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ID 46918
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Author
Nakao, Satoshi
Komagoe, Keiko
Abstract
The membrane-permeabilizing activities of mastoparans and related histamine-releasing agents were compared through measurements of K(+) efflux from bacteria, erythrocytes, and mast cells. Changes in bacterial cell viability, hemolysis, and histamine release, as well as in the shape of erythrocytes were also investigated. The compounds tested were mastoparans (HR1, a mastoparan from Polistes jadwagae, and a mastoparan from Vespula lewisii), granuliberin R, mast cell-degranulating peptide, and compound 48/80, as well as antimicrobial peptides, such as magainin I, magainin II, gramicidin S. and melittin. We used a K(+)-selective electrode to determine changes in the permeability to K(+) of the cytoplasmic membranes of cells. Consistent with the surface of mast cells becoming negatively charged during histamine release, due to the translocation of phosphatidylserine to the outer leaflet of the cytoplasmic membrane, histamine-releasing agents induced K(+) efflux from mast cells, dependent on their ability to increase the permeability of bacterial cytoplasmic membranes rich in negatively charged phospholipids. The present results demonstrated that amphiphilic peptides, possessing both histamine-releasing and antimicrobial capabilities, induced the permeabilization of the cytoplasmic membranes of not only bacteria but mast cells. Mastoparans increased the permeability of membranes in human erythrocytes at higher concentrations, and changed the normal discoid shape to a crenated form. The structural requirement for making the crenated form was determined using compound 48/80 and its constituents (monomer, dimer, and trimer), changing systematically the number of cationic charges of the molecules.
Keywords
Mastoparan
Compound 48/80
Antimicrobial peptide
Histamine-releasing agent
Membrane permeability
Cell shape
Published Date
2011-01
Publication Title
Biochimica et Biophysica Acta (BBA) - Biomembranes
Volume
volume1808
Issue
issue1
Publisher
Elsevier Science BV.
Start Page
490
End Page
497
ISSN
0005-2736
NCID
AA00564657
Content Type
Journal Article
language
英語
Copyright Holders
© 2010 Elsevier B.V. All rights reserved.
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Refereed
True
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