نتایج جستجو برای: phospholipase d pld

تعداد نتایج: 596477  

Journal: :FEBS letters 2003
Zuzana Novotná Jan Linek Radovan Hynek Jan Martinec Martin Potocký Olga Valentová

Phospholipase D (PLD) forms the major family of phospholipases that was first discovered and cloned in plants. In this report we have shown, for the first time, that C2 phosphatidylinositol-4,5-bisphosphate (PIP2)-dependent PLD(s) from 5 day hypocotyls of Brassica oleracea associated with plasma membrane is covalently modified-phosphorylated. Pre-incubation of the plasma membrane fraction with ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2001
H Interthal J J Pouliot J J Champoux

The phospholipase D (PLD) superfamily is a diverse group of proteins that includes enzymes involved in phospholipid metabolism, a bacterial toxin, poxvirus envelope proteins, and bacterial nucleases. Based on sequence comparisons, we show here that the tyrosyl-DNA phosphodiesterase (Tdp1) that has been implicated in the repair of topoisomerase I covalent complexes with DNA contains two unusual ...

2005
Jian Dai Johanna T.A. Meij Rodel Padua Vincenzo Panagia

Myocardial phospholipase D (PLD) is primarily localized at the sarcolemmal level and selectively hydrolyzes phosphatidylcholine to form phosphatidic acid as part of the signal transduction mechanisms for regulating Ca2' movements in the heart. Since the myocardial cell damage induced by oxidative stress is associated with abnormalities in Ca2' homeostasis and thiol status, we examined the thiol...

1998
Dong Geng Justin Chura Mary F. Roberts

The activity of bacterial phospholipase D (PLD), a Ca-dependent enzyme, toward phosphatidylcholine bilayers was enhanced 7-fold by incorporation of 10 mol % phosphatidic acid (PA) in the vesicle bilayer. Addition of other negatively charged lipids such as phosphatidylinositol, phosphatidylmethanol, and oleic acid either inhibited or had no effect on enzyme activity. Only negatively charged lipi...

Journal: :Plant & cell physiology 2007
Nick T Peters Kyle O Logan Anne Catherine Miller Darryl L Kropf

Recent studies in higher plants or animals have shown that phospholipase D (PLD) signaling regulates many aspects of development, including organization of microtubules (MTs), actin and the endomembrane system. PLD hydrolyzes structural phospholipids to form the second messenger phosphatidic acid (PA). To begin to understand the signaling pathways and molecules that regulate cytoskeletal and en...

Journal: :Journal of pharmacological sciences 2005
Ali A Peivandi Alexander Huhn Hans-Anton Lehr Shenchu Jin Joachim Troost Sonia Salha Tobias Weismüller Konrad Löffelholz

Evidence for a role of phospholipase D (PLD) in cellular proliferation and differentiation is accumulating. We studied PLD activity and expression in normal and hypertrophic rat and human hearts. In rat heart, abdominal aortic banding (constriction to 50% of original lumen) caused hypertrophy in the left ventricle (as shown by weight index and ANP expression) by about 15% after 30 days without ...

Journal: :Biochemistry 2006
Donmienne Leung Alan Saghatelian Gabriel M Simon Benjamin F Cravatt

N-Acyl ethanolamines (NAEs) constitute a large and diverse class of signaling lipids that includes the endogenous cannabinoid anandamide. Like other lipid transmitters, NAEs are thought to be biosynthesized and degraded on-demand rather than being stored in vesicles prior to signaling. The identification of enzymes involved in NAE metabolism is therefore imperative to achieve a complete underst...

Journal: :The Biochemical journal 1999
D H Jones B Bax A Fensome S Cockcroft

The small GTP-binding protein, ADP-ribosylation factor 1 (ARF1) is essential for the formation of coatomer-coated vesicles from the Golgi and is also an activator of phospholipase D (PLD). Moreover, ARF1-regulated PLD is part of the signal-transduction pathway that can lead to secretion. In this study, substitution and deletion mutants of ARF1 were tested for their ability to activate PLD. Thes...

Journal: :Molecular pharmacology 2011
Chenggang Zhu Carlos Solorzano Saurabh Sahar Natalia Realini Ernest Fung Paolo Sassone-Corsi Daniele Piomelli

Palmitoylethanolamide (PEA) is an endogenous lipid amide that modulates pain and inflammation by engaging peroxisome proliferator-activated receptor type-α. Here, we show that the proinflammatory bacterial endotoxin lipopolysaccharide (LPS) decreases PEA biosynthesis in RAW264.7 macrophages by suppressing the transcription of N-acylphosphatidylethanolamine-specific phospholipase D (NAPE-PLD), w...

Journal: :The Biochemical journal 1993
J Song D A Foster

Phospholipase D (PLD) activity, as measured by the transphosphatidylation of cellular phospholipids, is elevated in BALB/c 3T3 cells transformed by v-Src. Phorbol esters that activate protein kinase C (PKC) also increase PLC activity in BALB/c 3T3 cells. v-Src-induced PLD activity could be distinguished from phorbol ester-induced PLD activity by differential radiolabelling of phospholipids, whi...

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