Phospholipase A2: Difference between revisions
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PLA2 serve as pharmacological targets for therapeutical treatment of diseases like atherosclerosis, immune disorders, cardiovascular diseases and cancer<ref>PMID:24907600</ref>. | PLA2 serve as pharmacological targets for therapeutical treatment of diseases like atherosclerosis, immune disorders, cardiovascular diseases and cancer<ref>PMID:24907600</ref>. | ||
== Crystal structure of porcine pancreatic phospholipase A<sub>2</sub> in complex with 2-methoxycyclohexa-2-5-diene-1,4-dione | == Crystal structure of porcine pancreatic phospholipase A<sub>2</sub> in complex with 2-methoxycyclohexa-2-5-diene-1,4-dione == | ||
<ref >DOI 10.1080/21553769.2012.689262</ref> | <ref >DOI 10.1080/21553769.2012.689262</ref> | ||
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**[[1le6]], [[1le7]], [[4uy1]] – hPLA2G10 | **[[1le6]], [[1le7]], [[4uy1]] – hPLA2G10 | ||
*Human | *Human phospholipase A2 group XV | ||
**[[4x90]] – hPLA2G15<br /> | **[[4x90]] – hPLA2G15<br /> |
Revision as of 09:12, 29 June 2016
FunctionPhospholipase A2 (PLA2) is an enzyme which releases fatty acids from glycerol. It is found in mammals and in snake venoms[1]. PLA2 releases arachidonic acid from membranes causing inflammation and pain. The PLA2 contains many isozymes which are ordered by groups and named accordingly, ie., group I is PLA2G1.
RelevancePLA2 serve as pharmacological targets for therapeutical treatment of diseases like atherosclerosis, immune disorders, cardiovascular diseases and cancer[7]. Crystal structure of porcine pancreatic phospholipase A2 in complex with 2-methoxycyclohexa-2-5-diene-1,4-dione
possesses anti-inflammatory activity. The binding of curcumin with PLA2 was studied using X-ray crystallography. Since the electron density found in the active site did not match with curcumin, (the photo-degraded product of curcumin) in the unexplained electron density. To understand the , molecular docking studies was carried out. with respect to the ligand position and identified that of PLA2 with a binding energy -16.81 Kcal/mol. The binding mode is in such a manner that it can prevent the entry of substrate to the hydrophobic active site. These studies indicate that curcumin can be act as an inhibitor to PLA2. |
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3D Structures of Phospholipase A23D Structures of Phospholipase A2
Updated on 29-June-2016
ReferencesReferences
- ↑ Dennis EA. Diversity of group types, regulation, and function of phospholipase A2. J Biol Chem. 1994 May 6;269(18):13057-60. PMID:8175726
- ↑ Leitinger N, Watson AD, Hama SY, Ivandic B, Qiao JH, Huber J, Faull KF, Grass DS, Navab M, Fogelman AM, de Beer FC, Lusis AJ, Berliner JA. Role of group II secretory phospholipase A2 in atherosclerosis: 2. Potential involvement of biologically active oxidized phospholipids. Arterioscler Thromb Vasc Biol. 1999 May;19(5):1291-8. PMID:10323782
- ↑ Lapointe S, Brkovic A, Cloutier I, Tanguay JF, Arm JP, Sirois MG. Group V secreted phospholipase A2 contributes to LPS-induced leukocyte recruitment. J Cell Physiol. 2010 Jul;224(1):127-34. doi: 10.1002/jcp.22106. PMID:20232296 doi:http://dx.doi.org/10.1002/jcp.22106
- ↑ Hallstrand TS, Lai Y, Hooper KA, Oslund RC, Altemeier WA, Matute-Bello G, Gelb MH. Endogenous secreted phospholipase A2 group X regulates cysteinyl leukotrienes synthesis by human eosinophils. J Allergy Clin Immunol. 2016 Jan;137(1):268-77.e8. doi:, 10.1016/j.jaci.2015.05.026. Epub 2015 Jun 30. PMID:26139511 doi:http://dx.doi.org/10.1016/j.jaci.2015.05.026
- ↑ Platt RW, Brookhart MA, Cole SR, Westreich D, Schisterman EF. Reply to taguri and matsuyama. Stat Med. 2013 Sep 10;32(20):3592-3. doi: 10.1002/sim.5805. PMID:23943550 doi:http://dx.doi.org/10.1002/sim.5805
- ↑ Duncan RE, Sarkadi-Nagy E, Jaworski K, Ahmadian M, Sul HS. Identification and functional characterization of adipose-specific phospholipase A2 (AdPLA). J Biol Chem. 2008 Sep 12;283(37):25428-36. doi: 10.1074/jbc.M804146200. Epub 2008, Jul 9. PMID:18614531 doi:http://dx.doi.org/10.1074/jbc.M804146200
- ↑ Quach ND, Arnold RD, Cummings BS. Secretory phospholipase A2 enzymes as pharmacological targets for treatment of disease. Biochem Pharmacol. 2014 Aug 15;90(4):338-48. doi: 10.1016/j.bcp.2014.05.022. Epub, 2014 Jun 4. PMID:24907600 doi:http://dx.doi.org/10.1016/j.bcp.2014.05.022
- ↑ Crystal structure of porcine pancreatic phospholipase a2 in complex with 2-methoxycyclohexa-2-5-diene-1,4-dione. Dileep KV, Tintu I, Mandal PK, Karthe P, Haridas M, Sadasivan C. Frontiers In Life Sci. (2012) doi:http://dx.doi.org/10.1080/21553769.2012.689262