3 edition of Phospholipase A2 found in the catalog.
Includes bibliographical references and indexes.
|Statement||volume editors, W. Uhl, T.J. Nevalainen, M.W. Büchler.|
|Series||Progress in surgery ;, vol. 24|
|Contributions||Büchler, Markus, 1955-, Nevalainen, Timo J., Uhl, W.|
|LC Classifications||RB131 .P49 1997|
|The Physical Object|
|Pagination||xi, 250 p. :|
|Number of Pages||250|
|LC Control Number||97000261|
Snake venoms are a complex mixture of compounds with a wide range of biological and pharmacological activities, which more than 90% of their dry weight is composed by proteins, comprising a variety of enzymes, such as proteases (metalo and serine), phospholipases A 2, L-aminoacid oxidases, esterases, and others .A great number of proteins were purified and characterized from snake venoms Cited by: 5. from book Bioactive lipid We establish that the mitochondrion is an endogenous substrate of secreted phospholipase A2 IIA (sPLA2-IIA), a phospholipase otherwise specific for bacteria, likely.
Get this from a library! Phospholipase A2: Role and Function in Inflammation. [Patrick Y-K Wong; Edward A Dennis] -- This volume in the Advances in Experimental Medicine and Biology Series is dedicated to developing an overall view of the "state-of the-art" of knowledge in the field of phospholipase A2 and to. Secretory phospholipase A2 (sPLA2) plays a pivotal role in acute respiratory distress syndrome (ARDS). This enzyme seems an interesting target to reduce surfactant catabolism and lung tissue inflammation. Varespladib is a specifically designed indolic sPLA2 inhibitor, which has shown promising results in animals and by: 4.
Phospholipase A2 enzymes (PLA2 enzymes) are the most fascinating group of proteins and Venom Phospholipase A2 Enzymes is the first comprehensive book covering both fundamental and recent advances in phospholipase research. Particular emphasis is placed on the pharmalogical effects of snake venom PLA2 : R. Manjunatha Kini. View protein in InterPro IPR PLipase_A2 IPR PLipase_A2_Asp_AS IPR PLipase_A2_dom IPR PLipase_A2_dom_sf IPR PLipase_A2_His_AS: PANTHER i: PTHR PTHR, 1 hit: Pfam i: View protein in Pfam PF Phospholip_A2_1, 1 hit.
Essays on American industrialism: selected papers of Samuel M. Levin.
Pot lids, goss, commemorative and Staffordshire wares including portrait figures
The Music Index: A Subject-Author Guide to Music Periodical Literature : Annual Cumulation
Education in Asia
Hearing on H.R. 9, To Open for Settlement Certain Lands in the Kiowa, Comanche, and Apache Indian Reservations in Oklahoma Territory
Life histories of North American gallinaceous birds
Proceedings of a Symposium on Rhinos as Game Ranch Animals, Onderstepoort, Republic of South Africa, 9-10 September 1994
tutorial on the fife
Easy access to Locoscript 1 on the Amstrad personal computer word processor
Programming in Fortran
Encyclopedia of associations.
Big Green Thing Gb
Cultures in the context of sharing the gospel
Register of performers and composers.
The place-names of Dorset.
Phospholipase A>2: Role and Function in Inflammation (Advances in Experimental Medicine and Biology) Softcover reprint of the original 1st ed. Edition. Why is ISBN important. This bar-code number lets you verify that you're getting exactly the right version or edition of a by: 3.
This book grew out of two major symposia on phospholipase A2 held in I). "Phospholipase A2: Pathophysiological Role of Soluble and Membrane-Bound Enzymes" organized by Dr.
Doug Morgan and Dr. Ann Welton of Hoffmann-La Roche and sponsored Brand: Springer US. Phospholipase A2 in Clinical Inflammation presents an up-to-date topical review of the biochemistry, molecular biology, and biology of mammalian phospholipase A2 (PLA2).
The emphasis of this monograph is on the current aspects of PLA2 research using molecular approaches to investigate PLA2 structure and function, inhibitor design, and the regulation of sPLA2 and cPLA2 in cellular systems.
This book grew out of two major symposia on phospholipase A2 held in I). "Phospholipase A2: Pathophysiological Role of Soluble and Membrane-Bound Enzymes" organized by Dr. Doug Morgan and Dr. Ann Welton of Hoffmann-La Roche and sponsored. Phospholipase A 2 (PLA 2) hydrolyzes the sn-2 position of glycerophospholipids to yield fatty acids and the view of signal transduction, the PLA 2 reaction has been considered to be of particular importance since arachidonic acid, one of the polyunsaturated fatty acids released by PLA 2, is metabolized by cyclooxygenases and lipoxygenases to the potent lipid mediators.
Thromboxane A2 (TxA2) is in the family of lipids known as eicosanoids, which are metabolites of arachidonic acid generated by the sequential action of three enzymes – phospholipase A2, COX-1/COX-2 and TxA2 Synthase (TXAS).Author: Dane Rucker, Amit S.
Dhamoon. Phospholipase A 2 (PLA 2) enzymes are a family of proteins and to date at least 20 members have been identified in family can be classified into four classes on the basis of their nucleotide and amino acid sequence homology.
First, there are at present ten secreted phospholipase A 2 enzymes (sPLA 2-IB, -IIA, -IIC, -IID, -IIE, -IIF, -III, -V, -X, and -XII), which are of low. F PHOSPHOLIPASE A2.
Phospholipase A2 (PLA2) consists of a family of enzymes that catalyze the hydrolysis of phosphatidlycholine and/or phosphatidylethanolamine. The EnzChek Phospholipase A2 Kit provides enough reagents for 2 microplates, using µl volumes in 96 well format to perform continuous fluorometric monitoring of PLA2.
This product offers an alternative to our (B), (bis-BODIPY® FL CPC) reagent, by providing an PLA2 selective substrate and one that is ratiometric, thereby lowering. The PLA2G1B is a secreted phospholipase expressed primarily in the acinar cells of the pancreas and to lesser extent also in the lung and islet β-cells.
In pancreatic acinar cells, PLA2G1B is found within zymogen granules along with other digestive by: Bee stings and venomous snake bites cause immediate inflammation, resulting in pain and swelling. The enzyme in venom that triggers this immune response is phospholipase A2. This enzyme is also present in human tissue.
During infection, PLA2 activates a cascade that results in the destruction of the cell membranes of invading microbes. Lipoprotein‐associated phospholipase A2 (Lp‐PLA2) mediates vascular inflammation through the regulation of lipid metabolism in blood, thus, it has been extensively investigated to identify its role in vascular inflammation‐related diseases, mainly by: 1.
The expression of phospholipase A2 receptor 1 (PLA2R) on the podocyte membrane is recognized as an antigenic stimulus, against which an IgG4 or IgG1 is produced, local complement activation, inflammatory and oxidative response, with podocyte disruption and lesion in the filtration barrier with consequent : Rosa M.
Viero, Bruno M. Miamoto, Vanessa dos S. Silva, DanielaC. dos Santos. Phospholipase A2 acts on the intact lecithin molecule and hydrolyses the fatty acid esterified to the second carbon atom. The resulting products are lysolecithin and a fatty acid. Phospholipase A2 is an enzyme present in the venom of bees and viper snakes.
4 External links. Phospholipase A2 (PLA2) designates a class of enzymes that hydrolyze the sn-2 ester of glycerophospholipids to produce a fatty acid and a lysophospholipid.
It has become clear that some of these enzymes liberate arachidonic acid in mammalian cells for the biosynthesis of eicosanoids, and thus there has been considerable interest in developing PLA2 inhibitors.
Phospholipase A 2 (PLA 2) enzymes play a major role in many diseases including the inflammatory cascade and specific potent small molecule inhibitors could be useful in studying their physiological role as well as for the development of : Varnavas D. Mouchlis, Carol Mu, Renee Hammons, Edward A.
Dennis. Identification of calcium-independent phospholipase A2 (iPLA2) beta, and not iPLA2gamma, as the mediator of arginine vasopressin-induced arachidonic acid release in A smooth muscle cells.
Enantioselective mechanism-based discrimination of mammalian by: Phospholipase A 2 is one of the most intensively studied membrane proteins which hydrolyzes phospholipids at the sn-2 position to form fatty acid and lysophospholipid products.
These are small proteins and the 3-D structures are known to high resolution for several species. Phospholipase A 2 proteins are of high pharmaceutical concern since they are responsible for the release of arachidonic.
Phospholipase A1 encoded by the PLA1A gene is a phospholipase enzyme which removes the 1-acyl. Phospholipase A1 is an enzyme that resides in a class of enzymes called phospholipase that hydrolyze phospholipids into fatty acids.
There are 4 classes, which are BRENDA: BRENDA entry. ISBN: OCLC Number: Description: xi, pages: illustrations ; 25 cm. Contents: Part 1 Structure, distribution and function of phospholipase A2: history, classification, structure and function of phospholipase A2; expression of group II phospholipase A2 in human tissues; determinants of the antimicrobial action of kD phospholipase A2; downregulation of.
Phospholipase A2 is in fact a family of enzymes that are categorized by location and function. They have strong antibacterial and antiviral properties as part of the innate immune system, but also participate in many other biochemical processes that include cell signaling, cell proliferation and differentiation, cell migration and apoptosis.
First, there are at present ten secreted phospholipase A 2 enzymes (sPLA 2-IB, sPLA 2-IIA, sPLA 2-IIC, sPLA 2-IID, sPLA 2-IIE, sPLA 2-IIF, sPLA 2-III, sPLA 2-V, sPLA 2-X, and sPLA 2-XII), which are of low molecular weight (13–18 kDa) with a catalytic histidine in their active site and a requirement for calcium for enzyme activity.
Second, there are three characterized human cytosolic .The structure, function, and catalytic mechanism of the enzyme determine its place within the phospholipase A 2 superfamily, be it secretory PLA 2 (sPLA 2), cytosolic PLA 2 (cPLA 2), Ca 2+-independent phospholipase A 2 (iPLA 2), PAF acetylhydrolases (PAF-AH), or lysosomal PLA 2 (LPLA 2).The latest classification, based on genetic structure, divides these enzymes into groups from I to Cited by: