N-terminal gamma-carboxyglutamic acid (Gla) containing module (the Gla module). In

neg: Plasma protein binding the drug. The fraction unbound can be altered by a number of variables, such as the concentration of drug in the body, the amount and quality of plasma protein, and other drugs that bind to plasma proteins. Higher drug concentrations would lead to a higher fraction unbound, because the plasma protein would be saturated with drug and any excess drug would be unbound. If the amount of plasma protein is decreased (such as in catabolism, malnutrition, liver disease, renal disease), there would also be a higher fraction unbound. Additionally, the quality of the plasma protein may affect how many drug-binding

neg: Blood blood plasma proteins, and trace amounts of other materials. Plasma circulates dissolved nutrients, such as glucose, amino acids, and fatty acids (dissolved in the blood or bound to plasma proteins), and removes waste products, such as carbon dioxide, urea, and lactic acid. Other important components include: The term serum refers to plasma from which the clotting proteins have been removed. Most of the proteins remaining are albumin and immunoglobulins. Blood pH is regulated to stay within the narrow range of 7.35 to 7.45, making it slightly basic. Blood that has a pH below 7.35 is too acidic, whereas blood pH

neg: Protein targeting in the following genetic diseases: As discussed above (see protein translocation), most prokaryotic membrane-bound and secretory proteins are targeted to the plasma membrane by either a co-translation pathway that uses bacterial SRP or a post-translation pathway that requires SecA and SecB. At the plasma membrane, these two pathways deliver proteins to the SecYEG translocon for translocation. Bacteria may have a single plasma membrane (Gram-positive bacteria), or an inner membrane plus an outer membrane separated by the periplasm (Gram-negative bacteria). Besides the plasma membrane the majority of prokaryotes lack membrane-bound organelles as found in eukaryotes, but they may assemble proteins onto

neg: DEPDC1B as the cytoskeleton or plasma membrane. DEPDC1B protein product is predicted to be highly phosphorylated after translation. A single sumolaytion site, found within the RhoGAP domain, indicates the possible interaction of the protein with a SUMO protein, enabling or inhibiting interaction with other proteins. A single palmitoylation site, found within the RhoGAP domain, indicates the possible interaction of the DEPDC1B protein product with a membrane via lipid anchor. No conserved glycolation sites are predicted within the mature DEPDC1B protein product. No signal peptide or transmembrane domains are predicted within human or any ortholog protein. No prenylation sites are predicted in

neg: Congenital distal spinal muscular atrophy on chromosome 12, encodes for a protein that serves as an ion channel, typically found in the plasma membrane and is permeable to Ca. Abnormal regulation of Ca can lead to inefficient muscle contraction. "TRPV4" plays a major role in mechanosensation, as well as osmosensory functions in nerve endings, endothoelia, and alveoli. The TRPV4 protein consists of 871 amino acids with its N- and C- terminals facing intracellularly. The protein also contains six alpha helices that pass through the plasma membrane. Mutations in "TRPV4" can result in the loss of its normal function, or a toxic gain of function. In

neg: Pregnancy-associated plasma protein A with aneuploid fetuses (fetuses with an abnormal number of chromosomes). For example, low PAPPA may be commonly seen in prenatal screening for Down syndrome. Low levels may alternatively predict issues with the placenta, resulting in adverse complications such as intrauterine growth restriction, preeclampsia, placental abruption, premature birth, or fetal death. Pregnancy-associated plasma protein A has been shown to interact with Major basic protein. Pregnancy-associated plasma protein A Pappalysin-1, also known as pregnancy-associated plasma protein A, is a protein encoded by the PAPPA gene in humans. PAPPA is a secreted protease whose main substrate is insulin-like growth factor binding proteins. Pappalysin-1

neg: Protein C was the third protein ("peak C") that eluted from a DEAE-Sepharose ion-exchange chromotograph. Seegers was, at the time, searching for vitamin K-dependent coagulation factors undetected by clotting assays, which measure global clotting function. Soon after this, Seegers recognised Stenflo's discovery was identical with his own. Activated protein C was discovered later that year, and in 1977 it was first recognised that APC inactivates Factor V. In 1980, Vehar and Davie discovered that APC also inactivates Factor VIII, and soon after, Protein S was recognised as a cofactor by Walker. In 1982, a family study by Griffin "et al". first associated

neg: Plasma membrane H+-ATPase Plasma membrane H+-ATPase This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. To be specific, the protein is a part of the P-type ATPase family. The systematic name of this enzyme class is ATP phosphohydrolase (-exporting). -exporting ATPase is also known as proton ATPase or more simply proton pump. Other names in common use include proton-translocating ATPase, yeast plasma membrane -ATPase, plant plasma membrane -ATPase, yeast plasma membrane ATPase, plant plasma membrane ATPase, and ATP phosphohydrolase. The yeast (Saccharomyces cerevisiae) enzyme is encoded by the gene Pma1 and hence

neg: Pregnancy-associated plasma protein A Pregnancy-associated plasma protein A Pappalysin-1, also known as pregnancy-associated plasma protein A, is a protein encoded by the PAPPA gene in humans. PAPPA is a secreted protease whose main substrate is insulin-like growth factor binding proteins. Pappalysin-1 is also used in screening tests for Down syndrome. This gene encodes a secreted metalloproteinase which cleaves insulin-like growth factor binding proteins (IGFBPs). PAPPA's proteolytic function is activated upon collagen binding. It is thought to be involved in local proliferative processes such as wound healing and bone remodeling. Low plasma level of this protein has been suggested as a biochemical marker for pregnancies

neg: Choline transporter membrane of the brain microvascular endothelial cells. They are also found on the mitochondrial membrane. CTL2 was found to be highly expressed on the mitochondria. Meanwhile, CTL1 was mostly found on the plasma membrane of those microvascular cells. CTL2 is the main protein involved in the absorption of choline into the mitochondria for its oxidation, and CTL1 is the main protein for the choline uptake from the extracellular medium. CTL1 is a pH dependent protein. The absorption of choline through CTL1 proteins changes with the pH of the extracellular medium. When the pH of the medium is changed from 7.5

neg: Zafirlukast an apparent steady state volume of distribution of 70 liters. Zafirlukast is highly plasma protein bound, 99% bound to albumin. Albumin is the most abundant protein found in human plasma and is capable of carrying and transporting drugs (like zafirlkast) throughout the body. "In vivo" research indicates that zafirlukast has low blood-brain barrier penetration. The blood-brain barrier is a protective system that prevents many chemicals from entering the brain. Zafirlukast undergoes extensive hepatic metabolism into inactive metabolites. Zafirlukast is primarily metabolized by the enzyme CYP2C9 to a hydroxylated metabolite. Zafirlukast is primarily cleared through biliary excretion at a rate of

neg: NNT (gene) including failure to thrive, recurrent illnesses or infections, convulsions, and shock. Diagnosis is confirmed with a low plasma cortisol measurement in the presence of an elevated adrenocorticotropic hormone level, and normal aldosterone and plasma renin measurements. NNT (gene) NAD(P) transhydrogenase, mitochondrial is an enzyme that in humans is encoded by the "NNT" gene on chromosome 5. The NNT gene contains 26 exons and encodes a transhydrogenase protein that is ~109 kDa in molecular weight and is involved in antioxidant defense in the mitochondria. Two alternatively spliced variants, encoding the same protein, have been found for this gene. Transhydrogenases including NNT

neg: Serotonin–dopamine reuptake inhibitor of sertraline and the compound from which sertraline was originally derived, is an NDRI that was never marketed. Single doses of 50 to 200 mg sertraline have been found to result in peak plasma concentrations of 20 to 55 ng/mL (65–180 nM), while chronic treatment with 200 mg/day sertraline, the maximum recommended dosage, has been found to result in maximal plasma levels of 118 to 166 ng/mL (385–542 nM). However, sertraline is highly protein-bound in plasma, with a bound fraction of 98.5%. Hence, only 1.5% is free and theoretically bioactive. Based on this percentage, free concentrations of sertraline would be

neg: Bleeding The gut bacteria make vitamin K and are killed by antibiotics. This decreases vitamin K levels and therefore the production of these clotting factors. Deficiencies of platelet function may require platelet transfusion while deficiencies of clotting factors may require transfusion of either fresh frozen plasma or specific clotting factors, such as Factor VIII for patients with hemophilia. Dioxaborolane chemistry enables radioactive fluoride (F) labeling of red blood cells, which allows for positron emission tomography (PET) imaging of intracerebral hemorrhages. The word "Haemorrhage" (or "hæmorrhage"; using the æ ligature) comes from Latin haemorrhagia, from Ancient Greek αἱμορραγία (haimorrhagía, “a violent bleeding”),

neg: Lipid-anchored protein then amide linked to the C-terminal of the carboxyl group of the respective protein. The GPI attachment occurs through the action of GPI-transamidase complex. The fatty acid chains of the phosphatidylinositol are inserted into the membrane and thus are what anchor the protein to the membrane. These proteins are only located on the exterior surface of the plasma membrane. The sugar residues in the tetrasaccaride and the fatty acid residues in the phosphatidylinositol group vary depending on the protein. This great diversity is what allows the GPI proteins to have a wide range of functions including acting as hydrolytic enzymes,

neg: Electrolyte exclusion effect the concentration of an electrolyte, say Na is determined to be 140 mmol/L, it is the concentration in total plasma volume, not in plasma water volume. This phenomenon produces only a slight difference as volume fraction of water in plasma is sufficiently constant. But, in patients with severe endogenous or exogenous hypertriglyceridemia and in patients with high plasma protein concentration (usually due to paraproteinemia), water portion of plasma is replaced with either lipid or protein causing falsely low electrolyte value (pseudohyponatremia). Conversely, in patients with low plasma protein concentration (a finding often seen in critical care), the water content of

neg: K-Casein different types of proteases at levels when no milk clotting is yet apparent, unveiling its higher sensitivity over currently used assay procedures. Therefore, the method may find application as an indicator during the purification or characterization of new milk-clotting enzymes. K-Casein Κ-Casein (or kappa casein) is a mammalian milk protein involved in a number of important physiological processes. In the gut, the ingested protein is split into an insoluble peptide (para kappa-casein) and a soluble hydrophilic glycopeptide (caseinomacropeptide). Caseinomacropeptide is responsible for increased efficiency of digestion, prevention of neonate hypersensitivity to ingested proteins, and inhibition of gastric pathogens. Caseins are

neg: LRRC8E a recent study that found that this gene was nominally associated with panic disorder. LRRC8E Leucine-rich repeat-containing protein 8E is a protein that in humans is encoded by the "LRRC8E" gene. Researchers have found out that this protein, along with the other LRRC8 proteins LRRC8A, LRRC8B, LRRC8C, and LRRC8D, is sometimes a subunit of the heteromer protein Volume-Regulated Anion Channel. Volume-Regulated Anion Channels (VRACs) are crucial to the regulation of cell size by transporting chloride ions and various organic osmolytes, such as taurine or glutamate, across the plasma membrane, and that is not the only function these channels have been

neg: Tramadol 16% higher and the area-under-the-curve levels 36% higher than following a single oral 100-mg dose. Positron emission tomography imaging studies have reportedly found that tramadol levels are at least four-fold higher in the brain than in plasma. Conversely, brain levels of desmetramadol "only slowly approach those in plasma". The plasma protein binding of tramadol is only 4 to 20%; hence, almost all tramadol in circulation is free, thus bioactive. Co-administration of quinidine, a potent CYP2D6 enzyme inhibitor, with tramadol, a combination which results in markedly reduced levels of desmetramadol, was found not to significantly affect the analgesic effects of tramadol

neg: VKORC1 and rats, because the amount and effectiveness of the VKORC enzyme has not changed, but the ability of warfarin to exert its effect (antagonize the enzyme) has changed. These isoform mutations are rare except in Ethiopian and certain Jewish populations. VKORC1 The human gene "VKORC1" encodes for the enzyme, Vitamin K epOxide Reductase Complex (VKORC) subunit 1. This enzymatic protein complex is responsible for reducing vitamin K 2,3-epoxide to its active form, which is important for effective clotting. In humans, mutations in this gene can be associated with deficiencies in vitamin-K-dependent clotting factors. The VKORC1 protein is a key enzyme

neg: Calcium metabolism remain within very narrow limits by homeostatic negative feedback systems. Between 35-50% of the calcium in plasma is protein-bound, and 5-10% is in the form of complexes with organic acids and phosphates. The remainder (50-60%) is ionized. The ionized calcium can be determined directly by colorimetry, or it can be read off from nomograms, though the usefulness of the latter is limited when the pH and protein content of the plasma deviate widely from the normal. Not all the calcium in the diet can be readily absorbed from the gut. The calcium that is most readily absorbed is found in

neg: Plasma protein binding Plasma protein binding Plasma protein binding refers to the degree to which medications attach to proteins within the blood. A drug's efficiency may be affected by the degree to which it binds. The less bound a drug is, the more efficiently it can traverse cell membranes or diffuse. Common blood proteins that drugs bind to are human serum albumin, lipoprotein, glycoprotein, and α, β‚ and γ globulins. A drug in blood exists in two forms: bound and unbound. Depending on a specific drug's affinity for plasma protein, a proportion of the drug may become bound to plasma proteins, with the

neg: Autotransfusion concentration of fluid in an extracorporeal circuit. Postoperative autotransfusion refers to the recovery of blood in the extracorporeal circuit at the end of surgery or from aspirated drainage. The disadvantage of autotransfusion is the depletion of plasma and platelets. The washed autotransfusion system removes the plasma and platelets to eliminate activated clotting factors and activated platelets which would cause coagulopathy if they were reinfused to the patient, generating a packed red blood cell (PRBC) product. This disadvantage is only evident when very large blood losses occur. The autotransfusionist monitors blood loss and will recommend the transfusion of fresh frozen plasma

neg: Protein C protein C is a vitamin K-dependent glycoprotein that circulates in blood plasma. Its structure is that of a two-chain polypeptide consisting of a light chain and a heavy chain connected by a disulfide bond. The protein C zymogen is activated when it binds to thrombin, another protein heavily involved in coagulation, and protein C's activation is greatly promoted by the presence of thrombomodulin and endothelial protein C receptors (EPCRs). Because of EPCR's role, activated protein C is found primarily near endothelial cells (i.e., those that make up the walls of blood vessels), and it is these cells and leukocytes (white

neg: Autotransfusion counterclockwise rotation and clamps adjust, enabling the transfer of wash solution to the wash bowl. The washing phase removes cellular stromata, plasma free hemoglobin, anticoagulant solution, activated clotting factors, any plasma bound antibiotics, intracellular enzymes, plasma, platelets, and white cells. The unwanted fluid passes out of the wash bowl and into a waste reservoir bag. Washing continues until the reinfuse button is depressed (or the program ends, in the case of an automatic device) and the appropriate amount of wash solution has been delivered to the wash bowl. The wash phase is terminated when one to two liters of wash