| Concentration dependent effect of GsMTx4 on mechanosensitive channels of small conductance in E. coli spheroplasts. | |
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MedLine Citation:
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PMID: 19132368 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The spider peptide GsMTx4, at saturating concentration of 5 muM, is an effective and specific inhibitor for stretch-activated mechanosensitive (MS) channels found in a variety of eukaryotic cells. Although the structure of the peptide has been solved, the mode of action remains to be determined. Because of its amphipathic structure, the peptide is proposed to interact with lipids at the boundaries of the MS channel proteins. In addition, GsMTx4 has antimicrobial effects, inhibiting growth of several species of bacteria in the range of 5-64 microM. Previous studies on prokaryotic MS channels, which serve as model systems to explore the principle of MS channel gating, have shown that various amphipathic compounds acting at the protein-lipid interface affect MS channel gating. We have therefore analyzed the effect of different concentrations of extracellular GsMTx4 on MS channels of small conductance, MscS and MscK, in the cytoplasmic membrane of wild-type E. coli spheroplasts using the patch-clamp technique. Our study shows that the peptide GsMTx4 exhibits a biphasic response in which peptide concentration determines inhibition or potentiation of activity in prokaryotic MS channels. At low peptide concentrations of 2 and 4 microM the gating of the prokaryotic MS channels was hampered, manifested by a decrease in pressure sensitivity. In contrast, application of peptide at concentrations of 12 and 20 microM facilitated prokaryotic MS channel opening by increasing the pressure sensitivity. |
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Authors:
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Annette C Hurst; Philip A Gottlieb; Boris Martinac |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2009-01-09 |
Journal Detail:
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Title: European biophysics journal : EBJ Volume: 38 ISSN: 1432-1017 ISO Abbreviation: Eur. Biophys. J. Publication Date: 2009 Apr |
Date Detail:
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Created Date: 2009-03-17 Completed Date: 2009-06-02 Revised Date: 2011-09-20 |
Medline Journal Info:
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Nlm Unique ID: 8409413 Medline TA: Eur Biophys J Country: Germany |
Other Details:
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Languages: eng Pagination: 415-25 Citation Subset: IM |
Affiliation:
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Molecular Biophysics Laboratory, School of Biomedical Sciences, University of Queensland, St Lucia, QLD, 4072, Australia. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cell Membrane / physiology Escherichia coli / metabolism* Escherichia coli Proteins / metabolism* Ion Channels / metabolism* Mechanotransduction, Cellular / physiology Membrane Potentials Patch-Clamp Techniques Peptides / metabolism* Spheroplasts / metabolism* Spider Venoms / metabolism* Spiders |
| Chemical | |
Reg. No./Substance:
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0/Escherichia coli Proteins; 0/Ion Channels; 0/MTx4 protein, Grammostola spatulata; 0/MscS protein, E coli; 0/Peptides; 0/Spider Venoms |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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