PPAP2A

Lipid phosphate phosphohydrolase 1 is a member of the phosphatidic acid phosphatase (PAP) family. PAPs convert phosphatidic acid to diacylglycerol, and function in de novo synthesis of glycerolipids as well as in receptor-activated signal transduction mediated by phospholipase D. This protein is an integral membrane glycoprotein, and has been shown to be a surface enzyme that plays an active role in the hydrolysis and uptake of lipids from extracellular space. The expression of this gene is found to be regulated by androgen in a prostatic adenocarcinoma cell line. At least two alternatively spliced transcript variants encoding distinct isoforms have been described.

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• {{cite journal |vauthors=Kanoh H, Kai M, Wada I |title=Molecular characterization of the type 2 phosphatidic acid phosphatase |journal=Chem. Phys. Lipids |volume=98 |issue= 1–2 |pages= 119–126 |year= 1999 |pmid= 10358934 |doi=10.1016/S0009-3084(99)00024-9 }}
• {{cite journal |vauthors=Nanjundan M, Possmayer F |title=Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase |journal=Am. J. Physiol. Lung Cell Mol. Physiol. |volume=284 |issue= 1 |pages= L1–23 |year= 2003 |pmid= 12471011 |doi= 10.1152/ajplung.00029.2002 }}
• {{cite journal |vauthors=Ulrix W, Swinnen JV, Heyns W, Verhoeven G |title=Identification of the phosphatidic acid phosphatase type 2a isozyme as an androgen-regulated gene in the human prostatic adenocarcinoma cell line LNCaP |journal=J. Biol. Chem. |volume=273 |issue= 8 |pages= 4660–4665 |year= 1998 |pmid= 9468526 |doi=10.1074/jbc.273.8.4660 |doi-access=free }}
• {{cite journal |vauthors=Leung DW, Tompkins CK, White T |title=Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells |journal=DNA Cell Biol. |volume=17 |issue= 4 |pages= 377–385 |year= 1998 |pmid= 9570154 |doi=10.1089/dna.1998.17.377 }}
• {{cite journal |vauthors=Hooks SB, Ragan SP, Lynch KR |title=Identification of a novel human phosphatidic acid phosphatase type 2 isoform |journal=FEBS Lett. |volume=427 |issue= 2 |pages= 188–192 |year= 1998 |pmid= 9607309 |doi=10.1016/S0014-5793(98)00421-9 |s2cid=31610109 }}
• {{cite journal |vauthors=Roberts R, Sciorra VA, Morris AJ |title=Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform |journal=J. Biol. Chem. |volume=273 |issue= 34 |pages= 22059–22067 |year= 1998 |pmid= 9705349 |doi=10.1074/jbc.273.34.22059 |doi-access=free }}
• {{cite journal | author=Neumann J |title=Pharmacological characterization of protein phosphatase activities in preparations from failing human hearts |journal=J. Pharmacol. Exp. Ther. |volume=289 |issue= 1 |pages= 188–93 |year= 1999 |pmid= 10087003 |name-list-style=vanc| author2=Maas R | author3=Bokník P | display-authors=3 | last4=Jones | first4=LR | last5=Zimmermann | first5=N | last6=Scholz | first6=H }}
• {{cite journal | author=Moreno CS |title=WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A |journal=J. Biol. Chem. |volume=275 |issue= 8 |pages= 5257–5263 |year= 2000 |pmid= 10681496 |doi=10.1074/jbc.275.8.5257 |name-list-style=vanc| author2=Park S | author3=Nelson K | display-authors=3 | last4=Ashby | first4=D | last5=Hubalek | first5=F | last6=Lane | first6=WS | last7=Pallas | first7=DC | pmc=3505218|doi-access=free }}
• {{cite journal |vauthors=Roberts RZ, Morris AJ |title=Role of phosphatidic acid phosphatase 2a in uptake of extracellular lipid phosphate mediators |journal=Biochim. Biophys. Acta |volume=1487 |issue= 1 |pages= 33–49 |year= 2001 |pmid= 10962286 |doi= 10.1016/s1388-1981(00)00081-0}}
• {{cite journal | author=Woetmann A |title=Protein phosphatase 2A (PP2A) regulates interleukin-4-mediated STAT6 signaling |journal=J. Biol. Chem. |volume=278 |issue= 5 |pages= 2787–2791 |year= 2003 |pmid= 12426308 |doi= 10.1074/jbc.M210196200 |name-list-style=vanc| author2=Brockdorff J | author3=Lovato P | display-authors=3 | last4=Nielsen | first4=M. | last5=Leick | first5=V. | last6=Rieneck | first6=K. | last7=Svejgaard | first7=A. | last8=Geisler | first8=C. | last9=Odum | first9=N. | doi-access=free }}
• {{cite journal |vauthors=Pandey AV, Mellon SH, Miller WL |title=Protein phosphatase 2A and phosphoprotein SET regulate androgen production by P450c17 |journal=J. Biol. Chem. |volume=278 |issue= 5 |pages= 2837–2844 |year= 2003 |pmid= 12444089 |doi= 10.1074/jbc.M209527200 |doi-access= free }}
• {{cite journal | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–16903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |name-list-style=vanc| author2=Feingold EA | author3=Grouse LH | display-authors=3 | last4=Derge | first4=JG | last5=Klausner | first5=RD | last6=Collins | first6=FS | last7=Wagner | first7=L | last8=Shenmen | first8=CM | last9=Schuler | first9=GD |bibcode=2002PNAS...9916899M |doi-access=free }}
• {{cite journal | author=Smyth SS |title=Lipid phosphate phosphatases regulate lysophosphatidic acid production and signaling in platelets: studies using chemical inhibitors of lipid phosphate phosphatase activity |journal=J. Biol. Chem. |volume=278 |issue= 44 |pages= 43214–43223 |year= 2003 |pmid= 12909631 |doi= 10.1074/jbc.M306709200 |name-list-style=vanc| author2=Sciorra VA | author3=Sigal YJ | display-authors=3 | last4=Pamuklar | first4=Z | last5=Wang | first5=Z | last6=Xu | first6=Y | last7=Prestwich | first7=GD | last8=Morris | first8=AJ | doi-access=free }}
• {{cite journal | author=Tanyi JL |title=Role of decreased levels of lipid phosphate phosphatase-1 in accumulation of lysophosphatidic acid in ovarian cancer |journal=Clin. Cancer Res. |volume=9 |issue= 10 Pt 1 |pages= 3534–45 |year= 2004 |pmid= 14506139 |name-list-style=vanc| author2=Hasegawa Y | author3=Lapushin R | display-authors=3 | last4=Morris | first4=AJ | last5=Wolf | first5=JK | last6=Berchuck | first6=A | last7=Lu | first7=K | last8=Smith | first8=DI | last9=Kalli | first9=K }}
• {{cite journal | author=Gerhard DS |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–2127 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |name-list-style=vanc| author2=Wagner L | author3=Feingold EA | display-authors=3 | last4=Shenmen | first4=CM | last5=Grouse | first5=LH | last6=Schuler | first6=G | last7=Klein | first7=SL | last8=Old | first8=S | last9=Rasooly | first9=R }}
• {{cite journal |vauthors=Grkovich A, Johnson CA, Buczynski MW, Dennis EA |title=Lipopolysaccharide-induced cyclooxygenase-2 expression in human U937 macrophages is phosphatidic acid phosphohydrolase-1-dependent |journal=J. Biol. Chem. |volume=281 |issue= 44 |pages= 32978–32987 |year= 2006 |pmid= 16950767 |doi= 10.1074/jbc.M605935200 |doi-access= free }}
• {{cite journal | author=Kai M |title=Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid rafts |journal=J. Biochem. |volume=140 |issue= 5 |pages= 677–686 |year= 2007 |pmid= 17005594 |doi= 10.1093/jb/mvj195 |name-list-style=vanc| author2=Sakane F | author3=Jia YJ | display-authors=3 | last4=Imai | first4=S.-i. | last5=Yasuda | first5=S. | last6=Kanoh | first6=H. }}

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