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pyrularia/phospholipid
Länken sparas på Urklipp
8 resultat
Modification of phospholipid membrane structure by the plant toxic peptide Pyrularia thionin.
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Pyrularia thionin (P thionin) is a bioactive peptide from the parasitic plant Pyrularia pubera. The structural aspects of its interaction with phospholipid membranes were investigated by measuring the responses of phosphorescence quenching, EPR spin labels, and 1H and 31P NMR at different
Pyrularia thionin. Physical properties, binding to phospholipid bilayers and cellular responses.
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Pyrularia thionin increases arachidonate liberation and prolactin and growth hormone release from anterior pituitary cells.
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Pyrularia thionin is a 47 amino acid peptide isolated from the nuts of Pyrularia pubera. This peptide does not have intrinsic phospholipase A2 activity, but it increases the liberation of arachidonate from several tissues. Exposure of anterior pituitary cells to this toxin increases the liberation
Phospholipase activation in the cytotoxic mechanism of thionin purified from nuts of Pyrularia pubera.
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Treating NIH3T3 fibroblast cells with Pyrularia pubera thionin (100 micrograms/ml) stimulated release of labelled free fatty acids from phospholipids biosynthetically labelled by incorporation of [3H]arachidonic acid. Since Pyrularia thionin exhibited no detectable phospholipase activity, it was
Effect of calcium and phosphate ions on hemolysis induced by Pyrularia thionin and Naja naja kaouthia cardiotoxin.
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Pyrularia thionin is a strongly basic bioactive peptide of 47 amino acids isolated from nuts of Pyrularia pubera. It is hemolytic, cytotoxic and activates an endogenous phospholipase A2 in 3T3 cells. Earlier studies have shown that the cardiotoxin from Naja naja kaouthia has similar activities and
Pyrularia thionin binding to and the role of tryptophan-8 in the enhancement of phosphatidylserine domains in erythrocyte membranes.
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Pyrularia thionin is a small, strongly basic peptide which interacts readily with cellular and synthetic membranes. With cells it induces hemolysis, depolarizes the cellular membrane with an accompanying influx of Ca2+, and activates an endogenous phospholipase A2. Evidence points toward a binding
Binding to and hemolysis of human erythrocytes by pyrularia thionin and Naja naja kaouthia cardiotoxin: inhibition by prothrombin.
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Pyrularia thionin and snake venom cardiotoxin are strongly basic proteins which bind to and induce hemolysis of erythrocytes, cause depolarization of muscle cells, and influence the order and properties of phospholipids in cellular membranes. Earlier studies showed a competition between the thionin
Induction of interleukin-6 release by interleukin-1 in rat anterior pituitary cells in vitro: evidence for an eicosanoid-dependent mechanism.
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We have reported previously that a subpopulation(s) of anterior pituitary cells released IL-6 and that this release was stimulated by interleukin-1 (IL-1) through a non-cAMP-dependent mechanism. We now report that IL-1 induces IL-6 release from anterior pituitary cells in an eicosanoid-dependent
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