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{{Infobox_gene}}
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'''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>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Phospholipase A2, group V
| HGNCid = 9038
| Symbol = PLA2G5
| AltSymbols =; DKFZp686C2294; GV-PLA2; MGC46205; PLA2-10; hVPLA(2)
| OMIM = 601192
| ECnumber =
| Homologene = 716
| MGIid = 101899
  | GeneAtlas_image1 = PBB_GE_PLA2G5_206178_at_tn.png
| GeneAtlas_image2 = PBB_GE_PLA2G5_215870_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PLA2G5_gnf1h03549_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0047498 |text = calcium-dependent phospholipase A2 activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006644 |text = phospholipid metabolic process}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5322
    | Hs_Ensembl = ENSG00000127472
    | Hs_RefseqProtein = NP_000920
    | Hs_RefseqmRNA = NM_000929
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 20269288
    | Hs_GenLoc_end = 20290248
    | Hs_Uniprot = P39877
    | Mm_EntrezGene = 18784
    | Mm_Ensembl = ENSMUSG00000041193
    | Mm_RefseqmRNA = NM_011110
    | Mm_RefseqProtein = NP_035240
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 138071320
    | Mm_GenLoc_end = 138135558
    | Mm_Uniprot = Q6GTW1
  }}
}}
'''Phospholipase A2, group V''', also known as '''PLA2G5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PLA2G5 phospholipase A2, group V| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5322| accessdate = }}</ref>


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{{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">{{cite web | title = Entrez Gene: PLA2G5 phospholipase A2, group V| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5322| accessdate = }}</ref>
| 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}}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Schröder HC, Perovic S, Kavsan V, ''et al.'' |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   |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= 1-2 |pages= 48-58 |year= 2001 |pmid= 11080676 |doi=  }}
*{{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  | author=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  | 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  | author=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 |year= 1994 |pmid= 8300559 |doi=  }}
*{{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  | author=Tischfield JA, Xia YR, Shih DM, ''et al.'' |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 |year= 1997 |pmid= 8838795 |doi= 10.1006/geno.1996.0126 }}
*{{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  | author=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=  }}
*{{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 | author=Mavoungou E, Georges-Courbot MC, Poaty-Mavoungou V, ''et al.'' |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=  }}
*{{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  | author=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= }}
*{{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 | author=Bingham CO, Fijneman RJ, Friend DS, ''et al.'' |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=  }}
*{{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  | author=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=  }}
*{{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  | author=Kim KP, Han SK, Hong M, Cho W |title=The molecular basis of phosphatidylcholine preference of human group-V phospholipase A2. |journal=Biochem. J. |volume=348 Pt 3 |issue=  |pages= 643-7 |year= 2000 |pmid= 10839997 |doi=  }}
*{{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 | author=Seeds MC, Jones KA, Duncan Hite R, ''et al.'' |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=  }}
*{{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  | author=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 }}
*{{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 | author=Degousee N, Ghomashchi F, Stefanski E, ''et al.'' |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  | 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 | author=Kim YJ, Kim KP, Han SK, ''et al.'' |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   |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  | author=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=  }}
*{{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 | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{cite journal | author=Muñoz NM, Kim YJ, Meliton AY, ''et al.'' |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 }}
}}
}}
{{refend}}
{{refend}}


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Revision as of 18:15, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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]

[4]

References

  1. ↑ 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.
  2. ↑ 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. ↑ 3.0 3.1 "Entrez Gene: PLA2G5 phospholipase A2, group V".
  4. ↑ 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. PMID 23650617.

Further reading



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