PLA2G1B

Phospholipase A2, group IB (pancreas)
Rendering based on PDB 1YSK​.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1YSK​, 3ELO​
Identifiers
Symbols	PLA2G1B ; PLA2; PLA2A; PPLA2
External IDs	OMIM: 172410 MGI: 101842 HomoloGene: 715 ChEMBL: 4426 GeneCards: PLA2G1B Gene
EC number	3.1.1.4
Gene ontology Molecular function • phospholipase A2 activity • receptor binding • calcium ion binding • bile acid binding • calcium-dependent phospholipase A2 activity Cellular component • extracellular region • extracellular space • cell surface • secretory granule Biological process • activation of MAPK activity • innate immune response in mucosa • neutrophil mediated immunity • fatty acid biosynthetic process • phospholipid metabolic process • phosphatidic acid biosynthetic process • actin filament organization • signal transduction • positive regulation of calcium ion transport into cytosol • glucose transport • leukotriene biosynthetic process • antibacterial humoral response • neutrophil chemotaxis • activation of phospholipase A2 activity • interleukin-8 production • cellular response to insulin stimulus • intracellular signal transduction • phosphatidylglycerol acyl-chain remodeling • phosphatidylinositol acyl-chain remodeling • phosphatidylserine acyl-chain remodeling • phosphatidylcholine acyl-chain remodeling • phosphatidylethanolamine acyl-chain remodeling • multicellular organismal lipid catabolic process • small molecule metabolic process • positive regulation of DNA replication • positive regulation of transcription from RNA polymerase II promoter • phosphatidylcholine metabolic process • glycerophospholipid biosynthetic process • positive regulation of fibroblast proliferation • arachidonic acid secretion • positive regulation of protein secretion • positive regulation of immune response • defense response to Gram-positive bacterium • positive regulation of NF-kappaB transcription factor activity Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5319	18778
Ensembl	ENSG00000170890	ENSMUSG00000029522
UniProt	P04054	Q9Z0Y2
RefSeq (mRNA)	NM_000928	NM_011107
RefSeq (protein)	NP_000919	NP_035237
Location (UCSC)	Chr 12: 120.32 – 120.33 Mb	Chr 5: 115.47 – 115.47 Mb
PubMed search

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. "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

• 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.
• Sapirstein A, Bonventre JV (2000). "Phospholipases A2 in ischemic and toxic brain injury". Neurochem. Res. 25 (5): 745–53. doi:10.1023/A:1007583708713. PMID 10905638.
• Svensson CI, Yaksh TL (2002). "The spinal phospholipase-cyclooxygenase-prostanoid cascade in nociceptive processing". Annu. Rev. Pharmacol. Toxicol. 42: 553–83. doi:10.1146/annurev.pharmtox.42.092401.143905. PMID 11807183.
• Clark MA, Ozgür LE, Conway TM, et al. (1991). "Cloning of a phospholipase A2-activating protein". Proc. Natl. Acad. Sci. U.S.A. 88 (12): 5418–22. doi:10.1073/pnas.88.12.5418. PMC 51884. PMID 2052621.
• Verheij HM, Westerman J, Sternby B, De Haas GH (1983). "The complete primary structure of phospholipase A2 from human pancreas". Biochim. Biophys. Acta 747 (1–2): 93–9. doi:10.1016/0167-4838(83)90126-7. PMID 6349696.
• Sternby B, Akerström B (1984). "Immunoreactive pancreatic colipase, lipase and phospholipase A2 in human plasma and urine from healthy individuals". Biochim. Biophys. Acta 789 (2): 164–9. doi:10.1016/0167-4838(84)90201-2. PMID 6477929.
• Grataroli R, Dijkman R, Dutilh CE, et al. (1982). "Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region". Eur. J. Biochem. 122 (1): 111–7. doi:10.1111/j.1432-1033.1982.tb05855.x. PMID 7060561.
• Rönkkö S (1995). "Immunohistochemical localization of phospholipase A2 in human and bovine male reproductive organs". Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 110 (3): 503–9. doi:10.1016/0305-0491(94)00190-6. PMID 7584826.
• Lilja I, Smedh K, Olaison G, et al. (1995). "Phospholipase A2 gene expression and activity in histologically normal ileal mucosa and in Crohn's ileitis". Gut 37 (3): 380–5. doi:10.1136/gut.37.3.380. PMC 1382819. PMID 7590434.
• Ancian P, Lambeau G, Mattéi MG, Lazdunski M (1995). "The human 180-kDa receptor for secretory phospholipases A2. Molecular cloning, identification of a secreted soluble form, expression, and chromosomal localization". J. Biol. Chem. 270 (15): 8963–70. doi:10.1074/jbc.270.15.8963. PMID 7721806.
• Chen J, Engle SJ, Seilhamer JJ, Tischfield JA (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.
• Gispert S, Twells R, Orozco G, et al. (1993). "Chromosomal assignment of the second locus for autosomal dominant cerebellar ataxia (SCA2) to chromosome 12q23-24.1". Nat. Genet. 4 (3): 295–9. doi:10.1038/ng0793-295. PMID 8358438.
• Cupillard L, Koumanov K, Mattéi MG, et al. (1997). "Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2". J. Biol. Chem. 272 (25): 15745–52. doi:10.1074/jbc.272.25.15745. PMID 9188469.
• 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.
• "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. 1999. doi:10.1101/gr.8.11.1097. PMID 9847074.
• Sartipy P, Bondjers G, Hurt-Camejo E (1999). "Phospholipase A2 type II binds to extracellular matrix biglycan: modulation of its activity on LDL by colocalization in glycosaminoglycan matrixes". Arterioscler. Thromb. Vasc. Biol. 18 (12): 1934–41. doi:10.1161/01.ATV.18.12.1934. PMID 9848887.