EC Number |
Application |
Reference |
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3.1.3.4 | analysis |
radiolabeled and fluorescent lipid substrates for the detection, quantitation and analysis of the enzymatic activities of the LPPs measured using intact or broken cell preparations as the source of enzyme |
681760 |
3.1.3.4 | drug development |
the PAP1 colorimetric assay with pure enzyme and a water-soluble phosphatidate substrate is applicability to a 96-well format, which may facilitate a large-scale screen of PAP1 inhibitors (or activators) |
707100 |
3.1.3.4 | medicine |
loss of PAP activity contributes to fatty liver dystrophy phenotype. Insulin and epinephrine control lipin primarily by changing localization rather than intrinsic PAP activity |
680814 |
3.1.3.4 | medicine |
LPP1 overexpressing fibroblasts show a severe inhibition of lyso-phosphatidic acid-induced migration in a wound healing assay. Intracellular actions of LPP1 play important functions in regulating lyso-phosphatidic acid-induced fibroblast migration through phospholipase D2, also controls platelet-derived growth factor-betabeta-induced phosphatidate formation |
680723 |
3.1.3.4 | medicine |
LPP3 acts as an ecto-phosphatase that contributes to the equilibration between FTY720 and FTY720-P in vivo |
679860 |
3.1.3.4 | more |
fibroblasts that overexpress LPP1 enter S-phase at approximately the same time as vector control cells |
680744 |
3.1.3.4 | more |
fibroblasts that overexpress LPP3 enter S-phase at approximately the same time as vector control cells |
680744 |
3.1.3.4 | more |
increasing LPP2 activity causes premature entry into S-phase, premature cyclin A expression and decreased rates of proliferation at high passage and accumulation in G2/M. Cells transduced with LPP2 activate the G2/M checkpoint and show characteristics of senescence at high passage |
680744 |
3.1.3.4 | more |
LPP1 overexpression markedly reduces platelet-derived growth factor-induced activation of p42/p44 mitogen-activated protein kinase. This occurs via a mechanism that involves the LPP1-induced down-regulation of typical protein kinase C isoform(s), which are normally required for platelet-derived growth factor-induced activation of p42/p44 mitogen-activated protein kinase and migration |
663975 |