PLA2G1B: Difference between revisions

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{{Infobox_gene}}
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'''[[Phospholipase A2]], group 1B''' is an [[enzyme]] that in humans is encoded by the ''PLA2G1B'' [[gene]].<ref name="pmid8175726">{{cite journal | author = Dennis EA | title = Diversity of group types, regulation, and function of phospholipase A2 | journal = J Biol Chem | volume = 269 | issue = 18 | pages = 13057–60 |date=Jun 1994 | pmid = 8175726 | pmc = | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PLA2G1B phospholipase A2, group IB (pancreas)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5319| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Phospholipase A2, group IB (pancreas)
| HGNCid = 9030
| Symbol = PLA2G1B
| AltSymbols =; MGC119834; MGC119835; PLA2; PLA2A; PPLA2
| OMIM = 172410
| ECnumber = 
| Homologene = 715
| MGIid = 101842
| GeneAtlas_image1 = PBB_GE_PLA2G1B_206311_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004623 |text = phospholipase A2 activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006644 |text = phospholipid metabolic process}} {{GNF_GO|id=GO:0007015 |text = actin filament organization}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5319
    | Hs_Ensembl = ENSG00000170890
    | Hs_RefseqProtein = NP_000919
    | Hs_RefseqmRNA = NM_000928
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 119244298
    | Hs_GenLoc_end = 119249975
    | Hs_Uniprot = P04054
    | Mm_EntrezGene = 18778
    | Mm_Ensembl = ENSMUSG00000029522
    | Mm_RefseqmRNA = NM_011107
    | Mm_RefseqProtein = NP_035237
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 115727265
    | Mm_GenLoc_end = 115735716
    | Mm_Uniprot = Q9Z0Y2
  }}
}}
'''Phospholipase A2, group IB (pancreas)''', also known as '''PLA2G1B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PLA2G1B phospholipase A2, group IB (pancreas)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5319| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Phospholipase A2 (EC 3.1.1.4) catalyzes the release of [[fatty acid]]s from glycero-3-phosphocholines. The best known varieties are the digestive enzymes secreted as zymogens by the pancreas of mammals as well as fish.<ref name="pmid20836903">{{cite journal | vauthors = Sæle O, Nordgreen A, Olsvik PA, Hamre K | title = Characterisation and expression of secretory phospholipase A2 group IB during ontogeny of Atlantic cod ( Gadus morhua). | journal = Br J Nutr | year = 2010 | volume =  105| issue=  2| pages= 1–10 | pmid=20836903 | url= | doi=10.1017/S0007114510003466 }}</ref> Sequences of pancreatic PLA2 enzymes from a variety of mammals have been reported. One striking feature of these enzymes is their close homology to venom phospholipases of snakes. Other forms of PLA2 have been isolated from brain, liver, lung, spleen, intestine, macrophages, leukocytes, erythrocytes, inflammatory exudates, chondrocytes, and platelets (Seilhamer et al., 1986) .<ref name="entrez"/><ref name="pmid3028739">{{cite journal  | vauthors = Seilhamer JJ, Randall TL, Yamanaka M, Johnson LK | title = Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung. | journal = DNA | volume = 5 | issue = 6 | pages = 519–27 | year = 1987 | pmid = 3028739 | doi = 10.1089/dna.1.1986.5.519}}
{{PBB_Summary
</ref>
| section_title =
| summary_text = Phospholipase A2 (EC 3.1.1.4) catalyzes the release of fatty acids from glycero-3-phosphocholines. The best known varieties are the digestive enzymes secreted as zymogens by the pancreas of mammals. Sequences of pancreatic PLA2 enzymes from a variety of mammals have been reported. One striking feature of these enzymes is their close homology to venom phospholipases of snakes. Other forms of PLA2 have been isolated from brain, liver, lung, spleen, intestine, macrophages, leukocytes, erythrocytes, inflammatory exudates, chondrocytes, and platelets (Seilhamer et al., 1986) .[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: PLA2G1B phospholipase A2, group IB (pancreas)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5319| accessdate = }}</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=Dennis EA |title=Diversity of group types, regulation, and function of phospholipase A2. |journal=J. Biol. Chem. |volume=269 |issue= 18 |pages= 13057-60 |year= 1994 |pmid= 8175726 |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=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=Sapirstein A, Bonventre JV |title=Phospholipases A2 in ischemic and toxic brain injury |journal=Neurochem. Res. |volume=25 |issue= 5 |pages= 745–53 |year= 2000 |pmid= 10905638 |doi=10.1023/A:1007583708713 }}
*{{cite journal  | author=Sapirstein A, Bonventre JV |title=Phospholipases A2 in ischemic and toxic brain injury. |journal=Neurochem. Res. |volume=25 |issue= 5 |pages= 745-53 |year= 2000 |pmid= 10905638 |doi=  }}
*{{cite journal  | vauthors=Svensson CI, Yaksh TL |title=The spinal phospholipase-cyclooxygenase-prostanoid cascade in nociceptive processing |journal=Annu. Rev. Pharmacol. Toxicol. |volume=42 |issue=  |pages= 553–83 |year= 2002 |pmid= 11807183 |doi= 10.1146/annurev.pharmtox.42.092401.143905 }}
*{{cite journal  | author=Svensson CI, Yaksh TL |title=The spinal phospholipase-cyclooxygenase-prostanoid cascade in nociceptive processing. |journal=Annu. Rev. Pharmacol. Toxicol. |volume=42 |issue=  |pages= 553-83 |year= 2002 |pmid= 11807183 |doi= 10.1146/annurev.pharmtox.42.092401.143905 }}
*{{cite journal   |vauthors=Clark MA, Ozgür LE, Conway TM, etal |title=Cloning of a phospholipase A2-activating protein |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 12 |pages= 5418–22 |year= 1991 |pmid= 2052621 |doi=10.1073/pnas.88.12.5418 | pmc=51884 }}
*{{cite journal | author=Clark MA, Ozgür LE, Conway TM, ''et al.'' |title=Cloning of a phospholipase A2-activating protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 12 |pages= 5418-22 |year= 1991 |pmid= 2052621 |doi=  }}
*{{cite journal  | vauthors=Verheij HM, Westerman J, Sternby B, De Haas GH |title=The complete primary structure of phospholipase A2 from human pancreas |journal=Biochim. Biophys. Acta |volume=747 |issue= 1–2 |pages= 93–9 |year= 1983 |pmid= 6349696 |doi=10.1016/0167-4838(83)90126-7 }}
*{{cite journal  | author=Seilhamer JJ, Randall TL, Yamanaka M, Johnson LK |title=Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung. |journal=DNA |volume=5 |issue= 6 |pages= 519-27 |year= 1987 |pmid= 3028739 |doi=  }}
*{{cite journal  | vauthors=Sternby B, Akerström B |title=Immunoreactive pancreatic colipase, lipase and phospholipase A2 in human plasma and urine from healthy individuals |journal=Biochim. Biophys. Acta |volume=789 |issue= 2 |pages= 164–9 |year= 1984 |pmid= 6477929 |doi=10.1016/0167-4838(84)90201-2 }}
*{{cite journal  | author=Verheij HM, Westerman J, Sternby B, De Haas GH |title=The complete primary structure of phospholipase A2 from human pancreas. |journal=Biochim. Biophys. Acta |volume=747 |issue= 1-2 |pages= 93-9 |year= 1983 |pmid= 6349696 |doi=  }}
*{{cite journal   |vauthors=Grataroli R, Dijkman R, Dutilh CE, etal |title=Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region |journal=Eur. J. Biochem. |volume=122 |issue= 1 |pages= 111–7 |year= 1982 |pmid= 7060561 |doi=10.1111/j.1432-1033.1982.tb05855.x }}
*{{cite journal  | author=Sternby B, Akerström B |title=Immunoreactive pancreatic colipase, lipase and phospholipase A2 in human plasma and urine from healthy individuals. |journal=Biochim. Biophys. Acta |volume=789 |issue= 2 |pages= 164-9 |year= 1984 |pmid= 6477929 |doi=  }}
*{{cite journal  | author=Rönkkö S |title=Immunohistochemical localization of phospholipase A2 in human and bovine male reproductive organs |journal=Comp. Biochem. Physiol. B, Biochem. Mol. Biol. |volume=110 |issue= 3 |pages= 503–9 |year= 1995 |pmid= 7584826 |doi=10.1016/0305-0491(94)00190-6 }}
*{{cite journal | author=Grataroli R, Dijkman R, Dutilh CE, ''et al.'' |title=Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region. |journal=Eur. J. Biochem. |volume=122 |issue= 1 |pages= 111-7 |year= 1982 |pmid= 7060561 |doi=  }}
*{{cite journal   |vauthors=Lilja I, Smedh K, Olaison G, etal |title=Phospholipase A2 gene expression and activity in histologically normal ileal mucosa and in Crohn's ileitis |journal=Gut |volume=37 |issue= 3 |pages= 380–5 |year= 1995 |pmid= 7590434 |doi=10.1136/gut.37.3.380  | pmc=1382819 }}
*{{cite journal  | author=Rönkkö S |title=Immunohistochemical localization of phospholipase A2 in human and bovine male reproductive organs. |journal=Comp. Biochem. Physiol. B, Biochem. Mol. Biol. |volume=110 |issue= 3 |pages= 503-9 |year= 1995 |pmid= 7584826 |doi=  }}
*{{cite journal  | vauthors=Ancian P, Lambeau G, Mattéi MG, Lazdunski M |title=The human 180-kDa receptor for secretory phospholipases A2. Molecular cloning, identification of a secreted soluble form, expression, and chromosomal localization |journal=J. Biol. Chem. |volume=270 |issue= 15 |pages= 8963–70 |year= 1995 |pmid= 7721806 |doi=  10.1074/jbc.270.15.8963}}
*{{cite journal | author=Lilja I, Smedh K, Olaison G, ''et al.'' |title=Phospholipase A2 gene expression and activity in histologically normal ileal mucosa and in Crohn's ileitis. |journal=Gut |volume=37 |issue= 3 |pages= 380-5 |year= 1995 |pmid= 7590434 |doi=  }}
*{{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 |year= 1994 |pmid= 8300559 |doi=  }}
*{{cite journal  | author=Ancian P, Lambeau G, Mattéi MG, Lazdunski M |title=The human 180-kDa receptor for secretory phospholipases A2. Molecular cloning, identification of a secreted soluble form, expression, and chromosomal localization. |journal=J. Biol. Chem. |volume=270 |issue= 15 |pages= 8963-70 |year= 1995 |pmid= 7721806 |doi=  }}
*{{cite journal   |vauthors=Gispert S, Twells R, Orozco G, etal |title=Chromosomal assignment of the second locus for autosomal dominant cerebellar ataxia (SCA2) to chromosome 12q23-24.1 |journal=Nat. Genet. |volume=4 |issue= 3 |pages= 295–9 |year= 1993 |pmid= 8358438 |doi= 10.1038/ng0793-295 }}
*{{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=Cupillard L, Koumanov K, Mattéi MG, etal |title=Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2 |journal=J. Biol. Chem. |volume=272 |issue= 25 |pages= 15745–52 |year= 1997 |pmid= 9188469 |doi=10.1074/jbc.272.25.15745 }}
*{{cite journal | author=Gispert S, Twells R, Orozco G, ''et al.'' |title=Chromosomal assignment of the second locus for autosomal dominant cerebellar ataxia (SCA2) to chromosome 12q23-24.1. |journal=Nat. Genet. |volume=4 |issue= 3 |pages= 295-9 |year= 1993 |pmid= 8358438 |doi= 10.1038/ng0793-295 }}
*{{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=Cupillard L, Koumanov K, Mattéi MG, ''et al.'' |title=Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2. |journal=J. Biol. Chem. |volume=272 |issue= 25 |pages= 15745-52 |year= 1997 |pmid= 9188469 |doi=  }}
*{{cite journal  |title=Toward a complete human genome sequence |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097–108 |year= 1999 |pmid= 9847074 |doi=  10.1101/gr.8.11.1097}}
*{{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=Sartipy P, Bondjers G, Hurt-Camejo E |title=Phospholipase A2 type II binds to extracellular matrix biglycan: modulation of its activity on LDL by colocalization in glycosaminoglycan matrixes |journal=Arterioscler. Thromb. Vasc. Biol. |volume=18 |issue= 12 |pages= 1934–41 |year= 1999 |pmid= 9848887 |doi=  10.1161/01.ATV.18.12.1934}}
*{{cite journal  | author= |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097-108 |year= 1999 |pmid= 9847074 |doi=  }}
*{{cite journal  | author=Sartipy P, Bondjers G, Hurt-Camejo E |title=Phospholipase A2 type II binds to extracellular matrix biglycan: modulation of its activity on LDL by colocalization in glycosaminoglycan matrixes. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=18 |issue= 12 |pages= 1934-41 |year= 1999 |pmid= 9848887 |doi=  }}
}}
}}
{{refend}}
{{refend}}


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Latest 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

Phospholipase A2, group 1B is an enzyme that in humans is encoded by the PLA2G1B gene.[1][2]

Function

Phospholipase A2 (EC 3.1.1.4) catalyzes the release of fatty acids from glycero-3-phosphocholines. The best known varieties are the digestive enzymes secreted as zymogens by the pancreas of mammals as well as fish.[3] Sequences of pancreatic PLA2 enzymes from a variety of mammals have been reported. One striking feature of these enzymes is their close homology to venom phospholipases of snakes. Other forms of PLA2 have been isolated from brain, liver, lung, spleen, intestine, macrophages, leukocytes, erythrocytes, inflammatory exudates, chondrocytes, and platelets (Seilhamer et al., 1986) .[2][4]

References

  1. ↑ Dennis EA (Jun 1994). "Diversity of group types, regulation, and function of phospholipase A2". J Biol Chem. 269 (18): 13057–60. PMID 8175726.
  2. ↑ 2.0 2.1 "Entrez Gene: PLA2G1B phospholipase A2, group IB (pancreas)".
  3. ↑ Sæle O, Nordgreen A, Olsvik PA, Hamre K (2010). "Characterisation and expression of secretory phospholipase A2 group IB during ontogeny of Atlantic cod ( Gadus morhua)". Br J Nutr. 105 (2): 1–10. doi:10.1017/S0007114510003466. PMID 20836903.
  4. ↑ Seilhamer JJ, Randall TL, Yamanaka M, Johnson LK (1987). "Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung". DNA. 5 (6): 519–27. doi:10.1089/dna.1.1986.5.519. PMID 3028739.

Further reading



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