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PLD3 — SPP1
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
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