Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Echothiophate and cogeners decrease the voltage dependence of end-plate current decay in frog skeletal muscle.

E G Henderson1, D J Post-Munson, L S Reynolds

  • 1Department of Pharmacology, University of Connecticut Health Center, Farmington 06032.

The Journal of Pharmacology and Experimental Therapeutics
|December 1, 1989
PubMed
Summary

Three irreversible anticholinesterase agents, including echothiophate (217MI), altered acetylcholine receptor ion channel function. These compounds affected end plate currents (e.p.c.s) in frog muscle, suggesting a novel mechanism beyond esterase inhibition.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Expression of cGMP-specific phosphodiesterase 9A mRNA in the rat brain.

The Journal of neuroscience : the official journal of the Society for Neuroscience·2001
Same author

Targeting acute ischemic stroke with a calcium-sensitive opener of maxi-K potassium channels.

Nature medicine·2001
Same author

Structure and promoter activity of the mouse CDC25A gene.

Mammalian genome : official journal of the International Mammalian Genome Society·2000
Same author

Comparison of the novel antipsychotic ziprasidone with clozapine and olanzapine: inhibition of dorsal raphe cell firing and the role of 5-HT1A receptor activation.

Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology·1999
Same author

Antisense inhibition of phosphodiesterase expression.

Methods (San Diego, Calif.)·1998
Same author

Expression and regulation of mRNA for distinct isoforms of cAMP-specific PDE-4 in mitogen-stimulated and leukemic human lymphocytes.

Cell biochemistry and biophysics·1998

Area of Science:

  • Neuroscience
  • Pharmacology
  • Muscle Physiology

Background:

  • Anticholinesterase agents are crucial in treating conditions like myasthenia gravis.
  • Understanding their precise molecular mechanisms is vital for drug development.
  • Irreversible agents like echothiophate have distinct properties compared to reversible ones.

Purpose of the Study:

  • To investigate the effects of irreversible anticholinesterase agents on neuromuscular junction function.
  • To elucidate the mechanism by which these agents alter end plate currents (e.p.c.s).
  • To differentiate the effects from reversible anticholinesterase agents and known receptor interactions.

Main Methods:

  • Electrophysiological recordings of e.p.c.s in Rana pipiens cutaneous pectoris muscle.

Related Experiment Videos

  • Application of irreversible anticholinesterase agents (echothiophate, 217AO, Tetram) and a reversible agent (neostigmine).
  • Manipulation of acetylcholine release (Mg++ addition) and receptor binding assays ([3H]PCP, [125I]alpha-bungarotoxin).

    • Main Results:

    • Irreversible agents decreased e.p.c. decay rate (alpha) similarly to neostigmine.
    • Echothiophate and its derivatives significantly reduced the voltage dependence (H) of alpha, unlike neostigmine.
    • These effects were independent of acetylcholine release and direct receptor binding, and not modified by other irreversible agents.

    Conclusions:

    • Irreversible anticholinesterase agents modulate the acetylcholine receptor ion channel complex.
    • The observed effects on channel gating are distinct from esterase inhibition or channel blockade.
    • These findings suggest a novel mechanism of action for irreversible anticholinesterase agents at the neuromuscular junction.