Phospholipase A1 Mechanism
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Phospholipase A1 Mechanism
A phospholipase is an enzyme that hydrolyzes phospholipids into fatty acids and other lipophilic substances. There are four major classes, termed A, B, C, and D, which are distinguished by the type of reaction which they catalyze: *Phospholipase A ** Phospholipase A1 – cleaves the ''sn''-1 acyl chain (where ''sn'' refers to stereospecific numbering). ** Phospholipase A2 – cleaves the ''sn''-2 acyl chain, releasing arachidonic acid. *Phospholipase B – cleaves both ''sn''-1 and ''sn''-2 acyl chains; this enzyme is also known as a lysophospholipase. *Phospholipase C – cleaves before the phosphate, releasing diacylglycerol and a phosphate-containing head group. PLCs play a central role in signal transduction, releasing the second messenger inositol triphosphate. *Phospholipase D – cleaves after the phosphate, releasing phosphatidic acid and an alcohol. Types C and D are considered phosphodiesterases. Endothelial lipase is primarily a phospholipase. Phospholipase A2 a ...
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Inositol Triphosphate
Inositol trisphosphate or inositol 1,4,5-trisphosphate abbreviated InsP3 or Ins3P or IP3 is an inositol phosphate signaling molecule. It is made by hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2), a phospholipid that is located in the plasma membrane, by phospholipase C (PLC). Together with diacylglycerol (DAG), IP3 is a second messenger molecule used in signal transduction in biological cells. While DAG stays inside the membrane, IP3 is soluble and diffuses through the cell, where it binds to its receptor, which is a calcium channel located in the endoplasmic reticulum. When IP3 binds its receptor, calcium is released into the cytosol, thereby activating various calcium regulated intracellular signals. Properties Chemical formula and molecular weight IP3 is an organic molecule with a molecular mass of 420.10 g/mol. Its empirical formula is C6H15O15P3. It is composed of an inositol ring with three phosphate groups bound at the 1, 4, and 5 carbon positions, and three ...
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Peripheral Membrane Proteins
Peripheral membrane proteins, or extrinsic membrane proteins, are membrane proteins that adhere only temporarily to the biological membrane with which they are associated. These proteins attach to integral membrane proteins, or penetrate the peripheral regions of the lipid bilayer. The regulatory protein subunits of many ion channels and transmembrane receptors, for example, may be defined as peripheral membrane proteins. In contrast to integral membrane proteins, peripheral membrane proteins tend to collect in the water-soluble component, or fraction, of all the proteins extracted during a protein purification procedure. Proteins with GPI anchors are an exception to this rule and can have purification properties similar to those of integral membrane proteins. The reversible attachment of proteins to biological membranes has shown to regulate cell signaling and many other important cellular events, through a variety of mechanisms. For example, the close association between many en ...
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Infantile Neuroaxonal Dystrophy
Infantile neuroaxonal dystrophy (INAD) is a rare pervasive developmental disorder that primarily affects the nervous system. Individuals with infantile neuroaxonal dystrophy typically do not have any symptoms at birth, but between the ages of about 6 and 18 months they begin to experience delays in acquiring new motor and intellectual skills, such as crawling or beginning to speak. Eventually, they lose previously acquired skills. Presentation Cause This condition is inherited in an autosomal recessive pattern, which means two copies of the gene (''PLA2G6'') in each cell are altered. Most often, the parents of an individual with an autosomal recessive disorder each carry one copy of the altered gene but do not show signs and symptoms of the disorder. Pathophysiology Mutations in the '' PLA2G6'' gene have been identified in most individuals with infantile neuroaxonal dystrophy. The ''PLA2G6'' gene provides instructions for making an enzyme called an A2 phospholipase. This enz ...
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Patatin-like Phospholipase
Family of patatin-like phospholipases consists of various patatin glycoproteins from the total soluble protein from potato tubers, and also some proteins found in vertebrates. Patatin is a storage protein but it also has the enzymatic activity of phospholipase, catalysing the cleavage of fatty acids from membrane lipids. Subfamilies *Protein of unknown function UPF0028 Human proteins containing this domain PNPLA1; PNPLA2; PNPLA3; PNPLA4; PNPLA5; PNPLA6; PNPLA7; PNPLA8 Calcium-independent phospholipase A2-gamma is an enzyme that in humans is encoded by the ''PNPLA8'' gene In biology, the word gene has two meanings. The Mendelian gene is a basic unit of heredity. The molecular gene is a sequence of nucleot ...; References {{InterPro content, IPR002641 Protein domains Protein families Single-pass transmembrane proteins Hydrolases ...
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Viperidae
Vipers are snakes in the family Viperidae, found in most parts of the world, except for Antarctica, Australia, Hawaii, Madagascar, New Zealand, Ireland, and various other isolated islands. They are venomous snake, venomous and have long (relative to non-vipers), hinged fangs that permit deep envenomation of their prey. Three subfamilies are currently recognized. They are also known as viperids. The name "viper" is derived from the Latin word ''vipera'', -''ae'', also meaning viper, possibly from ''vivus'' ("living") and ''parere'' ("to beget"), referring to the trait viviparity (giving live birth) common in vipers like most of the species of Boidae. The earliest known vipers are believed to have diverged from the rest of the clade Caenophidia in the early Eocene. Description All viperids have a pair of relatively long Solenoglypha#Solenoglyph, solenoglyphous (hollow) fangs that are used to inject venom from glands located towards the rear of the upper jaws, just behind the ey ...
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Blennies
Blennies (from the Greek and , mucus, slime) are a diverse clade of ray-finned fish in the suborder Blennioidei of the percomorph order Blenniiformes. They inhabit marine, brackish, and occasionally freshwater habitats, and generally share similar morphology and behaviour. About 151 genera and nearly 900 species have been described within the order. Taxonomy The order was formerly classified as a suborder of the Perciformes. However, the 5th Edition of ''Fishes of the World'' divided the Perciformes into a number of new orders and the Blenniiformes were placed in the percomorph clade Ovalentaria alongside the such taxa as Cichliformes, Mugiliformes and Gobiesociformes. ''Eschmeyer's Catalog of Fishes'' added many more taxa, including the damselfishes and clingfishes, into the Blenniiformes, so the "true blennies" were redefined as the suborder Blennioidei. The six "true blenny" families are: * Blenniidae Rafinesque, 1810 - combtooth blennies, including the sabre-to ...
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Lysolecithin
Lysophosphatidylcholines (LPC, lysoPC), also called lysolecithins, are a class of chemical compounds which are derived from phosphatidylcholines. Overview Lysophosphatidylcholines are produced within cells mainly by the enzyme phospholipase A2, which removes one of the fatty acid groups from phosphatidylcholine to produce LPC. Among other properties, they activate endothelial cells during early atherosclerosis. LPC also acts as a find-me signal, released by apoptotic cells to recruit phagocytes, which then phagocytose the apoptotic cells. Moreover, LPCs can be used in the lab to cause demyelination of brain slices and to mimic the effects of demyelinating diseases such as multiple sclerosis. LPCs are also known to stimulate phagocytosis of the myelin sheath and can change the surface properties of erythrocytes. LPC-induced demyelination is thought to occur through the actions of recruited macrophages and microglia which phagocytose nearby myelin. Invading T cells are also th ...
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Histology And Histopathology
''Histology and Histopathology'' is a monthly peer-reviewed medical journal publishing original and review articles in the fields of histology and histopathology. It was established in 1986 and is published by the University of Murcia in Spain. The editors-in-chief are Francisco Hernández and Juan F. Madrid (University of Murcia). According to the ''Journal Citation Reports'', the journal has a 2016 impact factor The impact factor (IF) or journal impact factor (JIF) of an academic journal is a type of journal ranking. Journals with higher impact factor values are considered more prestigious or important within their field. The Impact Factor of a journa ... of 2.025. References External links * Histopathology Pathology journals Anatomy journals Academic journals established in 1986 Quarterly journals University of Murcia English-language journals {{Medical-journal-stub ...
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Endothelial Lipase
Endothelial lipase (LIPG) is a form of lipase secreted by vascular endothelial cells in tissues with high metabolic rates and vascularization, such as the liver, lung, kidney, and thyroid gland. The LIPG enzyme is a vital component to many biological processes. These processes include lipoprotein metabolism, cytokine expression, and lipid composition in cells. Unlike the lipases that hydrolyze Triglycerides, endothelial lipase primarily hydrolyzes phospholipids. Due to the hydrolysis specificity, endothelial lipase contributes to multiple vital systems within the body. On the contrary to the beneficial roles that LIPG plays within the body, endothelial lipase is thought to play a potential role in cancer and inflammation. Knowledge obtained in vitro and in vivo suggest the relations to these conditions, but human interaction knowledge lacks due to the recent discovery of endothelial lipase. Endothelial lipase was first characterized in 1999. The two independent research groups which ...
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Phosphodiesterase
A phosphodiesterase (PDE) is an enzyme that breaks a phosphodiester bond. Usually, ''phosphodiesterase'' refers to cyclic nucleotide phosphodiesterases, which have great clinical significance and are described below. However, there are many other families of phosphodiesterases, including phospholipases C and D, autotaxin, sphingomyelin phosphodiesterase, DNases, RNases, and restriction endonucleases (which all break the phosphodiester backbone of DNA or RNA), as well as numerous less-well-characterized small-molecule phosphodiesterases. The cyclic nucleotide phosphodiesterases comprise a group of enzymes that degrade the phosphodiester bond in the second messenger molecules cAMP and cGMP. They regulate the localization, duration, and amplitude of cyclic nucleotide signaling within subcellular domains. PDEs are therefore important regulators of signal transduction mediated by these second messenger molecules. History These multiple forms (isoforms or subtypes) of phosp ...
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Phosphatidic Acid
Phosphatidic acids are anionic phospholipids important to cell signaling and direct activation of lipid-gated ion channels. Hydrolysis of phosphatidic acid gives rise to one molecule each of glycerol and phosphoric acid and two molecules of fatty acids. They constitute about 0.25% of phospholipids in the bilayer. Structure Phosphatidic acid consists of a glycerol backbone, with, in general, a saturated fatty acid bonded to carbon-1, an unsaturated fatty acid bonded to carbon-2, and a phosphate group bonded to carbon-3. Formation and degradation Besides de novo synthesis, PA can be formed in three ways: * By phospholipase D (PLD), via the hydrolysis of the P-O bond of phosphatidylcholine (PC) to produce PA and choline. * By the phosphorylation of diacylglycerol (DAG) by DAG kinase (DAGK). * By the acylation of lysophosphatidic acid by lysoPA-acyltransferase (LPAAT); this is the most common pathway.Devlin, T. M. 2004. ''Bioquímica'', 4ª edición. Reverté, Barcelona. The glyc ...
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