1.
Enzyme inhibitor
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An enzyme inhibitor is a molecule that binds to an enzyme and decreases its activity. Since blocking an enzymes activity can kill a pathogen or correct a metabolic imbalance and they are also used in pesticides. The binding of an inhibitor can stop a substrate from entering the active site and/or hinder the enzyme from catalyzing its reaction. Inhibitor binding is reversible or irreversible. Irreversible inhibitors usually react with the enzyme and change it chemically and these inhibitors modify key amino acid residues needed for enzymatic activity. In contrast, reversible inhibitors bind non-covalently and different types of inhibition are produced depending on whether these inhibitors bind to the enzyme, many drug molecules are enzyme inhibitors, so their discovery and improvement is an active area of research in biochemistry and pharmacology. A medicinal enzyme inhibitor is often judged by its specificity and its potency, a high specificity and potency ensure that a drug will have few side effects and thus low toxicity. Enzyme inhibitors also occur naturally and are involved in the regulation of metabolism, for example, enzymes in a metabolic pathway can be inhibited by downstream products. This type of negative feedback slows the production line when products begin to build up and is an important way to maintain homeostasis in a cell, other cellular enzyme inhibitors are proteins that specifically bind to and inhibit an enzyme target. This can help control enzymes that may be damaging to a cell, a well-characterised example of this is the ribonuclease inhibitor, which binds to ribonucleases in one of the tightest known protein–protein interactions. Natural enzyme inhibitors can also be poisons and are used as defences against predators or as ways of killing prey, reversible inhibitors attach to enzymes with non-covalent interactions such as hydrogen bonds, hydrophobic interactions and ionic bonds. Multiple weak bonds between the inhibitor and the active site combine to produce strong and specific binding, in contrast to substrates and irreversible inhibitors, reversible inhibitors generally do not undergo chemical reactions when bound to the enzyme and can be easily removed by dilution or dialysis. There are four kinds of reversible enzyme inhibitors and they are classified according to the effect of varying the concentration of the enzymes substrate on the inhibitor. In competitive inhibition, the substrate and inhibitor cannot bind to the enzyme at the same time, as shown in the figure on the right. This usually results from the inhibitor having an affinity for the site of an enzyme where the substrate also binds. This type of inhibition can be overcome by high concentrations of substrate. However, the apparent Km will increase as it takes a higher concentration of the substrate to reach the Km point, competitive inhibitors are often similar in structure to the real substrate. In uncompetitive inhibition, the inhibitor binds only to the substrate-enzyme complex and this type of inhibition causes Vmax to decrease and Km to decrease
2.
Gamma-Linolenic acid
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Gamma-linolenic acid or GLA, is a fatty acid found primarily in vegetable oils. When acting on GLA, 5-lipoxygenase produces no leukotrienes and the conversion by the enzyme of arachidonic acid to leukotrienes is inhibited, GLA is categorized as an n−6 fatty acid, meaning that the first double bond on the methyl end is the sixth bond. In physiological literature, GLA is designated as 18,3, GLA is a carboxylic acid with an 18-carbon chain and three cis double bonds. It is an isomer of α-linolenic acid, which is a polyunsaturated n−3 fatty acid, found in rapeseed oil, soy beans, walnuts, flax seed, perilla, chia. GLA was first isolated from the oil of evening primrose. This herbal plant was grown by Native Americans to treat swelling in the body, in the 17th century, it was introduced to Europe and became a popular folk remedy, earning the name kings cure-all. In 1919, Heiduschka and Lüft extracted the oil from evening primrose seeds and described an unusual linolenic acid, later, the exact chemical structure was characterized by Riley. Although there are α- and γ- forms of acid, there is no β- form. One was once identified, but it turned out to be an artifact of the analytical process. GLA is obtained from vegetable oils such as evening primrose oil, blackcurrant seed oil, borage seed oil, GLA is also found in varying amounts in edible hemp seeds, oats, barley, and spirulina. Normal safflower oil does not contain GLA, but a genetically modified GLA safflower oil available in commercial quantities since 2011 contains 40% GLA, borage oil contains 20% GLA, evening primrose oil ranges from 8% to 10% GLA, and black-currant oil contains 15-20%. The human body produces GLA from linoleic acid and this reaction is catalyzed by Δ6-desaturase, an enzyme that allows the creation of a double bond on the sixth carbon counting from the carboxyl terminus. LA is consumed sufficiently in most diets, from such abundant sources as cooking oils, however, a lack of GLA can occur when there is a reduction of the efficiency of the D6D conversion or in disease states wherein there is excessive consumption of GLA metabolites. From GLA, the body forms dihomo-γ-linolenic acid and this is one of the bodys three sources of eicosanoids DGLA is the precursor of the prostaglandin PGH1, which in turn forms PGE1 and the thromboxane TXA1. PGE1 has a role in regulation of immune function and is used as the medicine alprostadil. Unlike AA and EPA, DGLA cannot yield leukotrienes, however, it can inhibit the formation of pro-inflammatory leukotrienes from AA. Although GLA is an n−6 fatty acid, a type of acid that is, in general, pro-inflammatory, in 2002 the UKs Medicines and Healthcare products Regulatory Agency withdrew marketing authorisations for evening primrose oil as an eczema remedy. Another single source suggests that Evening Primrose Oil with adjuvant vitamin E, may reduce breast pain
3.
Enzyme
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Enzymes /ˈɛnzaɪmz/ are macromolecular biological catalysts. Enzymes accelerate, or catalyze, chemical reactions, the molecules at the beginning of the process upon which enzymes may act are called substrates and the enzyme converts these into different molecules, called products. Almost all metabolic processes in the cell need enzymes in order to occur at rates fast enough to sustain life, the set of enzymes made in a cell determines which metabolic pathways occur in that cell. The study of enzymes is called enzymology, enzymes are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules, enzymes specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the rate of a reaction by lowering its activation energy, some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5-phosphate decarboxylase, which allows a reaction that would take millions of years to occur in milliseconds. Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules, inhibitors are molecules that decrease enzyme activity, many drugs and poisons are enzyme inhibitors. An enzymes activity decreases markedly outside its optimal temperature and pH, some enzymes are used commercially, for example, in the synthesis of antibiotics. French chemist Anselme Payen was the first to discover an enzyme, diastase and he wrote that alcoholic fermentation is an act correlated with the life and organization of the yeast cells, not with the death or putrefaction of the cells. In 1877, German physiologist Wilhelm Kühne first used the term enzyme, the word enzyme was used later to refer to nonliving substances such as pepsin, and the word ferment was used to refer to chemical activity produced by living organisms. Eduard Buchner submitted his first paper on the study of yeast extracts in 1897, in a series of experiments at the University of Berlin, he found that sugar was fermented by yeast extracts even when there were no living yeast cells in the mixture. He named the enzyme that brought about the fermentation of sucrose zymase, in 1907, he received the Nobel Prize in Chemistry for his discovery of cell-free fermentation. Following Buchners example, enzymes are usually named according to the reaction they carry out, the biochemical identity of enzymes was still unknown in the early 1900s. Sumner showed that the enzyme urease was a protein and crystallized it. These three scientists were awarded the 1946 Nobel Prize in Chemistry, the discovery that enzymes could be crystallized eventually allowed their structures to be solved by x-ray crystallography. This high-resolution structure of lysozyme marked the beginning of the field of structural biology, an enzymes name is often derived from its substrate or the chemical reaction it catalyzes, with the word ending in -ase
4.
Curcumin
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Curcumin is a bright yellow chemical produced by some plants. It is the principal curcuminoid of turmeric, a member of the ginger family and it is sold as an herbal supplement, cosmetics ingredient, food flavoring, and food coloring. As a food additive, its E number is E100 and it was isolated in 1815 when Vogel and Pelletier reported the isolation of a yellow coloring-matter from the rhizomes of turmeric and named it curcumin. Although curcumin has been used historically in Ayurvedic medicine, its potential for medicinal properties remains unproven and is doubted as a therapy when used orally, chemically, curcumin is a diarylheptanoid, belonging to the group of curcuminoids, which are natural phenols responsible for turmerics yellow color. It is a tautomeric compound existing in enolic form in organic solvents, the most common applications are as a dietary supplement, in cosmetics, as a food coloring, and as flavoring for foods such as turmeric-flavored beverages. Annual sales of curcumin have increased since 2012, largely due to an increase in its popularity as a dietary supplement and it is increasingly popular in skin care products that are marketed as containing natural ingredients or dyes, especially in Asia. The largest market is in North America, where sales exceeded US$20 million in 2014, curcumin incorporates several functional groups whose structure was first identified in 1910. The aromatic ring systems, which are phenols, are connected by two α, β-unsaturated carbonyl groups, the diketones form stable enols and are readily deprotonated to form enolates, the α, β-unsaturated carbonyl group is a good Michael acceptor and undergoes nucleophilic addition. Curcumin is used as an indicator for boron and it reacts with boric acid to form a red-color compound, rosocyanine. The biosynthetic route of curcumin is uncertain, in 1973, Roughly and Whiting proposed two mechanisms for curcumin biosynthesis. The first mechanism involves a chain reaction by cinnamic acid and 5 malonyl-CoA molecules that eventually arylized into a curcuminoid. The second mechanism involves two cinnamate units coupled together by malonyl-CoA, both use cinnamic acid as their starting point, which is derived from the amino acid phenylalanine. Plant biosyntheses starting with cinnamic acid is rare compared to the more common p-coumaric acid, only a few identified compounds, such as anigorufone and pinosylvin, build from cinnamic acid. In vitro, curcumin exhibits numerous interference properties which may lead to misinterpretation of results, although curcumin has been assessed in numerous laboratory and clinical studies, it has no medical uses established by well-designed clinical research. Cancer studies using curcumin conducted by Bharat Aggarwal, formerly a researcher at the MD Anderson Cancer Center, were deemed fraudulent, curcumin, which shows positive results in most drug discovery assays, may be a false lead that medicinal chemists refer to as pan-assay interference compounds. In vitro, curcumin has been shown to inhibit certain enzymes, transcriptional co-activator proteins. Two preliminary clinical studies in cancer patients consuming high doses of curcumin showed no toxicity, curcumin appears to reduce circulating C-reactive protein in human subjects, although no dose-response relationship was established. Turmeric and curcumin, from Memorial Sloan-Kettering Cancer Center Turmeric, from the University of Maryland Medical Center
5.
Cell signaling
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Cell signaling is part of any communication process that governs basic activities of cells and coordinates all cell actions. The ability of cells to perceive and correctly respond to their microenvironment is the basis of development, tissue repair, errors in signaling interactions and cellular information processing are responsible for diseases such as cancer, autoimmunity, and diabetes. By understanding cell signaling, diseases may be treated effectively and, theoretically. Traditional work in biology has focused on studying individual parts of cell signaling pathways, systems biology research helps us to understand the underlying structure of cell signaling networks and how changes in these networks may affect the transmission and flow of information. Such networks are complex systems in their organization and may exhibit a number of emergent properties including bistability and ultrasensitivity, analysis of cell signaling networks requires a combination of experimental and theoretical approaches including the development and analysis of simulations and modeling. Long-range allostery is often a significant component of signaling events. Cell signaling has been most extensively studied in the context of human diseases, however, cell signaling may also occur between the cells of two different organisms. In many mammals, early embryo cells exchange signals with cells of the uterus, in the human gastrointestinal tract, bacteria exchange signals with each other and with human epithelial and immune system cells. For the yeast Saccharomyces cerevisiae during mating, some cells send a signal into their environment. The mating factor peptide may bind to a surface receptor on other yeast cells. Cell signaling can be classified to be mechanical and biochemical based on the type of the signal, mechanical signals are the forces exerted on the cell and the forces produced by the cell. These forces can both be sensed and responded by the cells, biochemical signals are the biochemical molecules such as proteins, lipids, ions and gases. These signals can be categorized based on the distance between signaling and responder cells, Signaling within, between, and amongst cells is subdivided into the following classifications, Intracrine signals are produced by the target cell that stay within the target cell. Autocrine signals are produced by the cell, are secreted. Sometimes autocrine cells can target cells close by if they are the type of cell as the emitting cell. An example of this are immune cells and these signals are transmitted along cell membranes via protein or lipid components integral to the membrane and are capable of affecting either the emitting cell or cells immediately adjacent. Paracrine signals target cells in the vicinity of the emitting cell, endocrine cells produce hormones that travel through the blood to reach all parts of the body. Cells communicate with each other via direct contact, over short distances, some cell–cell communication requires direct cell–cell contact
6.
Diglyceride
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A diglyceride, or diacylglycerol, is a glyceride consisting of two fatty acid chains covalently bonded to a glycerol molecule through ester linkages. Two possible forms exist,1, 2-diacylglycerols and 1, 3-diacylglycerols, dAGs can acts as surfactants and are commonly used as emulsifiers in processed foods. Diglycerides are a component of many seed oils and are normally present at ~1-6%. Industrial production is achieved by a glycerolysis reaction between triglycerides and glycerol, the raw materials this may be either vegetable or animal fats. Diglycerides, generally in a mix with monoglycerides, are common food additives used as emulsifiers. The values given in the labels for total fat, saturated fat. They often are included in products, beverages, ice cream, peanut butter, chewing gum, shortening, whipped toppings, margarine, confections. Although inositol trisphosphate diffuses into the cytosol, diacylglycerol remains within the plasma membrane, iP3 stimulates the release of calcium ions from the smooth endoplasmic reticulum, whereas DAG is a physiological activator of protein kinase C. The production of DAG in the membrane translocation of PKC from the cytosol to the plasma membrane. Munc13 Activation, Diacylglycerol has been shown to some of its excitatory actions on vesicle release through interactions with the presynaptic priming protein family Munc13. Binding of DAG to the C1 domain of Munc13 increases the fusion competence of synaptic vesicles resulting in potentiated release, Diacylglycerol can be mimicked by the tumor-promoting compounds phorbol esters. Synthesis of diacylglycerol begins with glycerol-3-phosphate, which is derived primarily from dihydroxyacetone phosphate, glycerol-3-phosphate is first acylated with acyl-coenzyme A to form lysophosphatidic acid, which is then acylated with another molecule of acyl-CoA to yield phosphatidic acid. Phosphatidic acid is then de-phosphorylated to form diacylglycerol, dietary fat is mainly composed of triglycerides. Because triglycerides cannot be absorbed by the system, triglycerides must first be enzymatically digested into monoacylglycerol, diacylglycerol. Diacylglycerol is a precursor to triacylglycerol, which is formed in the addition of a fatty acid to the diacylglycerol under the catalysis of diglyceride acyltransferase. Since diacylglycerol is synthesized via phosphatidic acid, it will contain a saturated fatty acid at the C-1 position on the glycerol moiety. Diacylglycerol can be phosphorylated to phosphatidic acid by diacylglycerol kinase, Activation of PKC-θ by diacylglycerol may cause insulin resistance in muscle by decreasing IRS1-associated PI3K activity. Similarly, activation of PKCε by diacyglycerol may cause resistance in the liver
7.
Ubenimex
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Ubenimex, also known more commonly as bestatin, is a competitive, reversible protease inhibitor. It is an inhibitor of arginyl aminopeptidase, leukotriene A4 hydrolase, alanyl aminopeptidase, leucyl/cystinyl aminopeptidase and it is being studied for use in the treatment of acute myelocytic leukemia. It is derived from Streptomyces olivoreticuli, ubenimex has been found to inhibit the enzymatic degradation of oxytocin, vasopressin, enkephalins, and various other peptides and compounds. Amastatin Pepstatin The MEROPS online database for peptidases and their inhibitors, Bestatin
8.
ALOX15
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ALOX15 is, like other lipoxygenases, a seminal enzyme in the metabolism of polyunsaturated fatty acids to a wide range of physiologically and pathologically important products. In humans, it is encoded by the ALOX15 gene located on chromosome 17p13.3 and this 11 kilobase pair gene consists of 14 exons and 13 introns coding for a 75 kiloDalton protein composed of 662 amino acids. 15-LO is to be distinguished from another human 15-lipoxygenase enzyme, ALOX15B, orthologs of ALOX15, termed Alox15, are widely distributed in animal and plant species but commonly have different enzyme activities and make somewhat different products than ALOX15. Many of the latter Alox15 enzymes nonetheless possess predominantly or exclusively 12-lipoxygenase rather than 15-lipoxygenase activity, ALOX15 and Alox15 enzymes are non-heme, iron-containing dioxygenases. Rodent Alox15 enzymes, in contrast, produce almost exclusively ω-9 peroxy intermediates, concurrently, ALOX15 and rodent Alox15 enzymes rearrange the carbon-carbon double bonds to bring them into the 1S-hydroxy-2E, 4Z-diene configuration. ALOX15 and Alox15 enzymes act with a degree of Stereospecificity to form products that position the hydroperoxy residue in the S stereoisomer configuration. Eoxins stimulate vascular permeability in an ex vivo human vascular endothelial model system, the PUFA epoxide of arachidonic acid made by ALOX15 may also be conjugated with glutathione to form eoxin A4 which product can be further metabolized to eoxin B4, eoxin C4, and eoxin D4. The human enzyme is active on linoleic acid, preferring it over arachidonic acid it is less active on PUFA that are esters within the cited lipids. Arachidonic acid has double bonds between carbons 5-6, 8-9, 11-12, and 14-15, these bounds are in the cis and its 5-ketone analog. The minor products of ALOX15, 12--HpETE and 12-HETE, possess a range of activities. 12-Oxo-ETE, which along with 12S-HETE, activates the Leukotriene B4 receptor, Leukotriene B4 receptor 2 and this allows the possibility that 12-oxo-ETE contributes to the pro-inflammatory and other activities that BLT2 regulates. Human neutrophils, presumably using their ALOX15, metabolize Dihomo-γ-linolenic acid to 15S-hydroperoxy-8Z, 11Z, 13E-eicosatrienoic acid and 15S-hydroxy-8Z, 11Z and these mice also show an accelerated rate of progression of atherosclerosis whereas mice made to overexpress 12/15-lipoxygenase exhibit a delayed rate of atherosclerosis development. Alox15 overexpressing rabbits exhibited reduced tissue destruction and bone loss in a model of periodontitis, finally, Control mice, but not 12/15-lipoxygense deficient mice responded to eicospentaenoic acid administration by decreasing the number of lesions in a model of endometriosis. These synthetic analogs may prove to be useful for treating the cited human inflammatory diseases. In colorectal, breast, and kidney cancers, 15-LOX-1 levels are low or absent compared to the normal tissue counterparts and/or these levels sharply decline as the cancers progress. These results, as well as a 15-LOX-1 transgene study on colon cancer in mice suggests but do not prove that 15-LOX-1 is a tumor suppressor
9.
Caffeic acid
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Caffeic acid is an organic compound that is classified as a hydroxycinnamic acid. This yellow solid consists of both phenolic and acrylic functional groups and it is found in all plants because it is a key intermediate in the biosynthesis of lignin, one of the principal components of plant biomass and its residues. Caffeic acid can be found in the bark of Eucalyptus globulus and it can also be found in the freshwater fern Salvinia molesta or in the mushroom Phellinus linteus. Caffeic acid is found at a very modest level in coffee and it is one of the main natural phenols in argan oil. It is at a high level in black chokeberry and in fairly high level in lingonberry. It is also high in the South American herb yerba mate. It is also found in grain, and in rye grain. Caffeic acid, which is unrelated to caffeine, is biosynthesized by hydroxylation of coumaroyl ester of quinic acid and this hydroxylation produces the caffeic acid ester of shikimic acid, which converts to chlorogenic acid. It is the precursor to acid, coniferyl alcohol, and sinapyl alcohol. The transformation to ferulic acid is catalyzed by the enzyme caffeate O-methyltransferase, caffeic acid and its derivative caffeic acid phenethyl ester are produced in many kinds of plants. Dihydroxyphenylalanine ammonia-lyase was presumed to use 3, 4-dihydroxy-L-phenylalanine to produce trans-caffeate, however, the EC number for this purported enzyme was deleted in 2007, as no evidence has emerged for its existence. Caffeate O-methyltransferase is a responsible for the transformation of caffeic acid into ferulic acid. Caffeic acid and related o-diphenols are rapidly oxidized by o-diphenol oxidases in tissue extracts, caffeate 3, 4-dioxygenase is an enzyme that uses caffeic acid and oxygen to produce 3--cis, cis-muconate. 3-O-caffeoylshikimic acid and its isomers, are enzymic browning substrates found in dates, caffeic acid is an antioxidant in vitro and also in vivo. Caffeic acid also shows immunomodulatory and anti-inflammatory activity, caffeic acid outperformed the other antioxidants, reducing aflatoxin production by more than 95 percent. The studies are the first to show that stress that would otherwise trigger or enhance Aspergillus flavus aflatoxin production can be stymied by caffeic acid. This opens the door to use as a natural fungicide by supplementing trees with antioxidants, studies of the carcinogenicity of caffeic acid have mixed results. Some studies have shown that it inhibits carcinogenesis, and other experiments show carcinogenic effects, oral administration of high doses of caffeic acid in rats has caused stomach papillomas
10.
Ligand (biochemistry)
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In biochemistry and pharmacology, a ligand is a substance that forms a complex with a biomolecule to serve a biological purpose. In protein-ligand binding, the ligand is usually a molecule which produces a signal by binding to a site on a target protein, the binding typically results in a change of conformation of the target protein. In DNA-ligand binding studies, the ligand can be a molecule, ion. The relationship between ligand and binding partner is a function of charge, hydrophobicity, and molecular structure, the instance of binding occurs over an infinitesimal range of time and space, so the rate constant is usually a very small number. Binding occurs by intermolecular forces, such as bonds, hydrogen bonds. The association of docking is actually reversible through dissociation, measurably irreversible covalent bonding between a ligand and target molecule is atypical in biological systems. In contrast to the definition of ligand in metalorganic and inorganic chemistry, in biochemistry it is whether the ligand generally binds at a metal site. In general, the interpretation of ligand is contextual with regards to what sort of binding has been observed, the etymology stems from ligare, which means to bind. Ligand binding to a receptor protein alters the chemical conformation by affecting the shape orientation. The conformation of a receptor protein composes the functional state, ligands include substrates, inhibitors, activators, and neurotransmitters. The rate of binding is called affinity, and this measurement typifies a tendency or strength of the effect, binding affinity is actualized not only by host-guest interactions, but also by solvent effects that can play a dominant, steric role which drives non-covalent binding in solution. The solvent provides an environment for the ligand and receptor to adapt. Radioligands are radioisotope labeled compounds are used in vivo as tracers in PET studies, the interaction of most ligands with their binding sites can be characterized in terms of a binding affinity. In general, high-affinity binding results in a degree of occupancy for the ligand at its receptor binding site than is the case for low-affinity binding. A ligand that can bind to a receptor, alter the function of the receptor, high-affinity ligand binding implies that a relatively low concentration of a ligand is adequate to maximally occupy a ligand-binding site and trigger a physiological response. The lower the Ki concentration is, the more likely there will be a reaction between the pending ion and the receptive antigen. In the example shown to the right, two different ligands bind to the receptor binding site. Only one of the agonists shown can maximally stimulate the receptor and, thus, an agonist that can only partially activate the physiological response is called a partial agonist
11.
Linoleic acid
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Linoleic acid is a polyunsaturated omega-6 fatty acid. It is a liquid at room temperature. In physiological literature, it has a number of 18,2 cis. Linoleic acid is an acid with an 18-carbon chain and two cis double bonds, with the first double bond located at the sixth carbon from the methyl end. Linoleic acid belongs to one of the two families of essential fatty acids, which means that the body cannot synthesize it from other food components. The word linoleic derived from the Greek word linon, oleic means of, relating to, or derived from oil of olive or of or relating to oleic acid because saturating the omega-6 double bond produces oleic acid. LA is a fatty acid used in the biosynthesis of arachidonic acid and thus some prostaglandins, leukotrienes. It is found in the lipids of cell membranes and it is abundant in many nuts, fatty seeds and their derived vegetable oils, comprising over half of poppy seed, safflower, sunflower, corn, and soybean oils. LA is converted by various lipoxygenases, cyclooxygenases, certain cytochrome P450 enzymes, certain cytochrome P450 enzymes, the CYP epoxygenases, metabolize LA to epoxide products viz. its 12, 13-epoxide, Vernolic acid and its 9, 10-epoxide, Coronaric acid. All of these LA products have bioactivity and are implicated in human physiology and pathology as indicated in the cited linkages, linoleic acid is an essential fatty acid that must be consumed for proper health. A diet only deficient in linoleate causes mild skin scaling, hair loss, along with oleic acid, linoleic acid is released by cockroaches upon death which has the effect of preventing other roaches from entering the area. This is similar to the found in ants and bees. The first step in the metabolism of LA is performed by Δ6desaturase, there is evidence suggesting that infants lack Δ6desaturase of their own, and must acquire it through breast milk. Studies show that breast-milk fed babies have higher concentrations of GLA than formula-fed babies, GLA is converted to dihomo-gamma-linolenic acid, which in turn is converted to arachidonic acid. The three types of eicosanoids are prostaglandins, thromboxanes, and leukotrienes, eicosanoids produced from AA tend to promote inflammation and promote growth during and after physical activity in healthy humans. For example, both AA-derived thrombaxane and leukotrieneB4 are proaggregatory and vasoconstrictive eicosanoids during inflammation, there are some suggested negative health effects related to this inflammation promoting function of linoleic acid as an omega-6 fatty acid. Linoleic acid is used in making quick-drying oils, which are useful in oil paints and these applications exploit the easy reaction of the linoleic acid with oxygen in air, which leads to crosslinking and formation of a stable film called linoxyn. Reduction of linoleic acid yields linoleyl alcohol, linoleic acid is a surfactant with a critical micelle concentration of 1.5 x 10−4 M @ pH7.5
