The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

PPAP2A  -  phosphatidic acid phosphatase type 2A

Homo sapiens

Synonyms: LLP1a, LPP1, Lipid phosphate phosphohydrolase 1, PAP-2a, PAP2, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of PPAP2A


High impact information on PPAP2A


Chemical compound and disease context of PPAP2A


Biological context of PPAP2A


Anatomical context of PPAP2A

  • Pulmonary lipid phosphate phosphohydrolase (LPP) was shown previously to hydrolyze phosphatidic acid and lysophosphatidic acid in purified rat lung plasma membranes [10].
  • PAP-2b was expressed almost ubiquitously in all human tissues examined, whereas the expression of PAP-2a was relatively variable, being extremely low in the placenta and thymus [14].
  • In HeLa cells, the transcription of PAP-2a was not affected by different stimuli, whereas PAP-2b was induced (up to 3-fold) by epidermal growth factor [14].
  • Here, we demonstrate the presence of a Mg(2+)-independent and N-ethymaleimide-insensitive PAP2 activity in cultured guinea-pig airway smooth muscle (ASM) cells [12].
  • Transient expression of gpPAP2a2 in Cos-7 cells resulted in an approx. 4-fold increase in Mg(2+)-independent PAP activity, thereby confirming that gpPAP2a2 is another catalytically active member of an extended PAP2 family [12].

Associations of PPAP2A with chemical compounds

  • Members of the type 2 phosphatidic acid phosphatase (PAP2) family catalyse the dephosphorylation of phosphatidic acid (PA), lysophosphatidate and sphingosine 1-phosphate [12].
  • A 322-base pair cDNA fragment that was consistently induced by the synthetic androgen R1881 revealed 100% homology with the human phosphatidic acid phosphatase type 2a isozyme very recently reported by Kai et al [1].
  • Induction of PAP-2a mRNA was not affected by the protein synthesis inhibitor cycloheximide and was accompanied by a marked increase in PAP-2 activity as measured by the conversion of phosphatidic acid into diacylglycerol in membrane fractions of LNCaP [1].
  • The steroid specificity of PAP-2a mRNA regulation was found to be in agreement with the aberrant ligand specificity of the mutated androgen receptor in LNCaP cells, supporting the involvement of the androgen receptor in the induction process [1].
  • LPP is Mg(2+) independent and sulfhydryl reagent insensitive [15].

Other interactions of PPAP2A

  • The pulmonary LPP1 and LPP3 isoforms are essentially identical to the previously cloned rat liver and intestinal LPPs, respectively, and the LPP1a isoform has 80% sequence identity to the human homolog [10].
  • Other significant differences between gpPAP2a1/2 and hPAP2a, hPAP2b and hPAP2c occur at the cytoplasmic C-terminal [12].
  • Furthermore, low basal levels of PAP-2a mRNA and absence of androgen inducibility were observed in the poorly differentiated and androgen receptor-negative cell lines PC-3 and DU-145 [1].
  • Two isoforms, presumed to be alternative splice variants from a single gene, designated as PAP2-alpha1 and PAP2-alpha2, have been cloned and expressed [16].
  • The expression of phosphatidic acid phosphatase 2a, which hydrolyzes lipids to generate diacylglycerol, is regulated by p73, a member of the p53 family [17].

Analytical, diagnostic and therapeutic context of PPAP2A

  • To better investigate the nature of pulmonary LPP isoforms and their role in the lung, LPPs were cloned by RT-PCR from both adult rat lung and type II cell RNA [10].
  • The inducibility of PAP-2a mRNA by androgens was confirmed by Northern blot hybridization [1].


  1. Identification of the phosphatidic acid phosphatase type 2a isozyme as an androgen-regulated gene in the human prostatic adenocarcinoma cell line LNCaP. Ulrix, W., Swinnen, J.V., Heyns, W., Verhoeven, G. J. Biol. Chem. (1998) [Pubmed]
  2. Role of decreased levels of lipid phosphate phosphatase-1 in accumulation of lysophosphatidic acid in ovarian cancer. Tanyi, J.L., Hasegawa, Y., Lapushin, R., Morris, A.J., Wolf, J.K., Berchuck, A., Lu, K., Smith, D.I., Kalli, K., Hartmann, L.C., McCune, K., Fishman, D., Broaddus, R., Cheng, K.W., Atkinson, E.N., Yamal, J.M., Bast, R.C., Felix, E.A., Newman, R.A., Mills, G.B. Clin. Cancer Res. (2003) [Pubmed]
  3. Activated ras regulates the proliferation/apoptosis balance and early survival of developing micrometastases. Varghese, H.J., Davidson, M.T., MacDonald, I.C., Wilson, S.M., Nadkarni, K.V., Groom, A.C., Chambers, A.F. Cancer Res. (2002) [Pubmed]
  4. Three-dimensional high-frequency ultrasound imaging for longitudinal evaluation of liver metastases in preclinical models. Graham, K.C., Wirtzfeld, L.A., MacKenzie, L.T., Postenka, C.O., Groom, A.C., MacDonald, I.C., Fenster, A., Lacefield, J.C., Chambers, A.F. Cancer Res. (2005) [Pubmed]
  5. Lipid Phosphate Phosphatase-1 Regulates Lysophosphatidate-induced Fibroblast Migration by Controlling Phospholipase D2-dependent Phosphatidate Generation. Pilquil, C., Dewald, J., Cherney, A., Gorshkova, I., Tigyi, G., English, D., Natarajan, V., Brindley, D.N. J. Biol. Chem. (2006) [Pubmed]
  6. lazaro encodes a lipid phosphate phosphohydrolase that regulates phosphatidylinositol turnover during Drosophila phototransduction. Garcia-Murillas, I., Pettitt, T., Macdonald, E., Okkenhaug, H., Georgiev, P., Trivedi, D., Hassan, B., Wakelam, M., Raghu, P. Neuron (2006) [Pubmed]
  7. Identification and functional characterization of a presqualene diphosphate phosphatase. Fukunaga, K., Arita, M., Takahashi, M., Morris, A.J., Pfeffer, M., Levy, B.D. J. Biol. Chem. (2006) [Pubmed]
  8. Lipid phosphate phosphatases regulate lysophosphatidic acid production and signaling in platelets: studies using chemical inhibitors of lipid phosphate phosphatase activity. Smyth, S.S., Sciorra, V.A., Sigal, Y.J., Pamuklar, Z., Wang, Z., Xu, Y., Prestwich, G.D., Morris, A.J. J. Biol. Chem. (2003) [Pubmed]
  9. Sensitization of algal virus to UV by the incorporation of 5-bromouracil and mutations of host alga Plectonema boryanum. Singh, P.K. Z. Allg. Mikrobiol. (1975) [Pubmed]
  10. Molecular cloning and expression of pulmonary lipid phosphate phosphohydrolases. Nanjundan, M., Possmayer, F. Am. J. Physiol. Lung Cell Mol. Physiol. (2001) [Pubmed]
  11. Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. Roberts, R., Sciorra, V.A., Morris, A.J. J. Biol. Chem. (1998) [Pubmed]
  12. Molecular cloning of magnesium-independent type 2 phosphatidic acid phosphatases from airway smooth muscle. Tate, R.J., Tolan, D., Pyne, S. Cell. Signal. (1999) [Pubmed]
  13. Identification of a novel human phosphatidic acid phosphatase type 2 isoform. Hooks, S.B., Ragan, S.P., Lynch, K.R. FEBS Lett. (1998) [Pubmed]
  14. Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. Kai, M., Wada, I., Imai, S., Sakane, F., Kanoh, H. J. Biol. Chem. (1997) [Pubmed]
  15. Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase. Nanjundan, M., Possmayer, F. Am. J. Physiol. Lung Cell Mol. Physiol. (2003) [Pubmed]
  16. Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. Leung, D.W., Tompkins, C.K., White, T. DNA Cell Biol. (1998) [Pubmed]
  17. The expression of phosphatidic acid phosphatase 2a, which hydrolyzes lipids to generate diacylglycerol, is regulated by p73, a member of the p53 family. Ishida, T., Iwai, A., Hijikata, M., Shimotohno, K. Biochem. Biophys. Res. Commun. (2007) [Pubmed]
WikiGenes - Universities