PMID- 10359651 OWN - NLM STAT- MEDLINE DCOM- 19990802 LR - 20181113 IS - 0264-6021 (Print) IS - 0264-6021 (Linking) VI - 340 ( Pt 3) DP - 1999 Jun 15 TI - Lipid phosphate phosphohydrolase-1 degrades exogenous glycerolipid and sphingolipid phosphate esters. PG - 677-86 AB - Lipid phosphate phosphohydrolase (LPP)-1 cDNA was cloned from a rat liver cDNA library. It codes for a 32-kDa protein that shares 87 and 82% amino acid sequence identities with putative products of murine and human LPP-1 cDNAs, respectively. Membrane fractions of rat2 fibroblasts that stably expressed mouse or rat LPP-1 exhibited 3.1-3. 6-fold higher specific activities for phosphatidate dephosphorylation compared with vector controls. Increases in the dephosphorylation of lysophosphatidate, ceramide 1-phosphate, sphingosine 1-phosphate and diacylglycerol pyrophosphate were similar to those for phosphatidate. Rat2 fibroblasts expressing mouse LPP-1 cDNA showed 1.6-2.3-fold increases in the hydrolysis of exogenous lysophosphatidate, phosphatidate and ceramide 1-phosphate compared with vector control cells. Recombinant LPP-1 was located partially in plasma membranes with its C-terminus on the cytosolic surface. Lysophosphatidate dephosphorylation was inhibited by extracellular Ca2+ and this inhibition was diminished by extracellular Mg2+. Changing intracellular Ca2+ concentrations did not alter exogenous lysophosphatidate dephosphorylation significantly. Permeabilized fibroblasts showed relatively little latency for the dephosphorylation of exogenous lysophosphatidate. LPP-1 expression decreased the activation of mitogen-activated protein kinase and DNA synthesis by exogenous lysophosphatidate. The product of LPP-1 cDNA is concluded to act partly to degrade exogenous lysophosphatidate and thereby regulate its effects on cell signalling. FAU - Jasinska, R AU - Jasinska R AD - Department of Biochemistry (Signal Transduction Laboratories), Lipid and Lipoprotein Research Group, University of Alberta, 357 Heritage Medical Research Centre, Edmonton, Alberta, T6G 2S2, Canada. FAU - Zhang, Q X AU - Zhang QX FAU - Pilquil, C AU - Pilquil C FAU - Singh, I AU - Singh I FAU - Xu, J AU - Xu J FAU - Dewald, J AU - Dewald J FAU - Dillon, D A AU - Dillon DA FAU - Berthiaume, L G AU - Berthiaume LG FAU - Carman, G M AU - Carman GM FAU - Waggoner, D W AU - Waggoner DW FAU - Brindley, D N AU - Brindley DN LA - eng GR - R01 GM028140/GM/NIGMS NIH HHS/United States GR - GM-28140/GM/NIGMS NIH HHS/United States PT - Journal Article PT - Research Support, Non-U.S. Gov't PT - Research Support, U.S. Gov't, P.H.S. PL - England TA - Biochem J JT - The Biochemical journal JID - 2984726R RN - 0 (Esters) RN - 0 (Glycolipids) RN - 0 (Lysophospholipids) RN - 0 (Phosphates) RN - 0 (Recombinant Fusion Proteins) RN - 0 (Sphingolipids) RN - 0 (glycerolglycolipids) RN - 9007-49-2 (DNA) RN - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases) RN - EC 3.1.3.- (lipid phosphate phosphatase) RN - EC 3.1.3.2 (Phosphoric Monoester Hydrolases) RN - EC 3.1.3.4 (Phosphatidate Phosphatase) RN - SY7Q814VUP (Calcium) SB - IM MH - Animals MH - Calcium/pharmacology MH - Calcium-Calmodulin-Dependent Protein Kinases/metabolism MH - Cell Line MH - Cell Membrane/enzymology MH - Cell Membrane Permeability MH - DNA/biosynthesis MH - Enzyme Activation/drug effects MH - Esters/*metabolism MH - Glycolipids/*metabolism MH - Humans MH - Hydrolysis/drug effects MH - Kinetics MH - Lysophospholipids/metabolism/pharmacology MH - Mice MH - Phosphates/*metabolism MH - Phosphatidate Phosphatase/chemistry/genetics/*metabolism MH - Phosphoric Monoester Hydrolases/chemistry/genetics/*metabolism MH - Phosphorylation/drug effects MH - Rats MH - Recombinant Fusion Proteins/analysis/biosynthesis/metabolism MH - Sphingolipids/*metabolism MH - Substrate Specificity PMC - PMC1220298 EDAT- 1999/06/09 00:00 MHDA- 1999/06/09 00:01 CRDT- 1999/06/09 00:00 PHST- 1999/06/09 00:00 [pubmed] PHST- 1999/06/09 00:01 [medline] PHST- 1999/06/09 00:00 [entrez] PST - ppublish SO - Biochem J. 1999 Jun 15;340 ( Pt 3):677-86.