Histochemical Demonstration of Noradrenaline and Adrenaline in the Adrenal Medulla

Hillarp, Nils‐Åke; Hökfelt, Bernt

doi:10.1177/3.1.1

Cited by 156 publications

(18 citation statements)

References 11 publications

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“…By using both immunohistochemistry and in situ hybridization, the expression of PNMTase was localized to the outer two-thirds of the bovine adrenal medulla, in contrast to the rat adrenal gland, where the PNMTase-cells are more evenly distributed throughout the medulla (26,27). NPY was confined only to PNMTase-positive cells in the bovine adrenal medulla, whereas in the rat both epinephrine and norepinephrine cells contain this peptide (see ref.…”

Section: Discussionmentioning

confidence: 99%

Coexistence and gene expression of phenylethanolamine N-methyltransferase, tyrosine hydroxylase, and neuropeptide tyrosine in the rat and bovine adrenal gland: effects of reserpine.

Schalling

Dagerlind

Brené

et al. 1988

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

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Expression and regulation of the catecholamine-synthesizing enzymes phenylethanolamine N-methyltransferase (PNMTase; S-adenosyl-L-methionine:phenylethanolamine N-methyltransferase, EC 2.1.1.28) and tyrosine hydroxylase [TyrOHase; tyrosine 3-monooxygenase, L-tyrosine, tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating), EC 1.14.16.2] and the coexisting neuropeptide tyrosine (NPY) were studied in rat and bovine adrenal medulla. By using both immunohistochemistry and in situ hybridization, PNMTase-and NPY-positive cells exhibited a close overlap in bovine medulla and were preferentially localized in the outer two-thirds of the medulla. Although TyrOHase and its mRNA were observed in virtually all medullary gland cells, TyrOHase mRNA levels were much higher in the PNMTase-and NPYpositive cells. After administration of the catecholaminedepleting drug reserpine to rats, a brief increase, followed by a dramatic decrease, in the level of PNMTase mRNA was observed in the adrenal medulla. In contrast, mRNA for both TyrOHase and NPY only exhibited an increase, whereby the TyrOHase mRNA peak preceded that of NPY mRNA. Different regulatory mechanisms may thus operate for these three compounds coexisting in the adrenal medulla.

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Section: Discussionmentioning

confidence: 99%

Coexistence and gene expression of phenylethanolamine N-methyltransferase, tyrosine hydroxylase, and neuropeptide tyrosine in the rat and bovine adrenal gland: effects of reserpine.

Schalling

Dagerlind

Brené

et al. 1988

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

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“…The chromaffin reaction was performed on cultures fixed for 10-14 hr, in a solution of K2Cr2O4 and K2CrO4 according to the method of Hillarp & Hokfelt (1955). For formaldehyde induced fluorescence, cover-slip cultures of adrenal medulla cells were rapidly blown dry at room temperature and then further air dried over Pr05 for at least 3 days.…”

Section: Methodsmentioning

confidence: 99%

Electrical excitability of cultured adrenal chromaffin cells.

Biales¹,

Dichter²,

Tischler³

1976

The Journal of Physiology

154

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SUMMARY1. Adult human and gerbil adrenal medullary cells were maintained in dissociated cell culture and studied by micro-electrode penetration.2. In the best recordings, chromaffin cell transmembrane potentials exceeded -50 mV.3. Chromaffin cells were capable of generating all-or-nothing overshooting action potentials, similar to those generated by sympathetic neurones.4. The action potentials were blocked by tetrodotoxin (TTX, 106 g/ml.) but were not blocked by removal of Ca or by CoCl2 (10 mM). We conclude that the action potentials are probably generated by a Na mechanism.5. Chromaffin cells are depolarized by the iontophoretic application of acetylcholine (ACh). This depolarization was accompanied by an increased membrane conductance and could trigger action potentials.6. Action potentials were also found in cells in fresh slices of gerbil adrenal medullae.

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“…The identification criteria were validated by positive bichromate staining of cells from which recording had been done. Cells were stained by a modification of the method of Hillarp & Hokfelt (1955). After electrophysiological recording was completed the cell was photographed in situ with the micro-electrode still in place.…”

Section: Isolation and Identification Of Chromaffin Cellsmentioning

confidence: 99%

Action potentials in the rat chromaffin cell and effects of acetylcholine.

Brandt¹,

Hagiwara²,

Kidokoro³

et al. 1976

The Journal of Physiology

301

220

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SUMMARY1. Electrophysiological properties of the rat chromaffin cell were studied using intracellular recording techniques.2. The resting potential in the chromaffin cell was -49+6 mV (mean + S.D., n = 14) in standard saline containing 10 mm-Ca whereas that in Na-free saline was -63 + 9 mV (n = 17). At rest, the membrane has a substantial Na permeability.3. Action potentials were evoked by passing current through the recording electrode. In standard saline the major fraction of the action potential disappeared either upon omission of external Na ions from standard saline or addition of 1 /lM tetrodotoxin (TTX). We conclude that action potentials in the chromaffin cell are due mainly to an increase in the permeability of the membrane to Na ions.4. Small but significant regenerative action potentials were observed in Na-free saline, and when Ca in Na-free saline was replaced by Ba, prolonged action potentials occurred. We conclude that action potentials in the chromaffin cell also have a Ca component.5. Iontophoretic application of acetylcholine (ACh) produced a transient membrane depolarization in standard saline.6. Spontaneous action potentials were recorded extracellularly by microsuction electrodes. They occurred at a rate of 0 05-0-1/sec in almost all cells.7. When the perfusion fluid contained 3 x 10-7 M to 104 M ACh the spike frequency increased up to about 2/sec. This stimulatory effect of ACh was blocked by 10-7 M atropine but not by 10-3 M hexamethonium nor by 10-5 M-d-tubocurarine.8. The importance of Ca entry during action potentials for catecholamine secretion is discussed.

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Histochemical Demonstration of Noradrenaline and Adrenaline in the Adrenal Medulla

Cited by 156 publications

References 11 publications

Coexistence and gene expression of phenylethanolamine N-methyltransferase, tyrosine hydroxylase, and neuropeptide tyrosine in the rat and bovine adrenal gland: effects of reserpine.

Coexistence and gene expression of phenylethanolamine N-methyltransferase, tyrosine hydroxylase, and neuropeptide tyrosine in the rat and bovine adrenal gland: effects of reserpine.

Electrical excitability of cultured adrenal chromaffin cells.

Action potentials in the rat chromaffin cell and effects of acetylcholine.

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