◀ Back to PLD3

PLD3 — SPP2

Text-mined interactions from Literome

Meacci et al., FEBS Lett 1999 : SPP induced PLD activation did not involve membrane translocation of PLD1 or PLD2 and appeared to be fully dependent on protein kinase C ( PKC ) catalytic activity
Orlati et al., Arch Biochem Biophys 2000 : Phosphatidic acid formation was insensitive to protein kinase C inhibitors and almost completely inhibited by pertussis toxin treatment, suggesting that SPP activates phospholipase D via a G ( i/o ) protein coupled receptor
Porcelli et al., Cell Signal 2002 : SPP induced PLD activation and cytoskeletal remodelling were insensitive to brefeldin A and toxin B from Clostridium difficile, which conversely blocked the effect of LPA, suggesting that the monomeric GTPases ADP ribosylation factor ( ARF ) and Rho are involved in LPA, but not in SPP responses
Ghelli et al., Biochem J 2002 : The regulatory role of protein kinase C (PKC) delta isoform in the stimulation of phospholipase D ( PLD ) by sphingosine-1-phosphate ( SPP ) in a human-airway epithelial cell line ( CFNPE9o ( - ) ) was revealed by using antisense oligodeoxynucleotide to PKCdelta, in combination with the specific inhibitor rottlerin
Spiegel et al., J Lipid Mediat 1993 : Similar to sphingosine, SPP also stimulated the activity of phospholipase D , although a significant effect was observed at a much lower concentration
Meyer zu Heringdrof et al., Naunyn Schmiedebergs Arch Pharmacol 1996 : Furthermore, SPP also did not cause activation of either phospholipase D or A2