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phospholipase d/atrofi
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Elevation of oleate-activated phospholipase D activity during thymic atrophy.
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Various phospholipases are thought to be associated with the in vitro apoptosis of thymocytes. In the present study, the in vivo phospholipase D (PLD) activity of rat thymus was studied after whole-body X-irradiation or injection of dexamethasone (DEX). Using exogenous [14C]dipalmitoyl
Regulation of phototransduction responsiveness and retinal degeneration by a phospholipase D-generated signaling lipid.
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Drosophila melanogaster phototransduction proceeds via a phospholipase C (PLC)-triggered cascade of phosphatidylinositol (PI) lipid modifications, many steps of which remain undefined. We describe the involvement of the lipid phosphatidic acid and the enzyme that generates it, phospholipase D (Pld),
Molecular cloning and characterization of phospholipase D from Jatropha curcas.
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Phospholipase D (PLD, EC 3.1.4.4) is a key enzyme involved in phospholipid catabolism, initiating a lipolytic cascade in membrane deterioration during senescence and stress, which was cloned from Jatropha curcas L., an important plant species as its seed is the raw material for biodiesels. The cDNA
Phospholipase D regulates the size of skeletal muscle cells through the activation of mTOR signaling.
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mTOR is a major actor of skeletal muscle mass regulation in situations of atrophy or hypertrophy. It is established that Phospholipase D (PLD) activates mTOR signaling, through the binding of its product phosphatidic acid (PA) to mTOR protein. An influence of PLD on muscle cell size could thus be
Cloning, expression, and characterization of a novel phospholipase D complementary DNA from rat brain.
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Phospholipase D (PLD) is implicated in important cellular processes such as signal transduction, membrane trafficking, and mitosis regulation. Recently, cDNA for human PLD1 (hPLD1) was cloned from HeLa cells (Hammond, S. M., Altshuller, Y. M., Sung, T-C., Rudge, S. A., Rose, K., Engebrecht, J.,
Enhancing seed quality and viability by suppressing phospholipase D in Arabidopsis.
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Seed aging decreases the quality of seed and grain and results in agricultural and economic losses. Alterations that impair cellular structures and metabolism are implicated in seed deterioration, but the molecular and biochemical bases for seed aging are not well understood. Ablation of the gene
Cloning of a cDNA encoding phospholipase D from Pimpinella brachycarpa.
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Phospholipase D (PLD, EC 3.1.4.4) has been known to be related to various cellular processes in plants. To gain an understanding of the property of the enzyme in Pimpinella brachycarpa, the cDNA of the enzyme was isolated by PCR with degenerate primers, cDNA library screening, and 5' RACE. The
Antisense suppression of phospholipase D alpha retards abscisic acid- and ethylene-promoted senescence of postharvest Arabidopsis leaves.
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Membrane disruption has been proposed to be a key event in plant senescence, and phospholipase D (PLD; EC 3.1.4.4) has been thought to play an important role in membrane deterioration. We recently cloned and biochemically characterized three different PLDs from Arabidopsis. In this study, we
Identification and characterization of a novel plant phospholipase D that requires polyphosphoinositides and submicromolar calcium for activity in Arabidopsis.
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Phospholipase D (PLD; EC 3.1.4.4) has been proposed to be involved in a number of cellular processes including transmembrane signaling and membrane deterioration. PLD previously described from various plant sources generally requires millimolar ranges of calcium for optimal activity. In this study,
Capsaicin-sensitive primary sensory neurons in the mouse express N-Acyl phosphatidylethanolamine phospholipase D.
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Our previous finding, that the capsaicin- and KCl-induced Ca(2+)-dependent production of the intra- and intercellular signaling molecule N-arachidonoyl ethanolamine (anandamide) in cultured primary sensory neurons could be abolished and reduced by approximately 2/3 by capsaicin-induced degeneration
Molecular cloning and chromosome mapping of rat phospholipase D genes, Pld1a, Pld1b and Pld2.
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We have previously obtained three partial rat phospholipase D (PLD) cDNA fragments by a reverse transcriptase-polymerase chain reaction (RT-PCR) method using degenerate primers based on two conserved amino acid sequences in PLDs of human and yeast. The entire coding regions of these genes were
Differential mRNA expression of phospholipase D (PLD) isozymes during cAMP-induced differentiation in C6 glioma cells.
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GTP gamma S-dependent phospholipase D (PLD) activity time-dependently increased during differentiation of rat C6 glioma cells to astrocytic phenotypes induced by dibutyryl cyclic AMP (dbcAMP)/theophylline. The changes in PLD mRNA level were examined by reverse transcriptase-polymerase chain reaction
Functional analysis of mammalian phospholipase D enzymes.
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Phosphatidylcholine-specific phospholipase D (PLD) hydrolyzes the phosphodiester bond of the phosphatidylcholine to generate phosphatidic acid (PA) and regulates several sub-cellular functions. Mammalian genomes contain two genes encoding distinct isoforms of PLD in contrast to invertebrate genomes
Enzymatic characterization of phospholipase D of protozoan Tetrahymena cells.
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Phospholipase D (PLD), which is present in plant, bacterial, and mammalian cells, has been proposed to be involved in a number of cellular processes including transmembrane signaling and membrane deterioration. We demonstrated the existence of evolutionally related PLD activity in the unicellular
Characterization of microsomal and mitochondrial phospholipase D activities and cloning of a phospholipase D alpha cDNA from strawberry fruits.
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Phospholipase D alpha (PLD, EC 3.1.4.4)) is a key enzyme involved in membrane deterioration that occurs during fruit ripening and senescence. The biochemical and molecular characteristics of PLD was studied in strawberry (Fragaria ananassa Duch) fruits, which are non-climacteric fruits. PLD activity
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