Disease relevance of Lypla1

• The rat CaIPLA2 cDNA, when expressed in a baculovirus expression system, and the purified rabbit kidney cortex protein exhibit both CaIPLA2 and lysophospholipase activities [1].

High impact information on Lypla1

• Recombinant autotaxin was found to have lysophospholipase D activity; its substrate specificity and metal ion requirement were the same as those of the purified plasma enzyme [2].
• The activity of lysophospholipase D for exogenous lysophosphatidylcholine in human serum was found to increase in normal pregnant women at the third trimester of pregnancy and to a higher extent in patients in threatened preterm delivery, suggesting its roles in induction of parturition [2].
• We now show that the newly characterized acyl-protein thioesterase 1 (APT1) regulates eNOS depalmitoylation [3].
• Immunoblot analyses indicate that APT1 is expressed in bovine aortic endothelial cells, which express eNOS [3].
• Additionally, purified recombinant APT1 depalmitoylates eNOS assayed in biological membranes isolated from endothelial cells biosynthetically labeled with [(3)H]palmitate or COS-7 cells transfected with eNOS cDNA [3].

Biological context of Lypla1

• This lysophospholipase catalysed the hydrolysis of a variety of lysophosphatidic acids, but with different rates, depending on the length and degree of saturation of the sn-1 acyl group (1-oleoyl-LPA approximately 1-stearoyl-LPA > 1-palmitoyl-LPA > 1-myristoyl-LPA) [4].
• Total activities of lysophospholipase and acylation enzymes of lysophospholipid demonstrated 1.5-and 2.2-fold increase during 30-min recirculation [5].
• Induction of lipid peroxidation is shown to alter the structure of mitochondrial membrane and to activate endogenous phospholipases A2, C, D, and lysophospholipase A [6].

Anatomical context of Lypla1

• Previous studies have shown the high lysophospholipase activity of rat eosinophilic leukocytes and used this enzyme to measure the rise in eosinophilic population of peripheral tissues caused by parasitic infections [7].
• 2-acyl-sn-glycero-3-phosphoethanolamine lysophospholipase A2 activity in guinea-pig heart microsomes [8].
• PLA2/lysophospholipase activity was found in homogenates from rat right ventricles [9].
• L-ET-18-OCH3 was not hydrolyzed by lysophospholipase D from rat liver microsomes under conditions where cleavage of 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine was observed [10].
• However, similar experiments with rat kidney cytosol and rat and human platelet cytosol clearly separated lysophospholipase activities without PAF acetylhydrolase activity from specific PAF acetylhydrolases not having lysophospholipase activity [11].

Associations of Lypla1 with chemical compounds

• Purification of a lysophosphatidic acid-hydrolysing lysophospholipase from rat brain [4].
• The characteristics of the 2-acyl-GPE lysophospholipase A2 suggest it could play a role in the selective release of arachidonic and linoleic acids for further metabolism in cells [8].
• This membrane-bound lysophospholipase was solubilized by using n-octyl glucoside and purified by sequential cation, hydrophobic and gel-filtration chromatography [4].
• The stimulation of PLA2/lysophospholipase activity by noradrenaline (NA) was prevented either by the alpha1-adrenergic antagonist prazosin or arachidonyl trifluoromethyl ketone, a selective inhibitor of the 85-110 kDa, sn-2-arachidonyl-specific cytosolic PLA2 [9].
• GPC and GPE acted as competitive inhibitors of lysophospholipase activity, but failed to alter the activity of the other enzymes tested [12].

Other interactions of Lypla1

• However, we could not detect either the NPP activity or the lysophospholipase D activity in the immunoprecipitates with antibodies to NPP-5 from rat brain membranes [13].

References