Phospholipids are the basic barrier components of membranes in eukaryotic cells divided into glycerophospholipids (phosphatidic acid, phosphatidylethanolamine, phosphatidylcholine, phosphatidylserine, phosphatidylinositol and its phosphorylated derivatives) and sphingolipids (ceramide phosphorylcholine and ceramide phosphorylethanolamine).
Phosphoinositide-specific phospholipase C
Phosphoinositide-specific phospholipase C (PLC) catalyses the hydrolysis of PIP2 to IP3 and 1,2-diacylglycerol, each of which have major second messenger functions. Two domains, X and Y, essential for catalytic activity, are conserved in the different forms of PLC. Isoforms of PLC-β (ENSFM00270000056436) are activated primarily by G protein-coupled receptors through members of the Gq/11 family of G proteins. The receptor-mediated activation of PLC-γ involves their phosphorylation by receptor tyrosine kinases (RTK) in response to activation of a variety of growth factor receptors and immune system receptors. PLC-ε1 may represent a point of convergence of signalling via both G protein-coupled and catalytic receptors. Ca2+ ions are required for catalytic activity of PLC isoforms and have been suggested to be the major physiological form of regulation of PLC-δ activity. PLC has been suggested to be activated non-selectively by the small molecule m3M3FBS [3], although this mechanism of action has been questioned [16]. The aminosteroid U73122 has been described as an inhibitor of phosphoinositide-specific PLC [34], although its selectivity among the isoforms is untested and it has been reported to occupy the H1 histamine receptor [12].
Unless otherwise stated all data refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).
Enzymes 
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A series of PLC-like proteins (PLCL1 ENSG00000115896; PLCL2 ENSG00000154822 and PLCL3 ENSG00000114805) form a family (ENSF00000000386) with PLCδ and PLCζ1 isoforms, but appear to lack catalytic activity.
PLC-δ2 has been cloned from bovine sources [22].
Phospholipase A2
Phospholipase A2 (PLA2) cleaves the sn-2 fatty acid of phospholipids, primarily phosphatidylcholine, to generate lysophosphatidylcholine and arachidonic acid. Most commonly-used inhibitors (e.g. BEL, ATFMK or MAFP) are either non-selective within the family of phospholipase A2 enzymes or have activity against other eicosanoid-metabolising enzymes.
Secreted or extracellular forms: sPLA2-1B, sPLA2-2A, sPLA2-2D, sPLA2-2E, sPLA2-2F, sPLA2-3, sPLA2-10 and sPLA2-12A
Cytosolic, calcium-dependent forms: cPLA2-4A, cPLA2-4B, cPLA2-4C, cPLA2-4D, cPLA2-4E and cPLA2-4F
Other forms: PLA2-G5, iPLA2-G6 and PLA2-G7
Unless otherwise stated all data refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).
Enzymes
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PLA2-2C (ENSG00000187980) may be a pseudogene, while PLA2-12B (GXIIB, GXIII sPLA2-like, ENSG00000138308) appears to be catalytically inactive [31]. A further fragment has been identified with sequence similarities to Group II PLA2 members (ENSG00000187980).
A binding protein for secretory phospholipase A2 has been identified (ENSG00000153246) which shows modest selectivity for sPLA2-1B over sPLA2-2A, and also binds snake toxin phospholipase A2 [1]. The binding protein appears to have clearance function for circulating secretory phospholipase A2, as well as signalling functions, and is a candidate antigen for idiopathic membraneous nephropathy [4].
PLA2-G7 and a close homologue (HSD-PLA2, also known as serine-dependent phospholipase A2, PAFAH2, ENSG00000158006) also express platelet-activating factor acetylhydrolase activity (EC 3.1.1.47). Otoconin 90 (OC90, ENSG00000132297) shows sequence homology to PLA2-G10.
Phosphatidylcholine-specific phospholipase D
Phosphatidylcholine-specific phospholipase D (PLD, ENSFM00250000001375) catalyses the formation of phosphatidic acid from phosphatidylcholine. In addition, the enzyme can make use of alcohols, such as butanol in a transphosphatidylation reaction [30].
Unless otherwise stated all data refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).
Enzymes
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A lysophospholipase D activity (ENPP2, ENSG00000136960, also known as ectonucleotide pyrophosphatase/phosphodiesterase 2, phosphodiesterase I, nucleotide pyrophosphatase 2, autotaxin) has been described, which not only catalyses the production of lysophosphatidic acid (LPA) from lysophosphatidylcholine, but also cleaves ATP (see Goding et al., 2003 [7]). Additionally, an N-acylethanolamine-specific phospholipase D (NAPE-PLD, ENSG00000161048) has been characterized, which appears to have a role in the generation of endocannabinoids/endovanilloids, including anandamide [24]. This enzyme activity appears to be enhanced by polyamines in the physiological range [19] and fails to transphosphatidylate with alcohols [27].
Lipid phosphate phosphatases
Lipid phosphate phosphatases, divided into phosphatidic acid phosphatases (ENSFM00260000050433) or lipins (ENSFM00250000001227), catalyse the dephosphorylation of phosphatidic acid to generate inorganic phosphate and diacylglycerol.
Unless otherwise stated all data refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).
Enzymes
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Pyne, S; Lee, SC; Long, J; Pyne, NJ. (2009) Role of sphingosine kinases and lipid phosphate phosphatases in regulating spatial sphingosine 1-phosphate signalling in health and disease. Cell. Signal., 21 (1): 14-21. [PMID:18768158]
Qin, H; Zheng, X; Zhong, X; Shetty, AK; Elias, PM; Bollag, WB. (2011) Aquaporin-3 in keratinocytes and skin: its role and interaction with phospholipase D2. Arch. Biochem. Biophys., 508 (2): 138-43. [PMID:21276418]
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