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

Kanfer, J N; McCartney, Douglas G.; Singh, Inderjit; Freysz, L.

doi:10.1016/0014-5793(96)00205-0

Cited by 18 publications

(10 citation statements)

References 28 publications

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“…Brown et al (18) discovered that PLD is strongly stimulated by PIP 2 , and this has been observed for most but not all (10,19,20) preparations of the enzyme. PI-3,4,5-P 3 is also effective (6), 3 but other acidic phospholipids, including PI-3,4-P 2 , PI-4-P, and PI, are nearly or completely ineffective (18,21).…”

Section: Enzymology Of Pldmentioning

confidence: 99%

New Developments in Phospholipase D

Exton

1997

Journal of Biological Chemistry

294

273

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Section: Enzymology Of Pldmentioning

confidence: 99%

New Developments in Phospholipase D

Exton

1997

Journal of Biological Chemistry

294

273

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“…For example, a PtdCho-selective PLD has been partially purified from bovine kidney that is stimulated by PtdEtn, but not by PtdIns(4,5)P, [69]. Another PLD isoform has been identified in brain neuronal nuclei that is dependent on oleate, but is inhibited by PtdIns(4,5)P,, PtdH and PtdSer [70]. There are also variations between tissues and cells in the role played by PKC in the regulation of PLD [4], implying the existence of PKC-dependent and PKC-independent isozymes.…”

Section: Determinants Of Specifity Of Receptor and G-protein Activatimentioning

confidence: 99%

Cell Signalling Through Guanine‐Nucleotide‐Binding Regulatory Proteins (G Proteins) and Phospholipases

Exton

1997

European Journal of Biochemistry

153

109

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Phospholipases are important enzymes in cell signal transduction since they hydrolyze membrane phospholipids to generate signalling molecules. Heterotrimeric guanine-nucleotide-binding regulatory proteins (G proteins) play a major role in their regulation by a variety of agonists that activate receptors with seven membrane-spanning domains. Phospholipases of the C type, which hydrolyze inositol phospholipids to yield inositol trisphosphate and diacylglycerol, are regulated by the a and By subunits of certain heterotrimeric G proteins as well as by receptor-associated and non-receptor-associated tyrosine kinases. Phospholipases of the D type, which hydrolyze phosphatidylcholine to phosphatidic acid, are regulated by members of the ADP-ribosylation factor and Rho subfamilies of small G proteins, and by protein kinase C and other factors. This review presents recent information concerning the molecular details of G protein regulation of these phospholipases.

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“…It was also shown that an oleate-dependent form of PLD was present in rat brain neuronal nuclei and inhibited by acidic phospholipids, such as PIP 2 (25). However, the physiological roles of PLD in nuclei remain unclear.…”

mentioning

confidence: 99%

Nuclear ADP-ribosylation Factor (ARF)- and Oleate-dependent Phospholipase D (PLD) in Rat Liver Cells

Banno

Tamiya‐Koizumi

Oshima

et al. 1997

Journal of Biological Chemistry

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Two forms of phospholipase D (PLD) have been found to be present in nuclei isolated from rat hepatocytes by measuring phosphatidylbutanol produced from exogenous radiolabeled phosphatidylcholine in the presence of butanol. In nuclear lysates from either rat liver or ascites hepatoma AH 7974 cells, the PLD activity was markedly stimulated by a recombinant ADP-ribosylation factor (rARF) in the presence of the guanosine 5-O-(3-thiotriphosphate) (GTP␥S) and phosphatidylinositol 4,5-bisphosphate. ATP and phorbol-12-myristate 13-acetate had no synergistic effect on this PLD activity. On the other hand, the nuclear PLD was stimulated by unsaturated fatty acids, especially by oleic acid. The ARF-dependent nuclear PLD activity was increased in the S-phase of the regenerating rat liver after partial hepatectomy and also was much higher in AH 7974 cells than in the resting rat liver. In contrast, the levels of the oleate-dependent PLD activity remained constant throughout the cell cycle in liver regeneration. The intranuclear levels of the stimulating proteins of the nuclear PLD activity, e.g. ARF, RhoA, and protein kinase C␦ increased in the S-phase of the regenerating liver. These results suggested that the nuclear ARFdependent PLD activity may be associated with cell proliferation.It has been known that cell nuclei contain a variety of enzymes generating lipid second messengers, such as sphingomyelinase (1), phospholipase A2 (2), PI 1 -specific phospholipase C (3-6) and lipid kinases (7). Growth factors seem to be able to affect the phosphoinositide metabolism in nuclei, suggesting a subtle regulation during cell activation (8, 9). In addition, accumulation of diacylglycerol (DG) in nuclei and translocation of protein kinase C to them have been demonstrated in a variety of cell types (10, 11). A large rise in mass of DG, with only small changes in mass of phosphoinositides, suggested a source of DG other than polyphosphoinositides, for example, phosphatidylcholine (PC), in nuclei (12). A recent study (13) has demonstrated that phosphatidylethanol formation from phosphatidylcholine, which was specifically catalyzed by phospholipase D (PLD) in the presence of ethanol, was induced by PMA in nuclei isolated from kidney cells and that nuclei possess the ability to generate DG and phosphatidic acid through the PLD:phosphatidic acid phosphohydrolase pathway. Thus, upon cell stimulation with agonists, the enzymes involving PC metabolism are considered to be activated in the nucleus as well as in the plasma membrane.It was demonstrated that PLD activity can be regulated by several factors (14, 15); oleate, small G proteins (ARF and Rho family), phosphatidylinositol 4,5-bisphosphate (PIP 2 ), phosphatidylethanolamine (PE), Ca 2ϩ , protein kinase C, protein tyrosine kinase. Recently, two different types of PLD, oleatedependent and ARF-dependent, were isolated from rat brain membranes (16). The oleate-dependent PLD was purified from pig lung microsomes (17), and ARF-dependent PLD activity was found to be abundant in Golgi-enriched ...

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

Cited by 18 publications

References 28 publications

New Developments in Phospholipase D

New Developments in Phospholipase D

Cell Signalling Through Guanine‐Nucleotide‐Binding Regulatory Proteins (G Proteins) and Phospholipases

Nuclear ADP-ribosylation Factor (ARF)- and Oleate-dependent Phospholipase D (PLD) in Rat Liver Cells

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