PLA2G5: Difference between revisions
Jump to navigation
Jump to search
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}})) |
imported>Rjwilmsi m (Journal cites:, added 1 PMC) |
||
| (One intermediate revision by one other user not shown) | |||
| Line 1: | Line 1: | ||
{{Infobox_gene}} | |||
{{ | '''Calcium-dependent [[phospholipase A2]]''' is an [[enzyme]] that in humans is encoded by the ''PLA2G5'' [[gene]].<ref name="pmid8838795">{{cite journal | vauthors = Tischfield JA, Xia YR, Shih DM, Klisak I, Chen J, Engle SJ, Siakotos AN, Winstead MV, Seilhamer JJ, Allamand V, Gyapay G, Lusis AJ | title = Low-molecular-weight, calcium-dependent phospholipase A2 genes are linked and map to homologous chromosome regions in mouse and human | journal = Genomics | volume = 32 | issue = 3 | pages = 328–33 |date=February 1997 | pmid = 8838795 | pmc = | doi = 10.1006/geno.1996.0126 }}</ref><ref name="pmid8300559">{{cite journal | vauthors = Chen J, Engle SJ, Seilhamer JJ, Tischfield JA | title = Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2 | journal = J Biol Chem | volume = 269 | issue = 4 | pages = 2365–8 |date=March 1994 | pmid = 8300559 | pmc = | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PLA2G5 phospholipase A2, group V| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5322| accessdate = }}</ref> | ||
}} | |||
{{ | |||
| | |||
| | |||
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. --> | <!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. --> | ||
{{PBB_Summary | {{PBB_Summary | ||
| section_title = | | section_title = | ||
| summary_text = This gene is a member of the secretory phospholipase A2 family. It is located in a tightly-linked cluster of secretory phospholipase A2 genes on chromosome 1. The encoded enzyme catalyzes the hydrolysis of membrane phospholipids to generate lysophospholipids and free fatty acids including arachidonic acid. It preferentially hydrolyzes linoleoyl-containing phosphatidylcholine substrates. Secretion of this enzyme is thought to induce inflammatory responses in neighboring cells. Alternatively spliced transcript variants have been found, but their full-length nature has not been determined.<ref name="entrez" | | summary_text = This gene is a member of the secretory phospholipase A2 family. It is located in a tightly-linked cluster of secretory phospholipase A2 genes on chromosome 1. The encoded enzyme catalyzes the hydrolysis of membrane phospholipids to generate lysophospholipids and free fatty acids including [[arachidonic acid]]. It preferentially hydrolyzes linoleoyl-containing phosphatidylcholine substrates. Secretion of this enzyme is thought to induce inflammatory responses in neighboring cells. Alternatively spliced transcript variants have been found, but their full-length nature has not been determined.<ref name="entrez" /> | ||
}} | }} | ||
<ref>{{cite journal|last1=Otha|first1=Shin|title=Group V secretory phospholipase A2 is involved in macrophage activation and is sufficient for macrophage effector functions in allergic pulmonary inflammation.|journal=Journal of Immunology|date=15 June 2013|volume=12|issue=190|pages=5927-38|doi=10.4049/jimmunol.1203202|pmid=23650617|pmc=3939699}}</ref> | |||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | *{{cite journal |vauthors=Schröder HC, Perovic S, Kavsan V, etal |title=Mechanisms of prionSc- and HIV-1 gp120 induced neuronal cell death. |journal=Neurotoxicology |volume=19 |issue= 4–5 |pages= 683–8 |year= 1998 |pmid= 9745929 |doi= }} | ||
*{{cite journal | author=Cho W |title=Structure, function, and regulation of group V phospholipase A(2). |journal=Biochim. Biophys. Acta |volume=1488 |issue= | *{{cite journal | author=Cho W |title=Structure, function, and regulation of group V phospholipase A(2). |journal=Biochim. Biophys. Acta |volume=1488 |issue= 1–2 |pages= 48–58 |year= 2001 |pmid= 11080676 |doi= 10.1016/s1388-1981(00)00109-8}} | ||
*{{cite journal | | *{{cite journal | vauthors=de Beer FC, Webb NR |title=Inflammation and atherosclerosis: Group IIa and Group V sPLA2 are not redundant. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=26 |issue= 7 |pages= 1421–2 |year= 2006 |pmid= 16794232 |doi= 10.1161/01.ATV.0000227561.89488.9a }} | ||
*{{cite journal | | *{{cite journal | vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }} | ||
*{{cite journal |vauthors=Mavoungou E, Georges-Courbot MC, Poaty-Mavoungou V, etal |title=HIV and SIV envelope glycoproteins induce phospholipase A2 activation in human and macaque lymphocytes. |journal=J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. |volume=16 |issue= 1 |pages= 1–9 |year= 1997 |pmid= 9377118 |doi= 10.1097/00042560-199709010-00001}} | |||
*{{cite journal | vauthors=Chen Y, Dennis EA |title=Expression and characterization of human group V phospholipase A2. |journal=Biochim. Biophys. Acta |volume=1394 |issue= 1 |pages= 57–64 |year= 1998 |pmid= 9767110 |doi= 10.1016/s0005-2760(98)00098-8 }} | |||
*{{cite journal | *{{cite journal |vauthors=Bingham CO, Fijneman RJ, Friend DS, etal |title=Low molecular weight group IIA and group V phospholipase A(2) enzymes have different intracellular locations in mouse bone marrow-derived mast cells. |journal=J. Biol. Chem. |volume=274 |issue= 44 |pages= 31476–84 |year= 1999 |pmid= 10531350 |doi=10.1074/jbc.274.44.31476 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Johansen B, Rakkestad K, Balboa MA, Dennis EA |title=Expression of cytosolic and secreted forms of phospholipase A(2) and cyclooxygenases in human placenta, fetal membranes, and chorionic cell lines. |journal=Prostaglandins Other Lipid Mediat. |volume=60 |issue= 4–6 |pages= 119–25 |year= 2000 |pmid= 10751642 |doi=10.1016/S0090-6980(99)00057-X }} | ||
*{{cite journal | *{{cite journal | vauthors=Kim KP, Han SK, Hong M, Cho W |title=The molecular basis of phosphatidylcholine preference of human group-V phospholipase A2. | series=348 |journal=Biochem. J. |volume=Pt 3 |issue= 3|pages= 643–7 |year= 2000 |pmid= 10839997 |doi=10.1042/0264-6021:3480643 | pmc=1221108 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Seeds MC, Jones KA, Duncan Hite R, etal |title=Cell-specific expression of group X and group V secretory phospholipases A(2) in human lung airway epithelial cells. |journal=Am. J. Respir. Cell Mol. Biol. |volume=23 |issue= 1 |pages= 37–44 |year= 2000 |pmid= 10873151 |doi= 10.1165/ajrcmb.23.1.4034}} | ||
*{{cite journal | | *{{cite journal | vauthors=Bernatchez PN, Winstead MV, Dennis EA, Sirois MG |title=VEGF stimulation of endothelial cell PAF synthesis is mediated by group V 14 kDa secretory phospholipase A2. |journal=Br. J. Pharmacol. |volume=134 |issue= 1 |pages= 197–205 |year= 2001 |pmid= 11522612 |doi= 10.1038/sj.bjp.0704215 | pmc=1572915 }} | ||
*{{cite journal | *{{cite journal |vauthors=Degousee N, Ghomashchi F, Stefanski E, etal |title=Groups IV, V, and X phospholipases A2s in human neutrophils: role in eicosanoid production and gram-negative bacterial phospholipid hydrolysis. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 5061–73 |year= 2002 |pmid= 11741884 |doi= 10.1074/jbc.M109083200 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Kim YJ, Kim KP, Han SK, etal |title=Group V phospholipase A2 induces leukotriene biosynthesis in human neutrophils through the activation of group IVA phospholipase A2. |journal=J. Biol. Chem. |volume=277 |issue= 39 |pages= 36479–88 |year= 2002 |pmid= 12124392 |doi= 10.1074/jbc.M205399200 }} | ||
*{{cite journal | *{{cite journal | vauthors=Hichami A, Joshi B, Simonin AM, Khan NA |title=Role of three isoforms of phospholipase A2 in capacitative calcium influx in human T-cells. |journal=Eur. J. Biochem. |volume=269 |issue= 22 |pages= 5557–63 |year= 2003 |pmid= 12423354 |doi=10.1046/j.1432-1033.2002.03261.x }} | ||
*{{cite journal | *{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Muñoz NM, Kim YJ, Meliton AY, etal |title=Human group V phospholipase A2 induces group IVA phospholipase A2-independent cysteinyl leukotriene synthesis in human eosinophils. |journal=J. Biol. Chem. |volume=278 |issue= 40 |pages= 38813–20 |year= 2003 |pmid= 12796497 |doi= 10.1074/jbc.M302476200 }} | ||
*{{cite journal | |||
*{{cite journal | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{ | <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. --> | ||
{{ | {{PBB_Controls | ||
| update_page = yes | |||
| require_manual_inspection = no | |||
| update_protein_box = yes | |||
| update_summary = yes | |||
| update_citations = yes | |||
}} | |||
{{gene-1-stub}} | |||
Latest revision as of 15:49, 9 March 2018
| VALUE_ERROR (nil) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Aliases | |||||||
| External IDs | GeneCards: [1] | ||||||
| Orthologs | |||||||
| Species | Human | Mouse | |||||
| Entrez |
|
| |||||
| Ensembl |
|
| |||||
| UniProt |
|
| |||||
| RefSeq (mRNA) |
|
| |||||
| RefSeq (protein) |
|
| |||||
| Location (UCSC) | n/a | n/a | |||||
| PubMed search | n/a | n/a | |||||
| Wikidata | |||||||
| |||||||
Calcium-dependent phospholipase A2 is an enzyme that in humans is encoded by the PLA2G5 gene.[1][2][3]
This gene is a member of the secretory phospholipase A2 family. It is located in a tightly-linked cluster of secretory phospholipase A2 genes on chromosome 1. The encoded enzyme catalyzes the hydrolysis of membrane phospholipids to generate lysophospholipids and free fatty acids including arachidonic acid. It preferentially hydrolyzes linoleoyl-containing phosphatidylcholine substrates. Secretion of this enzyme is thought to induce inflammatory responses in neighboring cells. Alternatively spliced transcript variants have been found, but their full-length nature has not been determined.[3]
References
- ↑ Tischfield JA, Xia YR, Shih DM, Klisak I, Chen J, Engle SJ, Siakotos AN, Winstead MV, Seilhamer JJ, Allamand V, Gyapay G, Lusis AJ (February 1997). "Low-molecular-weight, calcium-dependent phospholipase A2 genes are linked and map to homologous chromosome regions in mouse and human". Genomics. 32 (3): 328–33. doi:10.1006/geno.1996.0126. PMID 8838795.
- ↑ Chen J, Engle SJ, Seilhamer JJ, Tischfield JA (March 1994). "Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2". J Biol Chem. 269 (4): 2365–8. PMID 8300559.
- ↑ 3.0 3.1 "Entrez Gene: PLA2G5 phospholipase A2, group V".
- ↑ Otha, Shin (15 June 2013). "Group V secretory phospholipase A2 is involved in macrophage activation and is sufficient for macrophage effector functions in allergic pulmonary inflammation". Journal of Immunology. 12 (190): 5927–38. doi:10.4049/jimmunol.1203202. PMC 3939699. PMID 23650617.
Further reading
- Schröder HC, Perovic S, Kavsan V, et al. (1998). "Mechanisms of prionSc- and HIV-1 gp120 induced neuronal cell death". Neurotoxicology. 19 (4–5): 683–8. PMID 9745929.
- Cho W (2001). "Structure, function, and regulation of group V phospholipase A(2)". Biochim. Biophys. Acta. 1488 (1–2): 48–58. doi:10.1016/s1388-1981(00)00109-8. PMID 11080676.
- de Beer FC, Webb NR (2006). "Inflammation and atherosclerosis: Group IIa and Group V sPLA2 are not redundant". Arterioscler. Thromb. Vasc. Biol. 26 (7): 1421–2. doi:10.1161/01.ATV.0000227561.89488.9a. PMID 16794232.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Mavoungou E, Georges-Courbot MC, Poaty-Mavoungou V, et al. (1997). "HIV and SIV envelope glycoproteins induce phospholipase A2 activation in human and macaque lymphocytes". J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 16 (1): 1–9. doi:10.1097/00042560-199709010-00001. PMID 9377118.
- Chen Y, Dennis EA (1998). "Expression and characterization of human group V phospholipase A2". Biochim. Biophys. Acta. 1394 (1): 57–64. doi:10.1016/s0005-2760(98)00098-8. PMID 9767110.
- Bingham CO, Fijneman RJ, Friend DS, et al. (1999). "Low molecular weight group IIA and group V phospholipase A(2) enzymes have different intracellular locations in mouse bone marrow-derived mast cells". J. Biol. Chem. 274 (44): 31476–84. doi:10.1074/jbc.274.44.31476. PMID 10531350.
- Johansen B, Rakkestad K, Balboa MA, Dennis EA (2000). "Expression of cytosolic and secreted forms of phospholipase A(2) and cyclooxygenases in human placenta, fetal membranes, and chorionic cell lines". Prostaglandins Other Lipid Mediat. 60 (4–6): 119–25. doi:10.1016/S0090-6980(99)00057-X. PMID 10751642.
- Kim KP, Han SK, Hong M, Cho W (2000). "The molecular basis of phosphatidylcholine preference of human group-V phospholipase A2". Biochem. J. 348. Pt 3 (3): 643–7. doi:10.1042/0264-6021:3480643. PMC 1221108. PMID 10839997.
- Seeds MC, Jones KA, Duncan Hite R, et al. (2000). "Cell-specific expression of group X and group V secretory phospholipases A(2) in human lung airway epithelial cells". Am. J. Respir. Cell Mol. Biol. 23 (1): 37–44. doi:10.1165/ajrcmb.23.1.4034. PMID 10873151.
- Bernatchez PN, Winstead MV, Dennis EA, Sirois MG (2001). "VEGF stimulation of endothelial cell PAF synthesis is mediated by group V 14 kDa secretory phospholipase A2". Br. J. Pharmacol. 134 (1): 197–205. doi:10.1038/sj.bjp.0704215. PMC 1572915. PMID 11522612.
- Degousee N, Ghomashchi F, Stefanski E, et al. (2002). "Groups IV, V, and X phospholipases A2s in human neutrophils: role in eicosanoid production and gram-negative bacterial phospholipid hydrolysis". J. Biol. Chem. 277 (7): 5061–73. doi:10.1074/jbc.M109083200. PMID 11741884.
- Kim YJ, Kim KP, Han SK, et al. (2002). "Group V phospholipase A2 induces leukotriene biosynthesis in human neutrophils through the activation of group IVA phospholipase A2". J. Biol. Chem. 277 (39): 36479–88. doi:10.1074/jbc.M205399200. PMID 12124392.
- Hichami A, Joshi B, Simonin AM, Khan NA (2003). "Role of three isoforms of phospholipase A2 in capacitative calcium influx in human T-cells". Eur. J. Biochem. 269 (22): 5557–63. doi:10.1046/j.1432-1033.2002.03261.x. PMID 12423354.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Muñoz NM, Kim YJ, Meliton AY, et al. (2003). "Human group V phospholipase A2 induces group IVA phospholipase A2-independent cysteinyl leukotriene synthesis in human eosinophils". J. Biol. Chem. 278 (40): 38813–20. doi:10.1074/jbc.M302476200. PMID 12796497.
 | This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it. |