Signalling roles of mammalian phospholipase D1 and D2

Phospholipase D (PLD) catalyses the hydrolysis of phosphatidylcholine to generate the lipid second messenger, phosphatidate (PA) and choline. PLD activity in mammalian cells is low and is transiently stimulated upon activation by G-protein-coupled and receptor tyrosine kinase cell surface receptors. Two mammalian PLD enzymes (PLD1 and PLD2) have been cloned and their intracellular regulators identified as ARF and Rho proteins, protein kinase Cα as well as the lipid, phosphatidylinositol [4, 5] bisphosphate (PIP₂). I discuss the regulation of these enzymes by cell surface receptors, their cellular localisation and the potential function of PA as a second messenger. Evidence is presented for a role of PA in regulating the lipid kinase activity of PIP 5-kinase, an enzyme that synthesises PIP₂. A signalling role of phospholipase D via PA and indirectly via PIP₂ in regulating membrane traffic and actin dynamics is indicated by the available data. Received 25 April 2001; received after revision 15 June 2001; accepted 15 June 2001     

Quantitative changes of the free phospholipids in the sea-urchin egg at fertilization

Riassunto Nelle uova diArbacia lixula si osserva una diminuzione di fosfolipidi liberi nei primi minuti dopo la fecondazione, seguita poi da un aumento che riporta, nel corso di 15 min circa, la quantità di fosfolipidi liberi al valore delle uova vergini. Non pare che vi sia alcuna variazione quantitativa nella frazione dei fosfolipidi legati.     

Adaptation of lipase and phospholipase A activities in pancreas and pancreatic juice in rats with diets rich in triglycerides and phospholipids]

Lipid rich diets containing about 20% of triglycerides or phospholipids given to Rats during 2 months were observed to increase lipase and phospholipase A2 activities in pancrease and pancreatic juice. The phospholipase and lipase activities are higher, respectively, on the phospholipid and triglyceride diet. Lower effects are observed after a 7-day administration of diet containing 40% of total lipid.     

Protein kinase C and phospholipase D: intimate interactions in intracellular signaling

Diacylglycerol (DAG) was discovered as a potent lipid second messenger with protein kinase C (PKC) as its major cellular target more than 25 years ago. There is increasing evidence of significant complexity within lipid signaling, and the classical DAG-PKC model no longer stands alone but is part of a larger bioactive lipid universe involving glycerolipids and sphingolipids. Multiple layers of regulation exist among PKC- and DAG-metabolizing enzymes such as phosphatidylcholine (PC)-specific phospholipase D, and cross-talk exists between the glycerolipid and sphingolipid pathways, with PKC at the center. Currently, there is intense interest in the question of whether DAG derived from PC can function as a lipid second messenger and regulate PKC analogous to DAG derived from phosphatidylinositol-4,5-bisphosphate (PIP₂). To address these issues and incorporate DAG-PKC and other signaling pathways into an expanded view of cell biology, it will be necessary to go beyond the classical approaches and concepts.Received 29 November 2004; received after revision 18 January 2005; accepted 4 March 2005This work is dedicated to the memory of Dr. Yasutomi Nishizuka, the discoverer of protein kinase C, who was both a gentleman and a scientist.     

Effect of phospholipids on purified lipoamidase

Phospholipids were added to purified lipoamidase from porcine brain microsomal membranes, and changes in lipoamidase activity were examined. Approximately twofold activation of lipoamidase activity occurred upon the addition of phosphatidylethanolamine. On the other hand, phosphatidylserine, cardiolipin, and phosphatidic acid reduced the enzyme activity by approximately 80%. This pattern of the activation of lipoamidase by phosphatidylethanolamine and its inhibition by phosphatidylserine is similar to the pattern for adenylate cyclase, and contrasts with the pattern for ATPase.     

Effect of phospholipids on purified lipoamidase

Summary Phospholipids were added to purified lipoamidase from porcine brain microsomal membranes, and changes in lipoamidase activity were examined. Approximately twofold activation of lipoamidase activity occurred upon the addition of phosphatidylethanolamine. On the other hand, phosphosphatidylserine, cardiolipin, and phosphatidic acid reduced the enzyme activity by approximately 80%. This pattern of the activation of lipoamidase by phosphatidylethanolamine and its inhibition by phosphatidylserine is similar to the pattern for adenylate cyclase, and contrasts with the pattern for ATPase.     

Action of cadmium on a free dinoflagellate Prorocentrum micans E: growth, cadmium absorption and cell modifications]

The study of the growth of Prorocentrum micans E. submitted to sublethal doses of cadmium demonstrated a high sensitivity of this Dinoflagellate to the polluant starting with concentration of 5 microgram/l. The uptake of cadmium was measured by pulse polarographic analysis of the filtered culture medium. Structural modifications, not apparent in living cells, are visible after fixation. The high sensitivity of Prorocentrum micans to cadmium, also its easy culture, makes it a suitable pollution indicator of this heavy metal.     

Effect of dipyridamole on human platelet phospholipids

Summary The effect of dipyridamole on platelet phospholipids has been studied. After the platelet incubation with dipyridamole, a 38% reduction in the concentration of the sphingomyelin and a 21% increase in phosphatidyl choline were produced.     

Effect of dipyridamole on human platelet phospholipids.

The effect of dipyridamole on platelet phospholipids has been studied. After the platelet incubation with dipyridamole, a 38% reduction in the concentration of the sphingomyelin and a 21% increase in phosphatidyl choline were produced.     

Influence of ethanol on calcium, inositol phospholipids and intracellular signalling mechanisms

Studies have implicated Ca++ in the actions of ethanol at many biochemical levels. Calcium as a major intracellular messenger in the central nervous system is involved in many processes, including protein phosphorylation enzyme activation and secretion of hormones and neurotransmitters. The control of intracellular calcium, therefore, represents a major step by which neuronal cells regulate their activities. The present review focuses on three primary areas which influence intracellular calcium levels; voltage-dependent Ca++ channels, receptor-mediated inositol phospholipid hydrolysis, and Ca++/Mg++-ATPase, the high affinity membrane Ca++ pump. Current research suggests that a subtype of the voltage-dependent Ca++ channel, the dihydropyridine-sensitive Ca++ channel, is uniquely sensitive to acute and chronic ethanol treatment. Acute exposure inhibits, while chronic ethanol exposure increases 45Ca++-influx and [3H]dihydropyridine receptor binding sites. In addition, acute and chronic exposure to ethanol inhibits, then increases Ca++/Mg++-ATPase activity in neuronal membranes. Changes in Ca++ channel and Ca++/Mg++-ATPase activity following chronic ethanol may occur as an adaptation process to increase Ca++ availability for intracellular processes. Since receptor-dependent inositol phospholipid hydrolysis is enhanced after chronic ethanol treatment, subsequent activation of protein kinase-C may also be involved in the adaptation process and may indicate increased coupling for receptor-dependent changes in Ca++/Mg++-ATPase activity. The increased sensitivity of three Ca++-dependent processes suggest that adaptation to chronic ethanol exposure may involve coupling of one or more of these processes to receptor-mediated events.