Isolated Bovine Adrenal Medullary Cells: Studies on Regulation of Catecholamine Synthesis and Release

Oka, M.; Isosaki, Minoru; Yanagihara, Nobuyuki

doi:10.1016/b978-1-4832-8363-0.50021-5

Cited by 33 publications

(19 citation statements)

References 4 publications

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“…This study shows that acetylcholine and muscarine stimulate the 32Pi incorporation into phosphatidic acid, the efflux of 45Ca2+, and the synthesis of cyclic GMP in cultured bovine chromaffin cells. Our observation is consistent with other reports [3,14-171 that acetylcholine stimulated the turnover of phosphatidylinositol in a variety of tissues via muscarinic receptor, and the reports [5, 15,16] that muscarinic agents stimulated the efflux of 45Ca2+ and increased cyclic GMP levels in pancreatic acinar cells, pituitary glands and chromaffin cells. We further demonstrate that phosphatidic acid exogenously added to cultured chromaffin cells mimicks the effect of acetylcholine in that it induces the efflux of 45Ca2+ from prelabelled cells and elevates the intracellular cyclic GMP content, thus extending our recent finding on cloned neuroblastoma NlE 115 cells [4].…”

Section: Resultssupporting

confidence: 93%

Phosphatidic acid mimicks the muscarinic action of acetylcholine in cultured bovine chromaffin cells

Ohsako¹,

Deguchi²

1983

FEBS Letters

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In cultured bovine chromaffin cells, acetylcholine as well as muscarine stimulated the 32Pi incorporation into phosphatidic acid, induced the efflux of 45Ca2+ from prelabelled cells, and, in parallel, elevated intracellular cyclic GMP content. Phosphatidic acid added to the medium also stimulated the efflux of 45Ca2+ and the synthesis of cyclic GMP in the cells in the same fashion as muscarinic agents, whereas it did not induce the secretion of catecholamines indicating that the effect of phosphatidic acid is specific to muscarinic action. The result supports the hypothesis that phosphatidic acid produced during phosphatidylinositol turnover is linked to the regulation mechanism of Ca2+ mobilization and cyclic GMP synthesis by muscarinic stimulation.

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Section: Resultssupporting

confidence: 93%

Phosphatidic acid mimicks the muscarinic action of acetylcholine in cultured bovine chromaffin cells

Ohsako¹,

Deguchi²

1983

FEBS Letters

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“…Cell preparation and culture Bovine adrenal chromaffin cells were dispersed enzymat ically as described previously (15). The cells were plated in 35-mm culture dishes at a density of 2 x 106 cells/dish for standard experiments or on 22 x 22 mm cover glasses in 35-mm culture dishes at a density of 1 x 106 cells/dish for measuring intracellular calcium.…”

Section: Methodsmentioning

confidence: 99%

Stimulatory Effect of Pituitary Adenylate Cyclase-Activating Polypeptide on Catecholamine Synthesis in Cultured Bovine Adrenal Chromaffin Cells: Involvements of Tyrosine Hydroxylase Phosphorylation Caused by Ca2+ Influx and cAMP

Hamano

Masuda

Ishimura

et al. 1994

Japanese Journal of Pharmacology

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ABSTRACT-In cultured bovine adrenal chromaffin cells, pituitary adenylate cylase-activating polypeptide (PACAP) stimulated [14C]catecholamine synthesis from [14C]tyrosine (but not from [14C]DOPA) in a con centration-dependent manner, causing maximal stimulation at 10' M. The stimulatory action of PACAP was not affected by staurosporine (an inhibitor of protein kinase C) or in the cells in which protein kinase C was down-regulated by prolonged exposure to TPA (an activator of protein kinase C), whereas it was partial ly attenuated in Ca"-free medium. PACAP (10-'M) increased the formation of [3H]inositol phosphates, [Ca2+]; and 41 Ca' uptake as well as cAMP. The peptide also stimulated the phosphorylation of tyrosine hydroxylase, the enzyme catalyzing the rate-limiting step in catecholamine synthesis. Catecholamine syn thesis and tyrosine hydroxylase phosphorylation stimulated by the maximal effective concentration of dibutyryl cAMP or high K+, which activates Ca 21 uptake, were further enhanced by PACAP, suggesting that both cAMP and Ca2+-dependent protein kinases may be involved in the stimulation of tyrosine hydroxylase phosphorylation and catecholamine synthesis caused by PACAP.

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“…Physiological stimulation such as acetylcholine for adrenal chroma n cells increases the level of [Ca 2+ ] i originated from intracellular pools and extracellular spaces, leading to biosynthesis and secretion of catecholamine in the cells (Oka et al, 1979;Masserano et al, 1990). The adrenal medulla is rich containing vascular endothelial cells and chroma n cells.…”

Section: Discussionmentioning

confidence: 99%

“…Bovine adrenal chroma n cells were dispersed enzymatically as described previously (Oka et al, 1979). Brie¯y, the medulla was sliced with a hand slicer, and the slices were digested in medium containing 0.1% collagenase, 0.01% soybean trypsin inhibitor and 0.5% bovine serum albumin in balanced salt solution [BSS: 135 mM NaCl, 5.6 mM KCl, 1.2 mM MgSO 4 , 2.2 mM CaCl 2 , 10 mM glucose, and 20 mM N-2-hydroxyethylpiperazine-N'-2-ethanesulphonic acid (HEPES)/NaOH, pH 7.4].…”

Section: Culture Of Bovine Adrenal Chroma N Cellsmentioning

confidence: 99%

“…Physiological stimulations of the adrenal chroma n cells cause an increase in the level of intracellular free Ca 2+ ([Ca 2+ ] i ). The increase in [Ca 2+ ] i leads to the stimulation of catecholamine biosynthesis and secretion (Oka et al, 1979;Masserano et al, 1990). However, possible interaction between the vascular endothelial cells and the adrenal chroma n cells is unknown.…”

Section: Introductionmentioning

confidence: 99%

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Endothelin‐1 stimulates sodium‐dependent calcium efflux from bovine adrenal chromaffin cells in culture

Yoshizumi¹,

Tsuchiya²,

Hirose³

et al. 1998

British J Pharmacology

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1 The e ect of endothelin (ET)-1 on Ca 2+ e ux from cultured bovine adrenal chroma n cells was examined. ET 45 Ca 2+ e ux from the cells. 3 ET-1, Suc-[Glu 9 , Ala 11,15 ]-ET-1 and SRTX increased the level of cyclic GMP in the adrenal chroma n cells. ET-1 induced an increase in the nitric oxide (NO) level in the cells. The stimulatory e ects by which ET-1 increases NO level and 45 Ca 2+ e ux were inhibited by N G -monomethyl-L-arginine acetate (L-NMMA), a competitive inhibitor of NO synthase. 4 The 45 Ca 2+ e ux stimulated by ET-1 was inhibited by deprivation of extracellular Na + , but not by deprivation of Ca 2+ . 5 These results suggest that ET-1 stimulates an extracellular Na + -dependent Ca 2+ e ux through the activation of NO synthase in cultured bovine adrenal chroma n cells.

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Isolated Bovine Adrenal Medullary Cells: Studies on Regulation of Catecholamine Synthesis and Release

Cited by 33 publications

References 4 publications

Phosphatidic acid mimicks the muscarinic action of acetylcholine in cultured bovine chromaffin cells

Phosphatidic acid mimicks the muscarinic action of acetylcholine in cultured bovine chromaffin cells

Stimulatory Effect of Pituitary Adenylate Cyclase-Activating Polypeptide on Catecholamine Synthesis in Cultured Bovine Adrenal Chromaffin Cells: Involvements of Tyrosine Hydroxylase Phosphorylation Caused by Ca2+ Influx and cAMP

Endothelin‐1 stimulates sodium‐dependent calcium efflux from bovine adrenal chromaffin cells in culture

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