Release of catecholamines and dopamine-β-oxidase from the adrenal medulla

Viveros, O. Humberto; Arqueros, L.; Kirshner, Norman

doi:10.1016/0024-3205(68)90186-0

Cited by 247 publications

(79 citation statements)

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“…Although the release of DBH -is considered to be an index of the exocytotic release of catecholamine from adrenal gland (Viveros et al 1968) and sympathetic neurones (De Potter, De Schaepdryver, Moerman & Smith, 1969), it has been reported that the time course of catecholamine secretion was different from that of concomitant DBH secretion in both tissues (Cubeddu et al 1974; Dixon et al 1975;Jacobs et al 158 S. ITO 1978;Edwards et al 1980;Ito et al 1980;Muscholl et al 1980). It may be possible that delayed output of DBH, compared with catecholamine secretion, results from a delayed washout of DBH from the release site into the circulation because of the presence of diffusion barriers for this large protein.…”

Section: Resultsmentioning

confidence: 99%

“…Catecholamine secretion from adrenal medulla was accompanied with the release of dopamine-/?-hydroxylase (DBH) (Viveros, Arqueros & Kirshner, 1968), adenine nucleotides (Douglas, Poisner & Rubin, 1965), chromogranin A (Blaschko, Comline, Schneider, Silver & Smith, 1967) and enkephalin (Viveros, Diliberto, Hazum & Chang, 1980). The release of these substances stored in adrenal chromaffin granules was considered to be an index of exocytotic release of catecholamine.…”

Section: Introductionmentioning

confidence: 99%

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Time course of release of catecholamine and other granular contents from perifused adrenal chromaffin cells of guinea‐pig.

Ito¹

1983

The Journal of Physiology

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SUMMARY1. Experiments were carried out to investigate the time course of the release of catecholamine, dopamine-,8-hydroxylase (DBH) and adenine nucleotides from isolated chromaffin cells of guinea-pig adrenal gland.2. When the isolated chromaffin cells were incubated with medium containing acetylcholine (ACh) (0-1 mM), veratridine (0-1 mM) or scorpion (Leiurus quinquestriatus) venom, (10 ,ug/ml.), catecholamine was released into the medium. Catecholamine secretion induced by veratridine or scorpion venom was inhibited by tetrodotoxin (1 gM) but not by atropine (0-1 mM) plus hexamethonium (041 mM). On the other hand, the secretary response to ACh was abolished by the cholinergic blocking drugs but not by tetrodotoxin.3. DBH was released together with catecholamine into the medium in which cells were suspended with these drugs. The ratio of catecholamine (n-mole) to DBH activity (n-mole/hr) appearing in the supernatant was 7-08 + 055, 6-60 + 0X27 and 8X91 + 0 47 for ACh, veratridine and scorpion venom, respectively. These values were close to that found in the lysate of chromaffin granules obtained from guinea-pig adrenal glands (7-37 + 0-39).4. The application of ACh or veratridine to perifused chromaffin cells was found to cause a parallel increase in catecholamine and DBH secretion in the perifusion medium without corresponding amounts of phenylethanolamine-N-methyltransferase leakage. However, DBH secretion tended to last for a longer period than catecholamine secretion.5. Adenine nucleotides were released from perifused chromaffin cells together with catecholamine, by ACh and veratridine. ATP added to the perifusion medium was metabolized to ADP and AMP, of which the ratio (ATP, 21-6 %; ADP, 34 %; AMP, 17-9 %) was close to those of adenine nucleotides released from the cells.6. The secretion ofadenine nucleotides induced by both secretagogues ceased much faster than the catecholamine secretion, so that the molar ratio of catecholamine to adenine nucleotides was gradually increased during and after stimulation. 7. The results indicate that catecholamine secretion is accompanied with a simultaneous release of DBH and ATP from adrenal chromaffin cells. Therefore, it is suggested that the delayed output of DBH, unlike catecholamine secretion, in perfused adrenal glands results from the presence of a diffusion barrier for this protein. The releasable secretary granules of isolated chromaffin cells are suggested to be heterogeneous with respect to the ratio of catecholamine to ATP.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Time course of release of catecholamine and other granular contents from perifused adrenal chromaffin cells of guinea‐pig.

Ito¹

1983

The Journal of Physiology

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“…It is uncertain whether the release of catecholamines induced by veratridine occurs by exocytosis. The biochemical evidence for the exocytotic release of catecholamines from adrenal chromaffin cells is that the 'soluble' contents of granules such as adenosine 5'-triphosphate (ATP) (Douglas, Poisner & Rubin, 1965;Banks, 1966;Douglas & Poisner, 1966a,b;Lastowecka & Trifar6, 1974), chromogranin A (Banks & Helle, 1965;Blaschko, Comline, Schneider, Silver & Smith, 1967;Kirshner, Sage & Smith, 1967;Schneider, Smith & Winkler, 1967) and dopamine-f,-hydroxylase (DBH) (Viveros, Arqueros & Kirshner, 1968;Sorimachi & Yoshida, 1979) are released with catecholamine in the same proportion as they are found in the lysate of the isolated chromaffin granules. In the present experiments, we tried to discover whether the release of catecholamines induced by veratridine was accompanied by release of DBH and ATP from perfused, isolated adrenal glands of guinea-pig.…”

Section: Introductionmentioning

confidence: 99%

“…In the present experiments, we tried to discover whether the release of catecholamines induced by veratridine was accompanied by release of DBH and ATP from perfused, isolated adrenal glands of guinea-pig. The results were compared with the effects of splanchnic nerve stimulation, acetylcholine (ACh) and excess K+ which are reported to cause the secretion of DBH (Viveros et al, 1968;Dixon, Garcia & Kirpekar, 1975;Jacobs, Henry, Johnson & Williams, 1978;Sorimachi & Yoshida, 1979) or adenine nucleotides (Douglas et al, 1965;Banks, 1966; Douglas & Poisner, 1966a) together with catecholamines in other species.…”

Section: Introductionmentioning

confidence: 99%

Exocytotic Release of Catecholamine From Perfused Adrenal Gland of Guinea‐pig Induced by Veratridine

Nakazato

Ohga

1980

British J Pharmacology

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I Experiments were carried out on perfused adrenal glands of guinea-pig to determine whether veratridine caused the exocytotic release of catecholamine by comparing its effect with that of splanchnic nerve stimulation and secretagogues such as acetylcholine and excess K+.2 Veratridine (100 gM) and excess K+ (56 mM) caused secretion of catecholamine and dopamine-f)-hydroxylase (DBH) activity in the venous effluents in the presence of atropine (30 gM) and hexamethonium (2 mM). Splanchnic nerve stimulation in the presence or absence of physostigmine (100 nM) and infusion of acetylcholine in the presence of physostigmine had the same effect. In all the responses, the release of DBH tended to last for a longer period than that of catecholamine. 3 The ratio of catecholamine to DBH activity appearing in the venous effluents was approximately 9, regardless of the method of stimulation. This value was close to the ratio of catecholamines to the 'soluble' DBH activity found in the chromaffin granules. 4 All the types of stimulation used caused a proportional release of adenine nucleotides and catecholamines in the effluents. The adenine nucleotides were mainly adenosine 5'-phosphate. 5 The ratio of catecholamine to adenine nucleotides was approximately 11, regardless of the method of stimulation. 6 It is suggested that the release of catecholamine induced by veratridine occurs by exocytosis in adrenal glands of guinea-pig.

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“…During exocytosis, the vesicle and plasma membrane fuse and the intravesicular products are discharged into the extracellular space (6)(7)(8)(9)(10). Membrane fusion is rapidly followed by retrieval of the excess membrane by micropinocytosis (7,11,12). The cytoplasmic surface of the plasma and vesicle membranes have net negative charges (4,5,13) and the electrostatic barrier should be decreased before the two membranes come into contact and fuse (4,5).…”

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confidence: 99%

Subcellualr distribution of protein carboxymethylase and its endogenous substrates in the adrenal medulla: possible role in excitation-secretion coupling.

Diliberto¹,

Veiveros²,

Axelrod³

1976

Proc. Natl. Acad. Sci. U.S.A.

108

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Protein carboxymethylase (S-adenosyl-L-methionine:protein O-methyltransferase, EC 2.1.1.24) transfers a methyl group from S-adenosyl-L-methionine to carboxyl side chains of proteins to form labile protein-methyl esters which, thus, neutralize negative charges. This enzyme was examined for its possible participation in excitation-secretion coupling in the adrenal medulla. Protein carboxymethylase has a specific activity several times higher in the adrenal medulla than in the adrenal cortex; also, the medulla has a higher concentration of methyl-acceptor proteins. In the adrenal medulla, 97% of the enzyme was localized in the cytosol. Of the various subeellular fractions of the medulla, the catecholamine-containing chromaffin vesicles had the highest concentrations of substrate~s) for (4,5). During exocytosis, the vesicle and plasma membrane fuse and the intravesicular products are discharged into the extracellular space (6-10). Membrane fusion is rapidly followed by retrieval of the excess membrane by micropinocytosis (7,11,12). The cytoplasmic surface of the plasma and vesicle membranes have net negative charges (4,5,13) and the electrostatic barrier should be decreased before the two membranes come into contact and fuse (4, 5). The reversal of the change in surface charge may contribute to the retrieval of the empty vesicle membrane.Secretion of catecholamines from the adrenal medulla occurs by exocytosis (6-10) and the negative surface potential of the catecholamine-containing chromaffin vesicle is mainly derived from carboxyl groups of protein in the vesicle membrane (4). For carboxymethylation to be a step in excitation-secretion coupling, the protein(s) in the cytoplasmic surface of the plasma and/or chromafin vesicle membrane should be exposed to, and be substrate(s) for, the enzyme. We report now the predominant localization of protein carboxymethylase in the cytosol of the adrenal medullary cells and of methyl-acceptor proteins on the surface of chromaffin vesicles. Preliminary reports of these findings have been published elsewhere (14, 15). MATERIALS AND METHODS Materials. S-adenosyl-L-[methyl-3H]methionine, 12.6 Ci/ mmol, and [14C]tryptamine, 8.7 mCi/mmol, were purchased from New England Nuclear Corp. Gelatin (swine skin type I) was obtained from Sigma Chemical Co., Sephadex G-100 and QAE-Sephadex A-50 were from Pharmacia Fine Chemicals Inc.; sucrose (crystalline, density gradient grade) was supplied by Schwarz/Mann. Enzyme Purification. Protein carboxymethylase was purified from bovine pituitaries by the procedure previously described (2, 3).Protein Carboxymethylase Assay. Protein carboxymethylase activity was assayed by a modification of the method previously described (2, 3). Protein-methyl esters formed through the transfer of the methyl group from S-adenosyl-L- [methyl-3H] and terminated by the addition of 1 ml of 10% trichloroacetic acid. After centrifugation, the protein-methyl esters were hydrolyzed with 400 Mul of 1.0 M borate buffer at pH 11.0 containing methanol, 0.7% (vol/vol), ...

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Release of catecholamines and dopamine-β-oxidase from the adrenal medulla

Cited by 247 publications

References 9 publications

Time course of release of catecholamine and other granular contents from perifused adrenal chromaffin cells of guinea‐pig.

Time course of release of catecholamine and other granular contents from perifused adrenal chromaffin cells of guinea‐pig.

Exocytotic Release of Catecholamine From Perfused Adrenal Gland of Guinea‐pig Induced by Veratridine

Subcellualr distribution of protein carboxymethylase and its endogenous substrates in the adrenal medulla: possible role in excitation-secretion coupling.

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