Show simple item record

dc.contributor.authorPetrou, Steven
dc.contributor.authorOrdway, Richard W.
dc.contributor.authorHamilton, James A.
dc.contributor.authorWalsh, John V.
dc.contributor.authorSinger, Joshua J.
dc.date2022-08-11T08:09:02.000
dc.date.accessioned2022-08-23T16:16:27Z
dc.date.available2022-08-23T16:16:27Z
dc.date.issued1994-03-01
dc.date.submitted2008-11-25
dc.identifier.citation<p>J Gen Physiol. 1994 Mar;103(3):471-86.</p>
dc.identifier.issn0022-1295 (Print)
dc.identifier.doi10.1085/jgp.103.3.471
dc.identifier.pmid8195783
dc.identifier.urihttp://hdl.handle.net/20.500.14038/34335
dc.description.abstractWe determined the structural features necessary for fatty acids to exert their action on K+ channels of gastric smooth muscle cells. Examination of the effects of a variety of synthetic and naturally occurring lipid compounds on K+ channel activity in cell-attached and excised membrane patches revealed that negatively charged analogs of medium to long chain fatty acids (but not short chain analogs) as well as certain other negatively charged lipids activate the channels. In contrast, positively charged, medium to long chain analogs suppress activity, and neutral analogs are without effect. The key requirements for effective compounds seem to be a sufficiently hydrophobic domain and the presence of a charged group. Furthermore, those negatively charged compounds unable to "flip" across the bilayer are effective only when applied at the cytosolic surface of the membrane, suggesting that the site of fatty acid action is also located there. Finally, because some of the effective compounds, for example, the fatty acids themselves, lysophosphatidate, acyl Coenzyme A, and sphingosine, are naturally occurring substances and can be liberated by agonist-activated or metabolic enzymes, they may act as second messengers targeting ion channels.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8195783&dopt=Abstract">Link to article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2216847/
dc.subjectAcyl Coenzyme A; Amines; Animals; Bufo marinus; Cell Separation; Electrochemistry; Electrophysiology; Fatty Acids; Lipid Bilayers; Lipids; Lysophospholipids; Muscle, Smooth; Potassium Channels; Sphingosine
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleStructural requirements for charged lipid molecules to directly increase or suppress K+ channel activity in smooth muscle cells. Effects of fatty acids, lysophosphatidate, acyl coenzyme A and sphingosine
dc.typeJournal Article
dc.source.journaltitleThe Journal of general physiology
dc.source.volume103
dc.source.issue3
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/983
dc.identifier.contextkey672511
html.description.abstract<p>We determined the structural features necessary for fatty acids to exert their action on K+ channels of gastric smooth muscle cells. Examination of the effects of a variety of synthetic and naturally occurring lipid compounds on K+ channel activity in cell-attached and excised membrane patches revealed that negatively charged analogs of medium to long chain fatty acids (but not short chain analogs) as well as certain other negatively charged lipids activate the channels. In contrast, positively charged, medium to long chain analogs suppress activity, and neutral analogs are without effect. The key requirements for effective compounds seem to be a sufficiently hydrophobic domain and the presence of a charged group. Furthermore, those negatively charged compounds unable to "flip" across the bilayer are effective only when applied at the cytosolic surface of the membrane, suggesting that the site of fatty acid action is also located there. Finally, because some of the effective compounds, for example, the fatty acids themselves, lysophosphatidate, acyl Coenzyme A, and sphingosine, are naturally occurring substances and can be liberated by agonist-activated or metabolic enzymes, they may act as second messengers targeting ion channels.</p>
dc.identifier.submissionpathgsbs_sp/983
dc.contributor.departmentDepartment of Physiology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages471-86


This item appears in the following Collection(s)

Show simple item record