Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
26
|
pubmed:dateCreated |
1993-10-7
|
pubmed:abstractText |
Insect defensins are cationic, cysteine-rich peptides (approximately 4 kDa) that appear after bacterial challenge or injury in the hemolymph of insects belonging to a large variety of orders. These peptides possess anti-Gram-positive activity and participate in the potent antibacterial defense reactions of insects. Using recombinant insect defensin and the strain Micrococcus luteus as a test organism, we have investigated the mode of action of this peptide. We show that defensin disrupts the permeability barrier of the cytoplasmic membrane of M. luteus, resulting in a loss of cytoplasmic potassium, a partial depolarization of the inner membrane, a decrease in cytoplasmic ATP, and an inhibition of respiration. Potassium loss is inhibited below the order-disorder transition of the lipid hydrocarbon chains. It is also inhibited by divalent cations and by a decrease in the membrane potential below a threshold of 110 mV. We propose that these permeability changes reflect the formation of channels in the cytoplasmic membrane by defensin oligomers. This proposal is supported by patch-clamp experiments that show that insect defensins form channels in giant liposomes.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Defensins,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
268
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
19239-45
|
pubmed:dateRevised |
2003-11-14
|
pubmed:meshHeading |
pubmed-meshheading:7690029-Adenosine Triphosphate,
pubmed-meshheading:7690029-Animals,
pubmed-meshheading:7690029-Anti-Bacterial Agents,
pubmed-meshheading:7690029-Blood Proteins,
pubmed-meshheading:7690029-Cell Membrane,
pubmed-meshheading:7690029-Cytoplasm,
pubmed-meshheading:7690029-Defensins,
pubmed-meshheading:7690029-Hydrogen-Ion Concentration,
pubmed-meshheading:7690029-Insects,
pubmed-meshheading:7690029-Ion Channels,
pubmed-meshheading:7690029-Kinetics,
pubmed-meshheading:7690029-Membrane Potentials,
pubmed-meshheading:7690029-Micrococcus luteus,
pubmed-meshheading:7690029-Osmolar Concentration,
pubmed-meshheading:7690029-Oxygen Consumption,
pubmed-meshheading:7690029-Potassium,
pubmed-meshheading:7690029-Recombinant Proteins,
pubmed-meshheading:7690029-Temperature
|
pubmed:year |
1993
|
pubmed:articleTitle |
Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in Micrococcus luteus.
|
pubmed:affiliation |
Laboratoire de Biologie Générale, Université Louis Pasteur, URA 1490 Centre National de la Recherche Scientifique Bases Cellulaires et Moléculaires de la Réponse Immunitaire des Insectes, Strasbourg, France.
|
pubmed:publicationType |
Journal Article
|