Phorbol ester and bryostatin differentially regulate the hydrolysis of phosphatidylethanolamine in Ha-ras- and raf-oncogene-transformed NIH 3T3 cells.

  title={Phorbol ester and bryostatin differentially regulate the hydrolysis of phosphatidylethanolamine in Ha-ras- and raf-oncogene-transformed NIH 3T3 cells.},
  author={Zoltan Kiss and Ulf R{\"u}diger Rapp and George R. Pettit and Wayne B. Anderson},
  journal={The Biochemical journal},
  volume={276 ( Pt 2)},
Previously it was reported that transformation of NIH 3T3 fibroblast by the Ha-ras, v-src, v-fms, and A-raf oncogenes decreased the stimulatory effects of phorbol 12-myristate 13-acetate (PMA; 'TPA'), an activator of protein kinase C (PKC), on the phosphorylation of an endogenous 80 kDa substrate and on 86Rb uptake [Wolfman, Wingrove, Blackshear & Macara (1987) J. Biol. Chem. 262, 16546-16552], as well as on sphingomyelin synthesis [Kiss, Rapp & Anderson (1988) FEBS Lett. 240, 221-226]. Here… Expand
Effects of bryostatin 1 and other pharmacological activators of protein kinase C on 1-[beta-D-arabinofuranosyl]cytosine-induced apoptosis in HL-60 human promyelocytic leukemia cells.
Assessment of DNA damage by quantitative spectrofluorophotometry of small molecular weight, double-stranded DNA fragments provided a more complete characterization of the interaction between ara-C and bryostatin 1, and a direct comparison of the relative effects of brystatin 1 treatment with other pharmacological manipulations known to modulate protein kinase C activity. Expand
Phospholipase D Activities and Phosphatidylcholine Turnover are Differentially Related to Expression of Protein Kinase C Isoforms and Marcks in Control and Transfected Neural Cells
Phosphatidylcholine (PtdCho) and phosphatidylethanolamine (PtdEtn) are major membrane phospholipids constituting 70–80% of the total phospholipids in most ceils (Vance, 1991; Kent, 1995).Expand
Regulation of phospholipase D by protein kinase C.
  • Z. Kiss
  • Chemistry, Medicine
  • Chemistry and physics of lipids
  • 1996
No convincing evidence has been reported to support the role of PLD in the mediation of any of the above cellular effects of activated PKC, but both the PLD and PKC systems have been implicated in the regulation of vesicle transport and exocytosis. Expand
The protein phosphatase inhibitor, okadaic acid, potentiates the stimulatory effect of phorbol ester on phosphatidylcholine synthesis, but not on phospholipid hydrolysis, in fibroblasts
  • Z. Kiss
  • Chemistry, Medicine
  • FEBS letters
  • 1992
The potent protein phosphatase inhibitor, okadaic acid, was used to determine the possible role of protein phosphorylation reaction(s) in phorbol ester‐induced synthesis and hydrolysis ofExpand
Phospholipase D activity of human amnion cells stimulated with phorbol ester and bradykinin
Abstract We investigated the activity of phospholipase D (PLD) in human amnion cells labeled with [3H]oleate. The PLD activity was detected as signal-induced synthesis of phosphatidic acid (PA) and.Expand
Ha‐Ras stimulates uptake and phosphorylation of ethanolamine: inhibition by wortmannin
Wortmannin, an inhibitor of phosphatidylinositol 3‐kinase (P13K), preferentially decreased phosphorylation of externally added Etn in the Ha‐Ras transformed, but not in the untransformed, fibroblasts. Expand
Ras protein is involved in the physiological regulation of phospholipase D by platelet derived growth factor
PDGF requires a complex system for PLD regulation implying the existence of at least two positive regulatory pathways, a Ras-dependent and a PKC-dependent mechanism, which implies that PLD is an important element in signaling by Ras proteins that is altered after ras-induced transformation. Expand
Parathyroid hormone stimulates phosphatidylethanolamine hydrolysis by phospholipase D in osteoblastic cells
The results suggest that both PC and PE are substrates for phospholipase D in UMR-106 osteoblastic cells and could therefore be sources ofospholipid hydrolysis products for downstream signaling in osteoblasts. Expand
Alkyl lysophospholipids inhibit phorbol ester‐stimulated phospholipase D activity and DNA synthesis in fibroblasts 1
The results suggest that the PLD and protein kinase C systems may be important cellular targets of ALP actions. Expand
Establishment of a murine leukaemia cell line resistant to the growth-inhibitory effect of bryostatin 1.
All four P388/BR sublines show an equal degree of resistance to the growth inhibitory effects of bryostatin 1, with a relative resistance ratio (RR) IC50 of approximately 4,000, and high and equal levels of cross-resistance to the PKC activatoryphorbol ester, phorbol 12-myristate 13-acetate (PMA). Expand