Biphasic Generation of Diacylglycerol by Angiotensin and Phorbol Ester in Bovine Adrenal Chromaffin Cells

Tuominen, Raimo K.; Werner, Mark H.; Ye, H.; McMillian, Michael; Hudson, Pearlie M.; Hannun, Y. A.; Hong, Jau–Shyong

doi:10.1006/bbrc.1993.1028

Cited by 6 publications

(3 citation statements)

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“…The initial peak, which appeared within 15 s of stimulation, was followed by a second peak that started at 5 min and was sustained at 1 h and later [130][131][132][133][134][135][136]. The initial peak of DAG corresponded with the production of IP 3 and was shown to arise from PLC-mediated hydrolysis of PI lipids, whereas the second peak was independent of IP 3 levels, and its source was unknown.…”

Section: Regulation Of Pkc By Pld-derived Dagmentioning

confidence: 99%

“…In contrast, incubation of cells with 2-butanol, which is not utilized by PLD, had no effect on either peak of DAG. Importantly, sustained elevations of DAG have been reported in a variety of pathological conditions, such as oncogenic Ras transformation [140][141][142][143][144], chronic angiotensin stimulation [135], lung cancer progression [145] and hyperglycemia [52]. [133,134,147].…”

Section: Regulation Of Pkc By Pld-derived Dagmentioning

confidence: 99%

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

Becker

Hannun

2005

CMLS, Cell. Mol. Life Sci.

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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.

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Section: Regulation Of Pkc By Pld-derived Dagmentioning

confidence: 99%

Section: Regulation Of Pkc By Pld-derived Dagmentioning

confidence: 99%

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

Becker

Hannun

2005

CMLS, Cell. Mol. Life Sci.

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“…In addition to generating inositol phosphates, activation of PLC by AngII generates the second messenger sn-1,2-diacylglycerol (Tuominen et al, 1993). The role of PLC in mediating the effects of AngII (100 nM) on stimulus-secretion coupling was examined by treating cells for 7 min with either the PLC inhibitor U-73122 (1 M) or its inactive isomer U-73443 (1 M).…”

Section: Ca 2؉ Mobilization Is Required For Angii-dependent Facilitatmentioning

confidence: 99%

Bidirectional Modulation of Exocytosis by Angiotensin II Involves Multiple G-Protein-Regulated Transduction Pathways in Chromaffin Cells

Teschemacher

Seward

2000

J. Neurosci.

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Angiotensin II (AngII) receptors couple to a multitude of different types of G-proteins resulting in activation of numerous signaling pathways. In this study we examined the consequences of this promiscuous G-protein coupling on secretion. Chromaffin cells were voltage-clamped at -80 mV in perforated-patch configuration, and Ca(2+)-dependent exocytosis was evoked with brief voltage steps to +20 mV. Vesicle fusion was monitored by changes in membrane capacitance (DeltaC(m)), and released catecholamine was detected with single-cell amperometry. Ca(2+) signaling was studied by recording voltage-dependent Ca(2+) currents (I(Ca)) and by measuring intracellular Ca(2+) ([Ca(2+)](i)) with fura-2 AM. AngII inhibited I(Ca) (IC(50) = 0.3 nm) in a voltage-dependent, pertussis toxin (PTX)-sensitive manner consistent with G(i/o)-protein coupling to Ca(2+) channels. DeltaC(m) was modulated bi-directionally; subnanomolar AngII inhibited depolarization-evoked exocytosis, whereas higher concentrations, in spite of I(Ca) inhibition, potentiated DeltaC(m) fivefold (EC(50) = 3.4 nm). Potentiation of exocytosis by AngII involved activation of phospholipase C (PLC) and Ca(2+) mobilization from internal stores. PTX treatment did not affect AngII-dependent Ca(2+) mobilization or facilitation of exocytosis. However, protein kinase C (PKC) inhibitors decreased the facilitatory effects but not the inhibitory effects of AngII on stimulus-secretion coupling. The AngII type 1 receptor (AT1R) antagonist losartan blocked both inhibition and facilitation of secretion by AngII. The results of this study show that activation of multiple types of G-proteins and transduction pathways by a single neuromodulator acting through one receptor type can produce concentration-dependent, bi-directional regulation of exocytosis.

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The enhancement of phosphatidylcholine biosynthesis by angiotensin II in H9c2 cells

Tran

Man

Choy

1995

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metaboli

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Biphasic Generation of Diacylglycerol by Angiotensin and Phorbol Ester in Bovine Adrenal Chromaffin Cells

Cited by 6 publications

References 0 publications

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

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

Bidirectional Modulation of Exocytosis by Angiotensin II Involves Multiple G-Protein-Regulated Transduction Pathways in Chromaffin Cells

The enhancement of phosphatidylcholine biosynthesis by angiotensin II in H9c2 cells

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