ADP-ribosylation Factor Functions Synergistically with a 50-kDa Cytosolic Factor in Cell-free Activation of Human Neutrophil Phospholipase D

Lambeth, J. David; Kwak, Jong‐Young; Bowman, Edward P.; Perry, David K.; Uhlinger, David J.; López, I.

doi:10.1074/jbc.270.6.2431

Cited by 89 publications

(44 citation statements)

References 30 publications

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“…Authentic phosphatidylethanol (PEth) was from Avanti polar-Lipids Inc. (Alabaster, USA). Recombinant ARF1 was prepared from Escherichia coli expressing human ARF1 and yeast myristoylCoA: protein N-myristoyltransferase (Lambeth et al, 1995). Anti-PLD1 antibody was a generous gift from Dr.…”

Section: Methodsmentioning

confidence: 99%

Dexamethasone enhances phospholipase D activity in M-1 cells

Kim

Lee²,

Park³

et al. 2000

Exp Mol Med

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Section: Methodsmentioning

confidence: 99%

Dexamethasone enhances phospholipase D activity in M-1 cells

Kim

Lee²,

Park³

et al. 2000

Exp Mol Med

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“…A 50-kDa factor has been shown to act synergistically with both ARF (11,12) and Rho in stimulating PLD (13). Similarly, both G proteins also act synergistically with protein kinase C␣ to activate PLD.…”

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confidence: 99%

ADP-ribosylation Factor and Rho Proteins Mediate fMLP-dependent Activation of Phospholipase D in Human Neutrophils

Fensome

Whatmore

Morgan

et al. 1998

Journal of Biological Chemistry

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Activation of intact human neutrophils by fMLP stimulates phospholipase D (PLD) by an unknown signaling pathway. The small GTPase, ADP-ribosylation factor (ARF), and Rho proteins regulate the activity of PLD 1 directly. Cell permeabilization with streptolysin O leads to loss of cytosolic proteins including ARF but not Rho proteins from the human neutrophils. PLD activation by fMLP is refractory in these cytosol-depleted cells. Readdition of myr-ARF1 but not non-myr-ARF1 restores fMLP-stimulated PLD activity. C3 toxin, which inactivates Rho proteins, reduces the ARF-reconstituted PLD activity, illustrating that although Rho alone does not stimulate PLD activity, it synergizes with ARF. To identify the signaling pathway to ARF and Rho activation by fMLP, we used pertussis toxin and wortmannin to examine the requirement for heterotrimeric G proteins of the G i family and for phosphoinositide 3-kinase, respectively. PLD activity in both intact cells and the ARFrestored response in cytosol-depleted cells is inhibited by pertussis toxin, indicating a requirement for G i2 /G i3 protein. In contrast, wortmannin inhibited only fMLPstimulated PLD activity in intact neutrophils, but it has no effect on myr-ARF1-reconstituted activity. fMLPstimulated translocation of ARF and Rho proteins to membranes is not inhibited by wortmannin. It is concluded that activation of G i proteins is obligatory for ARF/Rho activation by fMLP, but activation of phosphoinositide 3-kinase is not required.

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“…The original description of the existence of a mammalian PLD focused upon the isoform that is an integral membrane protein [1,2] and required the presence of an unsaturated fatty acid such as sodium oleate for in vitro measurements [3]. Another isoform of PLD requires a small molecular weight ARF like GTP binding protein and PIP2 for in vitro measurements [4][5][6][7][8][9]. Therefore, it seemed of interest to determine if PIP2 and other acidic lipids could influence this neuronal PLD activity.…”

Section: Introductionmentioning

confidence: 99%

Acidic phospholipids inhibit the phospholipase D activity of rat brain neuronal nuclei

et al. 1996

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An oleate dependent form of phospholipase D is present in rat brain neuronal nuclei and both the hydrolytic and transphosphatidylation activities measured. Several acidic phospholipids were found to inhibit this activity in a dose dependent manner. The IC5o values varied from 3.5 ttM for PIP2 to 200 pM for phosphatidic acid. The hydrolysis of PIP2 by phospholipase C would be expected to result in the disinhibition of the oleate dependent phospholipase D activity.

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ADP-ribosylation Factor Functions Synergistically with a 50-kDa Cytosolic Factor in Cell-free Activation of Human Neutrophil Phospholipase D

Cited by 89 publications

References 30 publications

Dexamethasone enhances phospholipase D activity in M-1 cells

Dexamethasone enhances phospholipase D activity in M-1 cells

ADP-ribosylation Factor and Rho Proteins Mediate fMLP-dependent Activation of Phospholipase D in Human Neutrophils

Acidic phospholipids inhibit the phospholipase D activity of rat brain neuronal nuclei

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