Autoradiographic localization of strychnine-sensitive glycine receptor in bovine adrenal medulla

Yadid, Gal; Maor, Gila; Youdim, Moussa B. H.; Silberman, M.; Zinder, Oren

doi:10.1007/bf00966683

Cited by 7 publications

(2 citation statements)

References 12 publications

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“…High-affinity [ 3 H]strychnine binding sites have been shown to exist in catecholamine-secreting chromaffin cells of the adrenal medulla (415,416). The same group subsequently demonstrated that glycine can stimulate significant catecholamine secretion from chromaffin cells in both in vitro and in vivo assays (414,417).…”

Section: Adrenomedullary Chromaffin Cellsmentioning

confidence: 99%

Molecular Structure and Function of the Glycine Receptor Chloride Channel

Lynch¹

2004

Physiological Reviews

686

732

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The glycine receptor chloride channel (GlyR) is a member of the nicotinic acetylcholine receptor family of ligand-gated ion channels. Functional receptors of this family comprise five subunits and are important targets for neuroactive drugs. The GlyR is best known for mediating inhibitory neurotransmission in the spinal cord and brain stem, although recent evidence suggests it may also have other physiological roles, including excitatory neurotransmission in embryonic neurons. To date, four alpha-subunits (alpha1 to alpha4) and one beta-subunit have been identified. The differential expression of subunits underlies a diversity in GlyR pharmacology. A developmental switch from alpha2 to alpha1beta is completed by around postnatal day 20 in the rat. The beta-subunit is responsible for anchoring GlyRs to the subsynaptic cytoskeleton via the cytoplasmic protein gephyrin. The last few years have seen a surge in interest in these receptors. Consequently, a wealth of information has recently emerged concerning GlyR molecular structure and function. Most of the information has been obtained from homomeric alpha1 GlyRs, with the roles of the other subunits receiving relatively little attention. Heritable mutations to human GlyR genes give rise to a rare neurological disorder, hyperekplexia (or startle disease). Similar syndromes also occur in other species. A rapidly growing list of compounds has been shown to exert potent modulatory effects on this receptor. Since GlyRs are involved in motor reflex circuits of the spinal cord and provide inhibitory synapses onto pain sensory neurons, these agents may provide lead compounds for the development of muscle relaxant and peripheral analgesic drugs.

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Section: Adrenomedullary Chromaffin Cellsmentioning

confidence: 99%

Molecular Structure and Function of the Glycine Receptor Chloride Channel

Lynch¹

2004

Physiological Reviews

686

732

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“…The chromaffin cell has been extensively studied as a cholinergic neurosecretory system, and activation of the nicotinic receptor in these cells leads to the Ca2l-dependent exocytotic release of catecholamines, adenosine triphosphate (ATP), chromogranins and enkephalins (Livett, 1984). Recently, Yadid et al (1989Yadid et al ( , 1993 showed that bovine adrenal medullary chromaffin cells possess a high affinity [3H]strychnine binding site. These authors also showed that glycine and milacemide, a glycine prodrug, can evoke catecholamine release from slices of adrenal medullary tissue and from freshly isolated chromaffin cells (Yadid et al, 1991;.…”

Section: Introductionmentioning

confidence: 99%

Inhibitory effect of strychnine on acetylcholine receptor activation in bovine adrenal medullary chromaffin cells

Kuijpers

Vergara

Calvo

et al. 1994

British J Pharmacology

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1 Strychnine, which is known as a potent and selective antagonist of the inhibitory glycine receptor in the central nervous system, inhibits the nicotinic stimulation of catecholamine release from bovine cultured adrenal chromaffin cells in a concentration-dependent (1-1100 AM) manner. At 10 JAM nicotine, the IC3o value for strychnine is approximately 30 tiM. Strychnine also inhibits the nicotine-induced membrane depolarization and increase in intracellular Ca2+ concentration. 2 The inhibitory action of strychnine is reversible and is selective for nicotinic stimulation, with no effect observed on secretion elicited by a high external K+ concentration, histamine or angiotensin II. 3 Strychnine competes with nicotine in its effect, but does not modify the apparent positive cooperativity of the nicotine binding sites. In the absence of nicotine, strychnine has no effect on catecholamine release. Glycine does not affect catecholamine release nor the inhibitory action of strychnine on this release. 4 These results suggest that strychnine interacts with the agonist binding site of the nicotinic acetylcholine receptor in chromaffin cells, thus exerting a pharmacological effect independently of the glycine receptor.

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