Pharmacological characterization of a homomeric nicotinic acetylcholine receptor formed by Ancylostoma caninum ACR-16

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dc.contributor.author Musselman, Nicole
dc.contributor.department Biomedical Sciences
dc.contributor.majorProfessor Alan Robterson
dc.date 2019-09-22T17:08:07.000
dc.date.accessioned 2020-06-30T01:36:18Z
dc.date.available 2020-06-30T01:36:18Z
dc.date.copyright Mon Jan 01 00:00:00 UTC 2018
dc.date.issued 2018-01-01
dc.description.abstract <p>Parasitic nematode infections affect millions of people worldwide and are a significant cause of human and veterinary disease. Chronic infections cause debilitating health problems in humans, domestic animals, and livestock. Infections are treated using anthelmintic drugs, some target nicotinic acetylcholine receptors located in several different tissues. The exact mode of action of antinematode drugs is unknown. Research leading to better understand the mode of action is desirable to appreciate how resistance mechanisms develop. There is an urgent need for novel therapeutic agents to overcome resistance.</p> <p>This study considered Anycylstoma caninum ACR-16 as a drug target and was investigated using two-electrode voltage-clamp electrophysiology. This technique allowed us to explore several agonist and antagonists of ACR-16 and their pharmacology expressed in X. <em>laevis</em> oocytes. The sequence of <em>Acn</em>-ACR-16 was compared with <em>Asu</em>-ACR-16, another homomeric nicotinic acetylcholine receptor, but widely distributed in <em>Ascaris</em> tissue. Also, the concentration-current-response relationships and the potencies of agonists are demonstrated for <em>Acn</em>-ACR-16. We concluded that <em>Acn</em>-ACR-16 was not sensitive to many of the currently used cholinomimetic anthelmintics. Though, the <em>A. caninum</em> channel was most sensitive to 3-bromocytisine unlike nicotine which was the most potent agonist for <em>A. suum </em>ACR-16 receptor. When considering antagonist pharmacology, the <em>A. caninum </em>receptor was moderately inhibited by α-BTX while Asu-ACR-16 was almost insensitive.</p>
dc.format.mimetype application/pdf
dc.identifier archive/lib.dr.iastate.edu/creativecomponents/87/
dc.identifier.articleid 1089
dc.identifier.contextkey 13357142
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath creativecomponents/87
dc.identifier.uri https://dr.lib.iastate.edu/handle/20.500.12876/17179
dc.source.bitstream archive/lib.dr.iastate.edu/creativecomponents/87/ACN_ACR_16_manuscript_FINAL.pdf|||Sat Jan 15 02:15:45 UTC 2022
dc.subject.disciplines Medicinal and Pharmaceutical Chemistry
dc.subject.keywords nAChR
dc.subject.keywords hookworms
dc.subject.keywords Acn-ACR-16
dc.subject.keywords anthelmintic
dc.subject.keywords Xenopus expression
dc.title Pharmacological characterization of a homomeric nicotinic acetylcholine receptor formed by Ancylostoma caninum ACR-16
dc.type article
dc.type.genre creativecomponent
dspace.entity.type Publication
relation.isOrgUnitOfPublication 184db3f2-d93f-4571-8ad7-07c8a9e6a5c9
thesis.degree.discipline Biomedical Sciences
thesis.degree.level creativecomponent
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