Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

Phospholipase A2

Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_4538-2

Definition

Phospholipase A 2 (PLA 2) enzymes are a family of proteins, and to date, at least 20 members have been identified in mammals. The family can be classified into four classes on the basis of their nucleotide and amino acid sequence homology:
  • First, there are at present ten secreted phospholipase A2 enzymes (sPLA2-IB, sPLA2-IIA, sPLA2-IIC, sPLA2-IID, sPLA2-IIE, sPLA2-IIF, sPLA2-III, sPLA2-V, sPLA2-X, and sPLA2-XII), which are of low molecular weight (13–18 kDa) with a catalytic histidine in their active site and a requirement for calcium for enzyme activity.

  • Second, there are three characterized human cytosolic PLA2 enzymes (cPLA2-α, cPLA2-β, and cPLA2-γ, also known as Group IVA, IVB, and IVC PLA2) that use a catalytic serine in their active site. cPLA2-α and cPLA2-β contain a C2 calcium-binding domain, and enzyme activity is calcium dependent, while cPLA2-γ lacks this domain and is thus a calcium-independent PLA2. Recently, a comprehensive homology search against the murine...

Keywords

Arachidonic Acid Arachidonic Acid Release Hydroxyeicosatetraenoic Acid Eicosanoid Synthesis Epoxyeicosatrienoic Acid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

  1. Chakraborti S (2003) Phospholipase A2 isoforms: a perspective. Cell Signal 15:637–665PubMedCrossRefGoogle Scholar
  2. Hua S et al (2013) Cytosolic phospholipase A2α sustains pAKT, pERK and AR levels in PTEN-null/mutated prostate cancer cells. Biochim Biophys Acta 1831:1146–1157PubMedCrossRefGoogle Scholar
  3. Murakami M, Kudo I (2002) Phospholipase A2. J Biochem 131:285–292PubMedCrossRefGoogle Scholar
  4. Six DA, Dennis EA (2000) The expanding superfamily of phospholipase A2 enzymes: classification and characterization. Biochim Biophys Acta 1488:1–19PubMedCrossRefGoogle Scholar
  5. Vignarajan S et al (2014) Loss of PTEN stabilizes the lipid modifying enzyme cytosolic phospholipase A2α via AKT in prostate cancer cells. Oncotarget 5:6289–6299PubMedPubMedCentralCrossRefGoogle Scholar
  6. Zheng Z et al (2014) Targeting cytosolic phospholipase A2 α in colorectal cancer cells inhibits constitutively activated protein kinase B (AKT) and cell proliferation. Oncotarget 5:12304–12316PubMedPubMedCentralCrossRefGoogle Scholar

See Also

  1. (2012) MAPK. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer, Berlin Heidelberg, p 2167. doi: 10.1007/978-3-642-16483-5_3532.Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  1. 1.The University of Western SydneySydneyAustralia
  2. 2.Department of Endocrinology, Central Clinical School, Royal Prince Alfred HospitalThe University of SydneySydneyAustralia