query: about 7 of plasma is made up of proteins . the most abundant of these plasma proteins is

pos: Blood proteins Blood proteins Blood proteins, also termed plasma proteins, are proteins present in blood plasma. They serve many different functions, including transport of lipids, hormones, vitamins and minerals in activity and functioning of the immune system. Other blood proteins act as enzymes, complement components, protease inhibitors or kinin precursors. Contrary to popular belief, haemoglobin is not a blood protein, as it is carried within red blood cells, rather than in the blood serum. Serum albumin accounts for 55% of blood proteins, and is a major contributor to maintaining the oncotic pressure of plasma to assist in the transport of lipids and

pos: Fetuin Fetuin Fetuins are blood proteins that are made in the liver and secreted into the bloodstream. They belong to a large group of binding proteins mediating the transport and availability of a wide variety of cargo substances in the bloodstream. Fetuin-A is a major carrier protein of free fatty acids in the circulation. The best known representative of carrier proteins is serum albumin, the most abundant protein in the blood plasma of adult animals. Fetuin is more abundant in fetal blood, hence the name "fetuin" (from Latin, "fetus"). Fetal bovine serum contains more fetuin than albumin, while adult serum contains

pos: Fructosamine serum proteins that have undergone glycation (the "glycated serum proteins"). Since albumin is the most abundant protein in blood, fructosamine levels typically reflect albumin glycation. (Some fructosamine tests specifically quantify the glycation of albumin, or "glycated serum albumin" instead of all proteins.). Because albumin has a half-life of approximately 20 days, the plasma fructosamine concentration reflects relatively recent (1–2 week) changes in blood glucose. In patients with diseases that reduce red blood cell lifespan, such as hemolytic anaemia or hemoglobinopathies such as sickle-cell disease, a hemoglobin-based A1c test can be misleadingly low. A1c results may also be falsely high or

pos: 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

pos: Snake venom solubility and lowest isoelectric point of all the major plasma proteins. This makes it the final fraction to be precipitated from its solution. Bovine serum albumin is located in fraction V. The precipitation of albumin is done by reducing the pH to 4.8, which is near the pI of the proteins, and maintaining the ethanol concentration to be 40%, with a protein concentration of 1%. Thus, only 1% of the original plasma remains in the fifth fraction. When the ultimate goal of plasma processing is a purified plasma component for injection or transfusion, the plasma component must be highly pure.

pos: Alpha-Parinaric acid in the protein and the bound chromophore, information may be gleaned about the molecular interactions between protein and lipid. For example, this technique is used to investigate how fatty acids bind to serum albumin (a highly abundant blood protein), lipid transport processes including structural characterization of lipoproteins, and phospholipid-transfer proteins. The concentrations of fatty acids in blood serum or plasma can be measured using α-parinaric acid, which will compete for binding sites on serum albumin. α-Parinaric acid has been used to study the hydrophobicity and foaming characteristics of food proteins, as well as the foam stability of beer. In this

neg: Blood plasma fractionation denature. Many of the proteins in plasma have important therapeutic uses. Albumin is commonly used to replenish and maintain blood volume after traumatic injury, during surgery, and during plasma exchange. Since albumin is the most abundant protein in the plasma its use may be the most well known, but many other proteins, although present in low concentrations, can have important clinical uses. See table below. When the ultimate goal of plasma processing is a purified plasma component for injection or transfusion, the plasma component must be highly pure. The first practical large-scale method of blood plasma fractionation was developed by

neg: Cell membrane a variety of mechanisms: The cell membrane consists of three classes of amphipathic lipids: phospholipids, glycolipids, and sterols. The amount of each depends upon the type of cell, but in the majority of cases phospholipids are the most abundant, often contributing for over 50% of all lipids in plasma membranes. Glycolipids only account for a minute amount of about 2% and sterols make up the rest. In RBC studies, 30% of the plasma membrane is lipid. However, for the majority of eukaryotic cells, the composition of plasma membranes is about half lipids and half proteins by weight. The fatty chains

neg: 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

neg: Blood proteins for biomarkers. These efforts started with two-dimensional gel electrophoresis efforts in the 1970s and in more recent times this research has been performed using LC-tandem MS based proteomics. The normal laboratory value of serum total protein is around 7 g/dL. Examples of specific blood proteins: Blood proteins Blood proteins, also termed plasma proteins, are proteins present in blood plasma. They serve many different functions, including transport of lipids, hormones, vitamins and minerals in activity and functioning of the immune system. Other blood proteins act as enzymes, complement components, protease inhibitors or kinin precursors. Contrary to popular belief, haemoglobin is not

neg: 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

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: Photosynthesis Earth's atmosphere, and supplies all of the organic compounds and most of the energy necessary for life on Earth. Although photosynthesis is performed differently by different species, the process always begins when energy from light is absorbed by proteins called reaction centres that contain green chlorophyll pigments. In plants, these proteins are held inside organelles called chloroplasts, which are most abundant in leaf cells, while in bacteria they are embedded in the plasma membrane. In these light-dependent reactions, some energy is used to strip electrons from suitable substances, such as water, producing oxygen gas. The hydrogen freed by the splitting

neg: Fresh frozen plasma use during pregnancy or breastfeeding is safe for the baby. Greater care should be taken in people with protein S deficiency, IgA deficiency, or heart failure. Fresh frozen plasma is made up of a complex mixture of water, proteins, carbohydrates, fats, and vitamins. When frozen it lasts about a year. Plasma first came into medical use during the Second World War. It is on the World Health Organization's List of Essential Medicines, the most effective and safe medicines needed in a health system. In the United Kingdom it costs about £30 per unit. A number of other versions also exist

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: Cell junction anchoring proteins extend through the plasma membrane to link cytoskeletal proteins in one cell to cytoskeletal proteins in neighboring cells as well as to proteins in the extracellular matrix . Three types of anchoring junctions are observed, and differ from one another in the cytoskeletal protein anchor as well as the transmembrane linker protein that extends through the membrane: Anchoring-type junctions not only hold cells together but provide tissues with structural cohesion. These junctions are most abundant in tissues that are subject to constant mechanical stress such as skin and heart. Desmosomes, also termed as maculae adherentes, can be visualized

neg: Blood plasma fractionation abundance of proteins many of which can be used as biomarkers, indicating the presence of certain diseases in an individual. Currently, 2D Electrophoresis is the primary method for discovery and detection of biomarkers in plasma. This involves the separation of plasma proteins on a gel by exploiting differences in their size and pI. Potential disease biomarkers may be present in plasma at very low concentrations, so, plasma samples must undergo preparation procedures for accurate results to be obtained using 2D Electrophoresis. These preparation procedures aim to remove contaminants that may interfere with detection of biomarkers, solubilize the proteins so they

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: Unconventional protein secretion pathway. Two types of unconventional protein secretion are these: signal-peptid-containing proteins and cytoplasmatic and nuclear proteins that are missing an ER-signal peptide (1). These proteins contain a specific signal-peptide sequence, which is to be translated into the endoplasmic reticulum, but are, however, able to reach the cell surface unconventionally. They can be packed into a COPII-coated vesicle and directly fuse with plasma membrane or can fuse with endosomal or lysosomal compartment. Alternatively, they can be packed into non-COPII-coated vesicle as well and fuse with Golgi (before reaching plasma membrane) or directly delivered to the plasma membrane. Soluble proteins can reach

neg: Tight junction exponentially with the number of strands. Each strand is formed from a row of transmembrane proteins embedded in both plasma membranes, with extracellular domains joining one another directly. There are at least 40 different proteins composing the tight junctions. These proteins consist of both transmembrane and cytoplasmic proteins. The three major transmembrane proteins are occludin, claudins, and junction adhesion molecule (JAM) proteins. These associate with different peripheral membrane proteins such as ZO-1 located on the intracellular side of plasma membrane, which anchor the strands to the actin component of the cytoskeleton. Thus, tight junctions join together the cytoskeletons of adjacent

neg: Proteomics be established. Capturing the most meaningful subset of proteins among the entire proteome to generate a diagnostic tool is one such priority. Secondly, since cancer is associated with enhanced glycosylation of proteins, methods that focus on this part of proteins will also be useful. Again: multiparameter analysis best reveals a pathological state. As these technologies improve, the disease profiles should be continually related to respective gene expression changes. Due to the above-mentioned problems plasma proteomics remained challenging. However, technological advancements and continuous developments seem to result in a revival of plasma proteomics as it was shown recently by a technology

neg: Hydrophobic mismatch Hydrophobic mismatch Hydrophobic mismatch is the difference between the thicknesses of hydrophobic regions of a transmembrane protein and of the biological membrane it spans. In order to avoid unfavorable exposure of hydrophobic surfaces to water, the hydrophobic regions of transmembrane proteins are expected to have approximately the same thickness as the hydrophobic (lipid acyl chain) region of the surrounding lipid bilayer. Nevertheless, the same membrane protein can be encountered in bilayers of different thickness. In eukaryotic cells, the plasma membrane is thicker than the membranes of the endoplasmic reticulum. Yet all proteins that are abundant in the plasma membrane are

neg: Blood plasma fractionation about 60% of the total protein in plasma and is present at concentrations between 35 and 55 mg/mL. It is the main contributor to osmotic pressure of the blood and it functions as a carrier molecule for molecules with low water solubility such as lipid-soluble hormones, enzymes, fatty acids, metal ions, and pharmaceutical compounds. Albumin is structurally stable due to its seventeen disulfide bonds and unique in that it has the highest water solubility and the lowest isoelectric point (pI) of the plasma proteins. Due to the structural integrity of albumin it remains stable under conditions where most other proteins

neg: Pregnancy zone protein expression in relation to in-vitro fertilisation (IVF) has also been studied, showing upregulation. PZP was shown to be one the proteins determined as potential biomarkers of Poor Ovarian Responder (POR) in IVF. Low PZP concentrations have also been linked to miscarriage during the early stages of pregnancy. Pregnancy zone protein Pregnancy zone protein (PZP) is a protein which in humans is encoded by the "PZP" gene on chromosome 12. PZP is part of the alpha-2 globulin family of proteins. It is often associated with pregnancy, during which it can be the most abundant amongst the plasma proteins. PZP is believed

neg: Hydrophobic mismatch plasma membrane, suggesting a concomitant increase in membrane thickness. In line with this, the average length of transmembrane segment of single-span plasma membrane proteins typically is five amino acids longer than the average length of proteins from the Golgi. Experimental evidence was obtained that protein sorting in the Golgi may be based on this length difference: for several proteins that normally reside in the Golgi, it was shown that increasing their hydrophobic length can reroute the proteins to the plasma membrane, or vice versa, that decreasing the hydrophobic length of proteins from the plasma membrane can cause their retention in

neg: Blood plasma fractionation Edwin J. Cohn during World War II. It is known as the Cohn process (or Cohn method). This process is also known as cold ethanol fractionation as it involves gradually increasing the concentration of ethanol in the solution at 5C and 3C. The Cohn Process exploits differences in properties of the various plasma proteins, specifically, the high solubility and low pI of albumin. As the ethanol concentration is increased in stages from 0% to 40% the [pH] is lowered from neutral (pH ~ 7) to about 4.8, which is near the pI of albumin. At each stage certain proteins are

neg: Pulmonary surfactant lipids diffuse from the blood into type II alveolar cells where they are assembled and packaged for secretion into secretory organelles called lamellar bodies. Proteins make up the remaining 10% of the surfactant. Half of this 10% is plasma proteins but the rest is formed by the apolipoproteins, surfactant proteins SP-A, SP-B, SP-C, and SP-D. The apolipoproteins are produced by the secretory pathway in type II cells. They undergo much post-translational modification, ending up in the lamellar bodies. These are concentric rings of lipid and protein, about 1 µm in diameter. The SP proteins reduce the critical temperature of DPPC's

neg: Blood plasma having a similar ion concentration to that of human blood plasma. SBF is normally used for the surface modification of metallic implants, and more recently in gene delivery application. 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%)

neg: Nitrendipine in reducing blood pressure by 15–20% within 1–2 hours of administration. With long-term treatments, the dosage may rise to as much as 40 mg/day; in elderly individuals, a lower dosage of up to 5 mg/day may be equally effective (this reduction in drug amount is attributed to decreased liver function or “first pass” metabolism). Once digested, nitrendipine is absorbed into the blood and binds to plasma proteins. The majority (98%) is bound to plasma proteins and 70-80% of its inactive polar metabolites are also bound to plasma proteins. Following hepatic metabolism, 80% of the 20 mg dose can be recovered

neg: ERM protein family ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament-plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. ERM proteins Moesin directly binds to microtubules via its N-terminal FERM domain "in vitro" and stabilizes microtubules at the cell cortex "in vivo". This interaction is required for specific ERM-dependent functions in mitosis. ERM proteins are highly regulated proteins. They exist in two forms: In culture cells, ERM proteins mainly exhibit the folded conformation (about 80-85%). The current model for ERM proteins activation is a two-steps mechanism:

neg: PCDHB13 clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3' exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections. PCDHB13 Protocadherin beta-13 is a protein that in humans is encoded by the "PCDHB13" gene. This gene is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. The gene clusters demonstrate an unusual genomic organization

neg: Affilin Affilin proteins are about 10 kDa in mass. The molecular mass of crystallin and ubiquitin based Affilin proteins is only one eighth or one sixteenth of an IgG antibody, respectively. This leads to an improved tissue permeability, heat stability up to 90 °C (195 °F), and stability towards proteases as well as acids and bases. The latter enables Affilin proteins to pass through the intestine, but like most proteins they are not absorbed into the bloodstream. Renal clearance, another consequence of their small size, is the reason for their short plasma half-life, generally a disadvantage for potential drugs. Molecular libraries

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: Plasma cell dyscrasia or repetitive sections, any of which such changes may promote malignancy in more complex and less well understood ways. These mutations lead to the uncontrolled overproduction of an IgG, IgA, IgE, or IgD antibody, a κ or λ light chain, or, very rarely, an α, γ, or μ heavy chain or fragments of these proteins. The overproduced Ig's, termed myeloma proteins, commonly circulate in blood, may accumulate in urine, and are the hallmarks of plasma cell dyscrasias including their most malignant forms viz., multiple myeloma, light chain multiple myeloma, and plasma cell leukemia. IgG-secretory, IgA-secretory, and light-chain secretory multiple myeloma

neg: 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.

neg: Proteomics daunting challenge. The depth of the plasma proteome encompassing a dynamic range of more than 10 between the highest abundant protein (albumin) and the lowest (some cytokines) and is thought to be one of the main challenges for proteomics. Temporal and spatial dynamics further complicate the study of human plasma proteome. The turnover of some proteins is quite faster than others and the protein content of an artery may substantially vary from that of a vein. All these differences make even the simplest proteomic task of cataloging the proteome seem out of reach. To tackle this problem, priorities need to

neg: Gene product class of proteins are found in plasma membranes. Membrane proteins can be associated with the plasma membrane in different ways, depending on their structure. These proteins allow the cell to import or export cell products, nutrients or signals to and from the extracellular space. Other proteins help the cell to perform regulatory functions. For example, transcription factors bind to DNA to help transcription of RNA. Gene product A gene product is the biochemical material, either RNA or protein, resulting from expression of a gene. A measurement of the amount of gene product is sometimes used to infer how active a

neg: Plasma cell dyscrasia antibody, free light chain, free heavy chain, shortened version of these proteins, or any combination of these proteins) in blood and/or urine as defined by various types of gel electrophoresis. Myeloma proteins form as a result of gene mutations rather than physiological gene remodeling responses to an instigating foreign antigen: typically these proteins are non-functional. However, they sometimes cause serious tissue damage with the kidney being a particularly vulnerable target. The toxic effects of monoclonal proteins may occur at early stages in the plasma cell dyscrasia spectrum and require treatment independently of the mass or tissue-destructive effects of the myeloma

neg: SLC25A31 plasma membrane-bounded apoptotic bodies which contain nuclear and or cytoplasmic elements. The ultrastructural appearance of necrosis is quite different, the main features being mitochondrial swelling, plasma membrane breakdown and cellular disintegration. Apoptosis occurs in many physiological and pathological processes. It plays an important role during embryonal development as programmed cell death and accompanies a variety of normal involutional processes in which it serves as a mechanism to remove "unwanted" cells. The SLC25A31 gene is important for the coding of the most abundant mitochondrial protein Ancp which represents 10% of the proteins of the inner membrane of bovine heart mitochondria. Ancp

neg: Vesicle (biology and chemistry) cell membrane. The vesicle "coat" is a collection of proteins that serve to shape the curvature of a donor membrane, forming the rounded vesicle shape. Coat proteins can also function to bind to various transmembrane receptor proteins, called cargo receptors. These receptors help select what material is endocytosed in receptor-mediated endocytosis or intracellular transport. There are three types of vesicle coats: clathrin, COPI and COPII. The various types of coat proteins help with sorting of vesicles to their final destination. Clathrin coats are found on vesicles trafficking between the Golgi and plasma membrane, the Golgi and endosomes and the plasma

neg: Von Willebrand factor type A domain Von Willebrand factor type A domain The von Willebrand factor is a large multimeric glycoprotein found in blood plasma. Mutant forms are involved in the aetiology of bleeding disorders. In von Willebrand factor, the type A domain (vWF) is the prototype for a protein superfamily. The vWF domain is found in various plasma proteins: complement factors B, C2, CR3 and CR4; the integrins (I-domains); collagen types VI, VII, XII and XIV; and other extracellular proteins. Although the majority of VWA-containing proteins are extracellular, the most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as

neg: Eisosome membrane consists of three compartments: The MCC, a furrow in the plasma membrane, is generated by eisosomes, it disappears in a cell lacking Pil1 which is one of the main eisosome components. These are large protein complexes composed primarily of subunits of two Bin-Amphiphysin-RVS (BAR) domain containing proteins Pil1 and Lsp1. These two paralogue proteins self-assemble in higher order structure helices and bind preferentially to phosphoinositide-containing membrane. It is also found that eisosome associated proteins Slm1 and Slm 2 have F-BAR domains that are used for targeting furrow like plasma membrane invagination. Eisosome Eisosomes ('eis' meaning into or portal and

neg: Alpha helix to their function. Common to many of them is that the hydrophobic face of the antimicrobial peptide forms pores in the plasma membrane after associating with the fatty chains at the membrane core. Myoglobin and hemoglobin, the first two proteins whose structures were solved by X-ray crystallography, have very similar folds made up of about 70% α-helix, with the rest being non-repetitive regions, or "loops" that connect the helices. In classifying proteins by their dominant fold, the Structural Classification of Proteins database maintains a large category specifically for all-α proteins. Hemoglobin then has an even larger-scale quaternary structure, in which

neg: Pregnancy zone protein Pregnancy zone protein Pregnancy zone protein (PZP) is a protein which in humans is encoded by the "PZP" gene on chromosome 12. PZP is part of the alpha-2 globulin family of proteins. It is often associated with pregnancy, during which it can be the most abundant amongst the plasma proteins. PZP is believed to play a role in immune-regulation during pregnancy, however many aspects of its mechanism, function and structure are yet to be determined. Recent research has largely focused on determining how dysregulated PZP levels can act as a markers of various diseases. The first publication reporting PZP was

neg: Clonazepam the brain corresponding with levels of unbound clonazepam in the blood serum. Clonazepam plasma levels are very unreliable amongst patients. Plasma levels of clonazepam can vary as much as tenfold between different patients. Clonazepam is largely bound to plasma proteins. Clonazepam passes through the blood–brain barrier easily, with blood and brain levels corresponding equally with each other. The metabolites of clonazepam include 7-aminoclonazepam, 7-acetaminoclonazepam and 3-hydroxy clonazepam. It is effective for 6–8 hours in children, and 6–12 in adults. A 2006 US government study of emergency department (ED) visits found that sedative-hypnotics were the most frequently implicated pharmaceutical drug in

neg: Protein targeting various types of inclusions such as gas vesicles and storage granules. In gram-negative bacteria proteins may be incorporated into the plasma membrane, the outer membrane, the periplasm or secreted into the environment. Systems for secreting proteins across the bacterial outer membrane may be quite complex and play key roles in pathogenesis. These systems may be described as type I secretion, type II secretion, etc. In most gram-positive bacteria, certain proteins are targeted for export across the plasma membrane and subsequent covalent attachment to the bacterial cell wall. A specialized enzyme, sortase, cleaves the target protein at a characteristic recognition site

neg: Plasma cell dyscrasia (e.g. "KIF2B") as well as cellular activation, proliferation, and apoptosis (e.g. "CIDEC," "TP52, ATM, KRAS, NRAS, Wnt," and "NF-κB"). In the most malignant form of plasma cell dyscrasias, primary plasma cell leukemia, the plasma cell population contains >1900 distinct DNA alterations in >600 genes. In general, the plasma cell dyscrasias are defined by 1) the presence of these genetically unstable clonal plasma cells, lymphoplasmacytoid cells, or B cells infiltrating the bone marrow or forming distinct masses in bone, and/or other tissues as defined by biopsy of involved tissues and 2) the presence of these cells' myeloma proteins (i.e. intact monoclonal

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: Proteomics evolutionary biology. Characterizing the human plasma proteome has become a major goal in the proteomics arena, but it is also the most challenging proteomes of all human tissues. It contains immunoglobulin, cytokines, protein hormones, and secreted proteins indicative of infection on top of resident, hemostatic proteins. It also contains tissue leakage proteins due to the blood circulation through different tissues in the body. The blood thus contains information on the physiological state of all tissues and, combined with its accessibility, makes the blood proteome invaluable for medical purposes. It is thought that characterizing the proteome of blood plasma is a

neg: Ticagrelor the bioavailability being 36%, and reaches its peak concentration after about 1.5 hours. The main metabolite, AR-C124910XX, is formed quickly via CYP3A4 by de-hydroxyethylation at position 5 of the cyclopentane ring. It peaks after about 2.5 hours. Both ticagrelor and AR-C124910XX are bound to plasma proteins (>99.7%), and both are pharmacologically active. Blood plasma concentrations are linearly dependent on the dose up to 1260 mg (the sevenfold daily dose). The metabolite reaches 30–40% of ticagrelor's plasma concentrations. Drug and metabolite are mainly excreted via bile and feces. Plasma concentrations of ticagrelor are slightly increased (12–23%) in elderly patients, women, patients

neg: Steroid hormone pathways are mediated by some type of steroid hormone receptor found at the plasma membrane. Ion channels, transporters, G-protein coupled receptors (GPCR), and membrane fluidity have all been shown to be affected by steroid hormones. Of these, GPCR linked proteins are the most common. For more information on these proteins and pathways, visit the steroid hormone receptor page. Steroid hormone A steroid hormone is a steroid that acts as a hormone. Steroid hormones can be grouped into two classes: corticosteroids (typically made in the adrenal cortex, hence "cortico-") and sex steroids (typically made in the gonads or placenta). Within those

neg: FFAT motif proteins with FFAT motifs were previously not known to be targeted to the endoplasmic reticulum, with the exception of OSBP, and PITPNM1 (the fly homologue of which is called RdgB). Instead, they were known for their localization to other sites especially the "trans" Golgi network (OSBP, Osh1p and CERT) and the plasma membrane (Osh2p, Osh3p). The discovery that these proteins also targeted the endoplasmic reticulum led to a far more detailed analysis of their targeting, and revealed that all the FFAT-containing lipid transfer proteins are present at both the endoplasmic reticulum and their other target Trans Golgi network or plasma

neg: Blood plasma fractionation diagnostic processes. The human plasma proteome may contain thousands of proteins, however, identifying them presents challenges due to the wide range of concentrations present. Some low abundance proteins may be present in picogram (pg/mL) quantities, while high abundance proteins can be present in milligram (mg/mL) quantities. Many efforts to expand the human plasma proteome overcome this difficulty by coupling some type of high performance liquid chromatography (HPLC) or reverse phase liquid chromatography (RPLC) with high efficiency cation exchange chromatography and subsequent tandem mass spectrometry for protein identification. Blood plasma fractionation Blood plasma fractionation refers to the general processes of separating

neg: Rab (G-protein) Rab (G-protein) The Rab family of proteins is a member of the Ras superfamily of monomeric G proteins. Approximately 70 types of Rabs have now been identified in humans. Rab proteins generally possess a GTPase fold, which consists of a six-stranded beta sheet which is flanked by five alpha helixes. Rab GTPases regulate many steps of membrane trafficking, including vesicle formation, vesicle movement along actin and tubulin networks, and membrane fusion. These processes make up the route through which cell surface proteins are trafficked from the Golgi to the plasma membrane and are recycled. Surface protein recycling returns proteins to

neg: Cell membrane groups, Archaea and Bacteria, with bacteria dividing further into gram-positive and gram-negative. Gram-negative bacteria have both a plasma membrane and an outer membrane separated by periplasm, however, other prokaryotes have only a plasma membrane. These two membranes differ in many aspects. The outer membrane of the gram-negative bacteria differ from other prokaryotes due to phospholipids forming the exterior of the bilayer, and lipoproteins and phospholipids forming the interior. The outer membrane typically has a porous quality due to its presence of membrane proteins, such as gram-negative porins, which are pore-forming proteins. The inner, plasma membrane is also generally symmetric whereas

neg: Potassium requires special environmental conditions. Potassium is the eighth or ninth most common element by mass (0.2%) in the human body, so that a 60 kg adult contains a total of about 120 g of potassium. The body has about as much potassium as sulfur and chlorine, and only calcium and phosphorus are more abundant (with the exception of the ubiquitous CHON elements). Potassium ions are present in a wide variety of proteins and enzymes. Potassium levels influence multiple physiological processes, including Potassium homeostasis denotes the maintenance of the total body potassium content, plasma potassium level, and the ratio of the

neg: Endomembrane system leave, preventing materials from entering the cell, averting needed materials from leaving the cell, maintaining the pH of the cytosol, and preserving the osmotic pressure of the cytosol. Transport proteins which allow some materials to pass through but not others are used for these functions. These proteins use ATP hydrolysis to pump materials against their concentration gradients. In addition to these universal functions, the plasma membrane has a more specific role in multicellular organisms. Glycoproteins on the membrane assist the cell in recognizing other cells, in order to exchange metabolites and form tissues. Other proteins on the plasma membrane allow

neg: Polar auxin transport its own by crossing the lipid bilayer. Hence the export of auxin from the cell requires an active component in plasma membrane - i.e. some membrane transport protein. Two protein families: The PIN proteins and ABCB (PGP proteins) transporters are functioning as "auxin efflux carriers" and transport the anionic form of auxin out of the cell. While the PGP auxin efflux carriers are evenly distributed, the PIN proteins are most often maintaining polar (i.e. asymmetric) localisation on the plasma membrane. That is to say that they locate mostly on one side of the cell. Furthermore, the asymmetrical localisation of the

neg: Lipoprotein plasma lipoprotein particles classified as HDL, LDL, IDL, VLDL and ULDL (a.k.a. chylomicrons) lipoproteins, according to density / size (an inverse relationship), compared with the surrounding plasma water. These complex protein capsules enable fats to be carried in all extracellular water, including the blood stream (an example of emulsification), subgroups of which are primary drivers / modulators of atherosclerosis, the transmembrane proteins of mitochondrion, chloroplast, and bacterial lipoproteins. Proteolipids are a different kind of protein-lipid combination that are insoluble in water. Proteolipids are abundant in brain tissue, and are also present in many other animal and plant tissues. The lipids

neg: Distribution (pharmacology) can cause important modifications in a drug's tissue concentration. This will, in turn, increase the risk of the drug having a toxic effect on tissues. Perhaps the most important plasma proteins are the albumins as they are present in relatively high concentrations and they readily bind to other substances. Other important proteins include the glycoproteins, the lipoproteins and to a lesser degree the globulins. It is therefore easy to see that clinical conditions that modify the levels of plasma proteins (for example, hypoalbuminemias brought on by renal dysfunction) may affect the effect and toxicity of a drug that has a

neg: Major intrinsic proteins unclassified X (XIPs) intrinsic proteins. One of the plant clusters includes only tonoplast (TIP) proteins, while another includes plasma membrane (PIP) proteins. The Major Intrinsic Protein (MIP) of the human lens of the eye (Aqp0), after which the MIP family was named, represents about 60% of the protein in the lens cell. In the native form, it is an aquaporin (AQP), but during lens development, it becomes proteolytically truncated. The channel, which normally houses 6-9 water molecules, becomes constricted so only three remain, and these are trapped in a closed conformation. These truncated tetramers form intercellular adhesive junctions (head to

neg: Cation diffusion facilitator eukaryotes. They transport heavy metal ions, such as cadmium, zinc, cobalt, nickel, copper and mercuric ions. There are 9 mammalian paralogues, ZnT1 - 8 and 10. Most proteins from the family have six transmembrane helices, but MSC2 of "S. cerevisiae") and Znt5 and hZTL1 of "H. sapiens" have 15 and 12 predicted TMSs, respectively. These proteins exhibit an unusual degree of sequence divergence and size variation (300-750 residues). Eukaryotic proteins exhibit differences in cell localization. Some catalyze heavy metal uptake from the cytoplasm into various intracellular eukaryotic organelles (ZnT2-7) while others (ZnT1) catalyze efflux from the cytoplasm across the plasma

neg: Farnesyltransferase inhibitor a fatty acid molecule to proteins (such as the oncogene, or cancer-generating, ras). Many proteins can exist in a cell in various locations, and the addition of a farnesyl group targets proteins to the plasma membrane. When ras gets to the plasma membrane, it becomes activated, and leads to tumour formation if this process is not stopped. It was thought that by inhibiting FT, ras will not be activated, therefore preventing cancer growth. The problem was that ras can also be modified by other mechanisms, and thus FTIs were not sufficient to inhibit malignant growth induced by ras signaling. Most

neg: PIN proteins PIN proteins In plants, the PIN proteins are integral membrane proteins that transport the anionic form of the phytohormone auxin across membranes. Most of the PIN proteins (e.g. PIN1/2/3/4/7 in the model plant "Arabidopsis thaliana") localize at the plasma membrane (PM) where they serve as secondary active transporters involved in the efflux of auxin. The PM-localized PIN proteins show asymmetrical localisations on the membrane and are therefore responsible for polar auxin transport. Some other members of the PIN family (e.g. PIN5 and 8 in "Arabidopsis") localize mostly at the ER-membrane or have a dual PM and ER localisation (e.g. PIN6

neg: Bowman's capsule platelets and large proteins do not. As a result, the filtrate leaving the Bowman's capsule is very similar to blood plasma (filtrate or glomerular filtrate is composed of blood plasma minus plasma protein i.e. it contains all the components of blood plasma except the proteins) in composition as it passes into the proximal convoluted tubule. Measuring the glomerular filtration rate (GFR) is a diagnostic test of kidney function. A decreased GFR may be a sign of renal failure. A number of diseases can result in various problems within the glomerulus. Examples include acute proliferative (endocapillary) glomerulonephritis, mesangioproliferative glomerulonephritis, mesangiocapillary (membranoproliferative)

neg: Distribution (pharmacology) earlier ideas and it depends on a number of distinct factors: Some drugs have the capacity to bind with certain types of proteins that are carried in blood plasma. This is important as only drugs that are present in the plasma in their free form can be transported to the tissues. Drugs that are bound to plasma proteins therefore act as a reservoir of the drug within the organism and this binding reduces the drug's final concentration in the tissues. The binding between a drug and plasma protein is rarely specific and is usually labile and reversible. The binding generally

neg: Grazoprevir carrier proteins SLCO1B1 and SLCO1B3. Drugs that inhibit this proteins, such as rifampicin, ciclosporin, and a number of AIDS medications (atazanavir, darunavir, lopinavir, saquinavir, tipranavir, cobicistat), can cause a significant increase in grazoprevir blood plasma levels. The substance is degraded by the liver enzyme CYP3A4. Combination with drugs that induce this enzyme, such as efavirenz, carbamazepine or St. John's wort, can lead to ineffectively low plasma levels of grazoprevir. Combination with CYP3A4 inhibitors may increase plasma levels. Grazoprevir blocks NS3, a serine protease enzyme the virus needs for splitting its polyprotein into the functional virus proteins, and NS4A, a cofactor

neg: Cefadroxil skin and urinary tract. The following represents MIC susceptibility data for a few medically significant microorganisms. Cefadroxil is almost completely absorbed from the gastrointestinal tract. After doses of 500 mg and 1 g by mouth, peak plasma concentrations of about 16 and 30 micrograms/ml, respectively, are obtained after 1.5 to 2.0 hours. Although peak concentrations are similar to those of cefalexin, plasma concentrations are more sustained. Dosage with food does not appear to affect the absorption of cefadroxil. About 20% of cefadroxil is reported to be bound to plasma proteins. Its plasma half-life is about 1.5 hours and is prolonged

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: Cohn process Cohn process The Cohn process, developed by Edwin J. Cohn, is a series of purification steps with the purpose of extracting albumin from blood plasma. The process is based on the differential solubility of albumin and other plasma proteins based on pH, ethanol concentration, temperature, ionic strength, and protein concentration. Albumin has the highest solubility and lowest isoelectric point of all the major plasma proteins. This makes it the final product to be precipitated, or separated from its solution in a solid form. Albumin was an excellent substitute for human plasma in World War Two. When administered to wounded soldiers

neg: Fences and pickets model of plasma membrane structure the inner surface of the plasma membrane also exhibit confinement within actin-based compartments. The movement of phospholipids, even those located in the outer leaflet of the membrane, is regulated by the actin-based membrane skeleton meshwork. Which is surprising, because the membrane skeleton is located on the cytoplasmic surface of the plasma membrane, and cannot directly interact with the phospholipids located in the outer leaflet of the plasma membrane. To explain the hop diffusion of phospholipids, consistently with that of TM proteins, a model named “anchored TM-protein picket model” has been proposed. In this model various TM proteins are anchored to

neg: Fences and pickets model of plasma membrane structure Therefore, transmembrane proteins are corralled by both fences and pickets. In both models, membrane proteins and lipids can hop from a compartment to an adjacent one, probably when thermal fluctuations of the membrane and the membrane skeleton create a space between them large enough to allow the passage of integral membrane proteins, when an actin filament temporarily breaks, and/or when membrane molecules have sufficient kinetic energy to cross the barrier when they are in the boundary region. Fences and pickets model of plasma membrane structure The Fences and pickets model of plasma membrane is a concept of cell membrane structure

neg: Fresh frozen plasma including plasma frozen within 24 hours after phlebotomy, cryoprecipitate reduced plasma, and solvent detergent plasma. In the United States it refers to the fluid portion of one unit of human blood that has been centrifuged, separated, and frozen solid at or colder within eight hours of collection. The phrase "FFP" is often used to mean any transfused plasma product. The other commonly transfused plasma, PF24, has similar indications as those for FFP with the exception of heat-sensitive proteins in the plasma such as factor V. There are few specific indications for FFP. These generally are limited to the treatment of

neg: Chemotaxis a single flagellum that is kept inside the cell wall. These bacteria move by spinning the whole cell, which is shaped like a corkscrew. Chemical gradients are sensed through multiple transmembrane receptors, called methyl-accepting chemotaxis proteins (MCPs), which vary in the molecules that they detect. These receptors may bind attractants or repellents directly or indirectly through interaction with proteins of periplasmatic space. The signals from these receptors are transmitted across the plasma membrane into the cytosol, where "Che proteins" are activated. The Che proteins alter the tumbling frequency, and alter the receptors. The proteins CheW and CheA bind to the

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: Oncotic pressure high quantities of albumin, a protein that constitutes approximately 80% of the total oncotic pressure exerted by blood plasma on interstitial fluid. The total oncotic pressure of an average capillary is about 28 mmHg with albumin contributing approximately 22 mmHg of this oncotic pressure. Because blood proteins cannot escape through capillary endothelium, oncotic pressure of capillary beds tends to draw water into the vessels. It is necessary to understand the oncotic pressure as a balance; because the blood proteins reduce interior permeability, less plasma fluid can exit the vessel. Oncotic pressure is represented by the symbol Π or π in

neg: Neuroproteomics receptors, and molecule transporters. Along the plasma membrane, the proteins involved in creating cholesterol-rich lipid rafts are being studied because they have been shown to be crucial for glutamate uptake during the initial stages of neuron formation. As mentioned before, vesicle proteins are also being studied closely because they are involved in disease. Neuroproteomics Neuroproteomics is the study of the protein complexes and species that make up the nervous system. These proteins interact to make the neurons connect in such a way to create the intricacies that nervous system is known for. Neuroproteomics is a complex field that has a

neg: Dock2 context is known to require the formation of a complex between Dock180 and its cognate adaptor proteins, which assist its translocation to the plasma mambrane and binding to Rac. Similarly, Dock2 has been shown to form a complex with the well described DOCK-binding protein ELMO1 and this interaction is required for Dock2-mediated Rac activation in lymphocyte cell lines. ELMO proteins contain a C-terminal proline-rich region which binds to the N-terminal SH3 domain of DOCK proteins and mediates their recruitment to sites of high Rac availability (primarily the plasma membrane). ELMO proteins also contain a PH domain which appears to induce

neg: Endocytic cycle forward as it moves. • Evidence indicates that those molecules in the cell’s surface that act as the feet of the cell — the integrins, which attach the cell to the substratum — can also be endocytosed and transported through the cell. In this way, fresh adhesion sites (see cell adhesion) are provided at the cell’s front. • The flow of membrane from the front rearward is not a flow of average plasma membrane proteins: The membrane internalised is a subset of plasma membrane proteins, such as LDL or transferrin receptors and the lipid bilayer in which they sit. These

neg: Hemodynamics a non-Newtonian fluid, best studied using rheology rather than hydrodynamics. Blood vessels are not rigid tubes, so classic hydrodynamics and fluids mechanics based on the use of classical viscometers are not capable of explaining hemodynamics. The study of the blood flow is called hemodynamics. The study of the properties of the blood flow is called hemorheology. Blood is a complex liquid. Blood is composed of plasma and formed elements. The plasma contains 91.5% water, 7% proteins and 1.5% other solutes. The formed elements are platelets, white blood cells and red blood cells, the presence of these formed elements and their

neg: Hop diffusion Hop diffusion Hop diffusion - is a non-Brownian diffusion of proteins and lipid molecules within the plasma membrane. Hop diffusion occurs due to the discontinuity of the cell cytoplasmic membrane. According to the Fences and pickets model, plasma membrane is compartmentalized by actin-based membrane-skeleton “fences”, that occur when cytoplasmic domains collide with the actin-based membrane skeleton; and anchored-transmembrane protein “pickets”. Due to these obstacles membrane proteins undergo temporary confinement within 30–700- nm compartments with infrequent intercompartmental hops. Hops between adjacent compartments presumably occur due to: While simple Brownian diffusion is isotropic and homogeneous, hop diffusion is more complex and combines

neg: Desmosome and longer "b" form. The inner dense plaque, also about 15–20 nm in length, contains the C-terminus end of desmoplakin and their attachment to keratin intermediate filaments. Desmoplakin is the most abundant part of the desmosome, as it operates as the mediator between the cadherin proteins in the plasma membrane and the keratin filaments. Desmoplakin has two isoforms that differ in the length of their middle rod domain. All desmoplakins have an N-terminal head, a C-tail consisting of three plakin repeats, and a glycine-serine-arginine rich domain (GSR) at the C-end. Mutations within the desmosome are the main cause of arrhythmogenic

neg: Snake venom The first practical large-scale method of blood plasma fractionation was developed by Edwin J. Cohn during World War II. It is known as the Cohn process (or Cohn method). This process is also known as cold ethanol fractionation as it involves gradually increasing the concentration of ethanol in the solution at 5C and 3C. The Cohn Process exploits differences in properties of the various plasma proteins, specifically, the high solubility and low pI of albumin. As the ethanol concentration is increased in stages from 0% to 40% the [pH] is lowered from neutral (pH ~ 7) to about 4.8, which

neg: Hop diffusion free diffusion, which occurs inside cell membrane compartments, and infrequent intercompartmental transitions (hops). The complexity of this type of anomalous diffusion is further enhanced due to an inherent broad distribution of compartment sizes. Hop diffusion Hop diffusion - is a non-Brownian diffusion of proteins and lipid molecules within the plasma membrane. Hop diffusion occurs due to the discontinuity of the cell cytoplasmic membrane. According to the Fences and pickets model, plasma membrane is compartmentalized by actin-based membrane-skeleton “fences”, that occur when cytoplasmic domains collide with the actin-based membrane skeleton; and anchored-transmembrane protein “pickets”. Due to these obstacles membrane proteins undergo

neg: Plantibody Plantibody passive immunization is a medical strategy long employed to provide temporary protection against pathogens. Early implementations involved recovering ostensibly cell-free plasma from the blood of human survivors or from non-human animals deliberately exposed to a specific pathogen or toxin. These approaches resulted in crude purifications of plasma-soluble proteins including antibodies. Antibodies (also known as an immunoglobulins) are complex proteins produced by vertebrates that recognize antigens (or molecular patterns) on pathogens and some dangerous compounds in order to alert the Adaptive immune system that there are pathogens within the body. A plantibody is an antibody that is produced by plants

neg: Chlorpropamide with mild to moderate hepatic and renal impairment. Chlorpropamide is also used in partial central diabetes insipidus. Maximal plasma concentrations are reached 3 to 5 hours after quick and nearly complete (>90%) resorption from the gut. Plasma half life is 36 hours; the drug is effective for about 24 hours, longer than other sulfonylureas. A stable plasma level is only reached after three days of continuous application. 90% of the drug are bound to plasma proteins; at least two albumin binding sites exist. More than 99% of chlorpropamide are excreted unchanged via the kidneys. It is first filtrated in the

neg: Plasmapheresis in and of itself is useful to temper the disease process, while simultaneous medical and immunosuppressive therapy is required for long-term management. Plasma exchange offers the quickest short-term answer to removing harmful autoantibodies; however, the production of autoantibodies by the immune system must also be suppressed, usually by the use of medications such as prednisone, cyclophosphamide, cyclosporine, mycophenolate mofetil, rituximab, or a mixture of these. Other uses are the removal of blood proteins where these are overly abundant and cause hyperviscosity syndrome. Examples of diseases that can be treated with plasmapheresis: Though plasmapheresis is helpful in certain medical conditions, like

neg: Phosphatidylinositol (3,4,5)-trisphosphate Btk1, and ARNO. The generation of PtdIns(3,4,5)"P" at the plasma membrane upon the activation of class I PI 3-kinases causes these proteins to translocate to the plasma membrane and affects their activity accordingly. In many types of eukaryotic cells, the production of PtdIns(3,4,5)"P" and recruitment of PH domain proteins to the membrane results in localized actin polymerization, leading to cellular protrusions that are important for cell migration, division, and phagocytosis. The PH domain allows binding between PtdIns(3,4,5)"P" and G protein-coupled receptor kinases (GRKs). This enhances the binding of the GRK to the plasma membrane. Phosphatidylinositol (3,4,5)-trisphosphate Phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)"P"), abbreviated

neg: Biological membrane phospholipid bilayer, the outer leaflet and inner leaflet of the membrane are asymmetrical in their composition. Certain proteins and lipids rest only on one surface of the membrane and not the other. • Both the plasma membrane and internal membranes have cytosolic and exoplasmic faces • This orientation is maintained during membrane trafficking – proteins, lipids, glycoconjugates facing the lumen of the ER and Golgi get expressed on the extracellular side of the plasma membrane. In eucaryotic cells, new phospholipids are manufactured by enzymes bound to the part of the endoplasmic reticulum membrane that faces the cytosol. These enzymes, which

neg: Blood product the group is usually distinguished from volume expanders, which typically refer to artificially produced substances and are thereby within the scope of "blood substitutes". Blood product A blood product is any therapeutic substance prepared from human blood. This includes: whole blood; blood components; and plasma derivatives. Whole blood is not commonly used in transfusion medicine. Blood components include: red blood cell concentrates or suspensions; platelets produced from whole blood or via apheresis; plasma; and cryoprecipitate. Plasma derivatives are plasma proteins prepared under pharmaceutical manufacturing conditions, these include: albumin; coagulation factor concentrates; and immunoglobulins. Blood products may also be called blood-based

neg: FERM domain domain. The FERM domain has also been called the amino-terminal domain, the 30kDa domain, 4.1N30, the membrane-cytoskeletal-linking domain, the ERM-like domain, the ezrin-like domain of the band 4.1 superfamily, the conserved N-terminal region, and the membrane attachment domain. FERM domain containing proteins include: 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

neg: Endomembrane system that perform the functions of the plasma membrane. The plasma membrane is not a fixed or rigid structure, the molecules that compose the membrane are capable of lateral movement. This movement and the multiple components of the membrane are why it is referred to as a fluid mosaic. Smaller molecules such as carbon dioxide, water, and oxygen can pass through the plasma membrane freely by diffusion or osmosis. Larger molecules needed by the cell are assisted by proteins through active transport. The plasma membrane of a cell has multiple functions. These include transporting nutrients into the cell, allowing waste to

neg: Viral protein membrane called the viral envelope. In most cases, the viral envelope is obtained by the capsid from the host cell's plasma membrane when a virus leaves its host cell through a process called budding. The viral envelope is made up of a lipid bilayer embedded with viral proteins, including viral glycoproteins. These viral glycoproteins bind to specific receptors and coreceptors on the membrane of host cells, and they allow viruses to attach onto their target host cells. Some of these glycoproteins include: Viral glycoproteins play a critical role in virus-to-cell fusion. Virus-to-cell fusion is initiated when viral glycoproteins bind to

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: Blood product Blood product A blood product is any therapeutic substance prepared from human blood. This includes: whole blood; blood components; and plasma derivatives. Whole blood is not commonly used in transfusion medicine. Blood components include: red blood cell concentrates or suspensions; platelets produced from whole blood or via apheresis; plasma; and cryoprecipitate. Plasma derivatives are plasma proteins prepared under pharmaceutical manufacturing conditions, these include: albumin; coagulation factor concentrates; and immunoglobulins. Blood products may also be called blood-based products to differ from blood substitutes, which usually refer to artificially produced products. Also, although many blood products have the effect of volume expansion,

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: Phosphatidylinositol 3,4-bisphosphate PI 3-kinases and SHIP phosphatases causes these proteins to translocate to the plasma membrane, thereby affecting their activity. Phosphatidylinositol 3,4-bisphosphate Phosphatidylinositol (3,4)-bisphosphate (PtdIns(3,4)"P") is a minor phospholipid component of cell membranes, yet an important second messenger. The generation of PtdIns(3,4)"P" at the plasma membrane activates a number of important cell signaling pathways. PtdIns(3,4)"P" is dephophosphorylated by the phosphatase INPP4B on the 4 position of the inositol ring and by the TPTE (transmembrane phosphatases with tensin homology) family of phosphatases on the 3 position of the inositol ring. The PH domain in a number of proteins binds to PtdIns(3,4)"P" including the

neg: Ankyrin Ankyrin Ankyrins are a family of proteins that mediate the attachment of integral membrane proteins to the spectrin-actin based membrane cytoskeleton. Ankyrins have binding sites for the beta subunit of spectrin and at least 12 families of integral membrane proteins. This linkage is required to maintain the integrity of the plasma membranes and to anchor specific ion channels, ion exchangers and ion transporters in the plasma membrane. The name is derived from the Greek word for "fused". Ankyrins contain four functional domains: an N-terminal domain that contains 24 tandem ankyrin repeats, a central domain that binds to spectrin, a death

neg: Cytosol cells is extremely high, and approaches 200 mg/ml, occupying about 20-30% of the volume of the cytosol. However, measuring precisely how much protein is dissolved in cytosol in intact cells is difficult, since some proteins appear to be weakly associated with membranes or organelles in whole cells and are released into solution upon cell lysis. Indeed, in experiments where the plasma membrane of cells were carefully disrupted using saponin, without damaging the other cell membranes, only about one quarter of cell protein was released. These cells were also able to synthesize proteins if given ATP and amino acids, implying that

neg: Fences and pickets model of plasma membrane structure meshwork is directly situated on the cytoplasmic surface of the plasma membrane. Membrane skeleton fence, or membrane skeleton corralling model, suggests that this meshwork is likely to partition the plasma membrane into many small compartments with regard to the lateral diffusion of membrane molecules. Cytoplasmic domains collide with the actin-based membrane skeleton which induces temporary confinement or corralling of transmembrane (TM) proteins in the membrane skeleton mesh. TM proteins are capable to hop between adjacent compartments when the distance between the meshwork and the membrane becomes large enough, or when the meshwork temporarily and locally dissociates. Cytoplasmic molecules located on