Phospholipase D activity of isolated rat brain plasma membranes

Kanfer, Julian N.; McCartney, Douglas G.

doi:10.1016/0014-5793(94)80202-5

Cited by 19 publications

(14 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Traces of PLD activity were detected in cytosol prepared from brain (Chalifour and Kanfer, 1980;DeVries et al, 1983;Hattori and Kanfer, 1985;Song et al, 1993;Exton, 1994) and other tissue (Exton, 1994). Isolated rat brain plasma membranes possess PLD activity (Kanfer and McCartney, 1994), which may be the form of this enzyme responding to receptor occupancy. The properties of the PLD activity were documented for human polymorphonuclear leukocytes (Exton.…”

mentioning

confidence: 95%

Phospholipase D Activity of Rat Brain Neuronal Nuclei

Kanfer

McCartney

Singh

et al. 1996

Journal of Neurochemistry

Self Cite

View full text Add to dashboard Cite

Phospholipase D activity of rat brain neuronal nuclei, measured with exogenous phosphatidylcholine as substrate, was characterized. The measured activity of neuronal nuclei was at least 36‐fold greater than the activity in glia nuclei. The pH optimum was 6.5, and unsaturated but not saturated fatty acids stimulated the enzyme. The optimal concentration of sodium oleate for stimulation of the enzyme activity was 1.2 mM in the presence of 0.75 mM phosphatidylcholine. This phospholipase D activity was cation independent. In the absence of NaF, used as a phosphatidic acid phosphatase inhibitor, the principal product was diglyceride; whereas in the presence of NaF, the principal product was phosphatidic acid. The phospholipase D, in addition to having hydrolytic activity, was able to catalyze a transphosphatidylation reaction. Maximum phosphatidylethanol formation was seen with 0.2–0.3 M ethanol. GTPγS, ATPγS, BeF2, AIF3, phosphatidic acid, and phosphatidylethanol inhibited the neuronal nuclei phospholipase D activity. The addition of the cytosolic fraction of brain, liver, kidney, spleen, and heart to the incubation mixtures resulted in inhibition of the phospholipase D activity. Phospholipase D activity was detectable in nuclei prepared from rat kidney, spleen, heart, and liver.

show abstract

mentioning

confidence: 95%

Phospholipase D Activity of Rat Brain Neuronal Nuclei

Kanfer

McCartney

Singh

et al. 1996

Journal of Neurochemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…For example, activation of L-serine base enzyme (Kanfer & McCartney, 1991), phospholipases D (Kiss & Anderson, 1990;Lavie & Liscovitch, 1990) and C (Hashizume et al, 1992), and inhibition of phosphatidate phosphohydrolase (Lavie et al, 1990;Mullman et al, 1991) by sphingosine lead to increased synthesis of acidic phospholipids. Increased phosphatidic acid levels have been shown to accompany sphingosine-stimulated proliferation of quiescent Swiss 3T3 cells (Zhang et al, 1990b), and a PKC-independent modulatory role for sphingosine on cell growth was suggested (Zhang et al, 1990a).…”

mentioning

confidence: 97%

Effects of sphingosine on peripheral membrane interactions: Comparison of adriamycin, cytochrome c, and phospholipase A2

Mustonen¹,

Lehtonen²,

Kõiv³

et al. 1993

Biochemistry

View full text Add to dashboard Cite

As revealed by resonance energy transfer utilizing pyrene-labeled phosphatidylcholine donor, the mainly electrostatically controlled binding of adriamycin (Adr) and cytochrome c (cyt c) to mixed egg yolk phosphatidic acid/phosphatidylcholine (eggPA/eggPC, 15:85 molar ratio) liposomes was reversed upon the inclusion of increasing contents of sphingosine. At a [sphingosine]/[eggPA] molar ratio of approximately 2:1, the degree of fluorescence quenching by cyt c and Adr was approximately the same as when using liposomes lacking eggPA. Similarly, the increase in the surface pressure of sphingosine/eggPA monolayers on an air/water interface due to the membrane penetration of either cyt c or Adr was progressively reduced by increasing the content of sphingosine in the monolayers. The above critical [sphingosine]/[acidic phospholipid] stoichiometry yielding dissociation of the positively charged ligands Adr or cyt c from membrane acidic phospholipids was shifted from 2:1 to 1:1 upon substituting egg phosphatidylglycerol (eggPG) for eggPA. Accordingly, charge neutralization of the acidic phospholipids by sphingosine could be involved. One eggPA (having maximally two negative charges) appears to require two molecules of sphingosine whereas the maximally singly charged eggPG is neutralized by one sphingosine. For comparison we also studied the effects of sphingosine on the phospholipase A2 catalyzed hydrolysis of the pyrene-labeled acidic alkylacyl phospholipid analog 1-octacosanyl-2-[6-(pyren-1-yl)]hexanoyl-sn-glycero-3- phosphatidylmethanol (C28-O-PHPM) and the corresponding phosphatidylcholine (C28-O-PHPC). In the presence of low Ca2+ concentrations (approximately 50 nM) limiting the rate of the enzymatic reaction, sphingosine gradually inhibited the hydrolysis of phosphatidylcholine, and at 1:6 sphingosine/C28-O-PHPC a nearly complete lack of hydrolysis was evident.(ABSTRACT TRUNCATED AT 250 WORDS)

show abstract

“…Exposure to oxygen-derived free radicals also stimulates cellular PLD activity (8,9). Using PLD from various sources, it has been shown that divalent metal ions can activate this enzyme (10,11).…”

mentioning

confidence: 99%

Metal ion stimulation of phospholipase D‐like activity of isolated rat intestinal mitochondria

Madesh

Balasubramanian

1997

Lipids

View full text Add to dashboard Cite

Presence of phospholipase D-like (PLD) activity in the intestinal mitochondria was identified using endogenous phospholipids as substrate. The enzyme had a pH optimum of 6.5, did not show trans-phosphatidylation activity in the presence of ethanol or butanol, and the product formed was phosphatidic acid (PA). This was confirmed by separation of reaction products by high-performance liquid chromatography and analysis of composition of the PA formed which gave phosphate/fatty acid ratio of 1:2 PLD-like activity was further confirmed by the formation of ethanolamine and choline as products of enzyme action. This activity was stimulated by various metal ions; when stimulated by Mg2+ and Ba2+, it hydrolyzed both phosphatidylcholine and phosphatidylethanolamine, and when stimulated by Ca2+, it preferentially hydrolyzed phosphatidylethanolamine. There was no requirement for sodium oleate for the PLD-like activity in mitochondria. These results suggest that intestinal mitochondria have an active PLD-like enzyme which differs in certain properties from phospholipase D from other tissues.

show abstract

Phospholipase D activity of isolated rat brain plasma membranes

Cited by 19 publications

References 28 publications

Phospholipase D Activity of Rat Brain Neuronal Nuclei

Phospholipase D Activity of Rat Brain Neuronal Nuclei

Effects of sphingosine on peripheral membrane interactions: Comparison of adriamycin, cytochrome c, and phospholipase A2

Metal ion stimulation of phospholipase D‐like activity of isolated rat intestinal mitochondria

Contact Info

Product

Resources

About