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Open AccessJournal ArticleDOI

Signaling through phosphatidylcholine breakdown.

John H. Exton
- 05 Jan 1990 - 
- Vol. 265, Iss: 1, pp 1-4
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TLDR
The rapid formation of high concentrations of this lipid during stimulation by agonists strongly suggests that it has signaling functions, and the prolonged formation of DAG from PC may be important in cellular control mechanisms that require long term activation of protein kinase C.
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This article is published in Journal of Biological Chemistry.The article was published on 1990-01-05 and is currently open access. It has received 1255 citations till now. The article focuses on the topics: Protein kinase A & Protein kinase C.

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Citations
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Journal ArticleDOI

Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C

TL;DR: It is becoming clear that agonist-induced hydrolysis of other membrane phospholipids, particularly choline phospholipsids, by phospholIPase D and phospholiptase A2 may also take part in cell signaling.
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Small GTP-Binding Proteins

TL;DR: In this review, functions of small G proteins and their modes of activation and action are described.
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Phosphatidylcholine breakdown and signal transduction

TL;DR: PC hydrolysis by PLA2, PLC or PLD is a widespread response elicited by most growth factors, cytokines, neurotransmitters, hormones and other extracellular signals and the mechanisms can involve G-proteins, PKC, Ca2+ and tyrosine kinase activities.
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Banting Lecture. Insulin action, diabetogenes, and the cause of type II diabetes.

TL;DR: The person who passes urine which is exceedingly sweet, cool, slightly viscid, turbid, and resembling the juices of the sugarcane … suffers from glycosuria.
Journal ArticleDOI

Enzymes of triacylglycerol synthesis and their regulation

TL;DR: De novo biosynthesis of triacylglycerol in eukaryotic cells, the isoenzymes that are involved, their subcellular locations, how they are regulated, and their putative individual roles in glycerolipid biosynthesis are focused on.
References
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Journal ArticleDOI

The molecular heterogeneity of protein kinase C and its implications for cellular regulation

TL;DR: Protein kinase C is now known to be a large family of proteins, with multiple subspecies that have subtle individual enzymological characteristics, and probably have distinct functions in the processing and modulation of a variety of physiological and pathological responses to external signals.
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Studies of inositol phospholipid-specific phospholipase C.

TL;DR: The diversity in primary structure together with different regional and cellular expression of the isozymes suggests that each isozyme has a defined function in processing the physiological response of different cell types to a variety of external stimuli and that each is regulated differently.
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Separation of phospholipids and individual molecular species of phospholipids by high-performance liquid chromatography.

TL;DR: Using this method, it is found that for each of these phospholipids from 30 to 35 different molecular species can be routinely identified and reproducibly quantitated.
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Growth factor-like action of phosphatidic acid

TL;DR: The results indicate that, unlike an ionophore, PA acts by triggering the hydrolysis of phosphoinositides, with consequent formation of second messengers such as inositol trisphosphate signalling Ca2+ release, which strengthens the notion that any Cai2+-mobilizing stimulus acting through phospholipase C may ultimately function as a growth factor.
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Sustained diacylglycerol formation from inositol phospholipids in angiotensin II-stimulated vascular smooth muscle cells.

TL;DR: Diglyceride production in vascular smooth muscle stimulated with angiotensin II inositol 1,4,5-trisphosphate formation is transient, suggesting that initial and sustained diglyceride formation from the phosphoinositides results from different biochemical and/or cellular processes.