Characterization of Muscarinic Cholinergic Receptors in the Crab Nervous System

David L. Barker, Thomas F. Murray, Joseph F. Siebenaller, George J. Mpitsos

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

Abstract: The selective muscarinic antagonist L‐[3H]‐quinuclidinyl benzilate (L‐[3H]QNB) binds reversibly and with high affinity (KD= 0.3 nM) to a single population (Bmax= 105 fmol/mg protein) of specific sites in nervous tissue of the crab Cancer magister. The binding site is stereoselective; (‐)QNB is over 200 times more potent than (+)QNB as an inhibitor of specific L‐[3H]QNB binding. The muscarinic antagonists scopolamine and atropine are over 10,000 times more potent inhibitors of L‐[3H]QNB binding than the nicotinic antagonists deca‐methonium and d‐tubocurarine. The muscarinic agonists oxotremorine, pilocarpine, arecoline, and carbachol also compete effectively for the L‐[3H]QNB binding site. This pharmacological profile strongly suggests the presence of classical muscarinic receptors in the crab nervous system. These receptors are localized to nervous tissue containing cell bodies and neuropil, whereas specific L‐[3H]QNB binding is low or absent in peripheral nerve, skeletal muscle, and artery.

Original languageEnglish (US)
Pages (from-to)583-588
Number of pages6
JournalJournal of Neurochemistry
Volume46
Issue number2
DOIs
StatePublished - Feb 1986
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cellular and Molecular Neuroscience

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