Disease relevance of Pyrularia

• Synthetic and structural studies on Pyrularia pubera thionin: a single-residue mutation enhances activity against Gram-negative bacteria [1].
• We investigated the mode of action of Pyrularia thionin on adenylate cyclase in S49 lymphoma cell membranes [2].

High impact information on Pyrularia

• Pyrularia thionin, isolated from nuts of Pyrularia pubera, is a strongly basic peptide of 47 amino acids [3].
• Depolarization of sartorius muscle by Pyrularia thionin also requires a functional Ca2+ channel, as shown by verapamil inhibition [3].
• Interactions of thionin from Pyrularia pubera with dipalmitoylphosphatidylglycerol large unilamellar vesicles [4].
• The PLA2 inhibitor aristolochic acid (10 microM) blocked IL-1 beta-induced IL-6 release and the release of IL-6 caused by Pyrularia pubera thionin (5 micrograms/ml), a stimulator of PLA2 activity [5].
• In this respect they resemble thionins described previously from various cereals and from Pyrularia pubera, which also contain eight cysteine residues at identical positions [6].

Biological context of Pyrularia

• A toxic thionin from Pyrularia pubera: purification, properties, and amino acid sequence [7].

Anatomical context of Pyrularia

• 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 [8].
• The results of the recent study (VERNON, L. P. and ROGERS, A., Toxicon 30, 701-709) agree with this companion study on the binding of 125I-labeled pyrularia thionin and cardiotoxin to erythrocytes under the same conditions [9].
• Effects of different antagonists on depolarization of cultured chick myotubes by cobra venom cardiotoxins and Pyrularia thionin from the plant Pyrularia pubera [10].

Associations of Pyrularia with chemical compounds

• The general response of cells to Pyrularia thionin involves a membrane alteration leading to depolarization and a channel-mediated influx of Ca2+ [3].
• Pyrularia thionin increases arachidonate liberation and prolactin and growth hormone release from anterior pituitary cells [11].
• Consistent with coordinate activation of lysosomal enzymes, Pyrularia thionin also stimulates the production of small, trichloroacetic acid-soluble peptides and nucleic acid fragments from biosynthetically-labelled RNA and proteins in treated cells [8].
• Modification of Trp 8 with N-bromosuccinimide inhibits the hemolytic activity of the thionin, showing that Trp 8 is necessary for Pyrularia thionin activity [12].
• Pyrularia thionin (P. thionin) is a strongly basic peptide of 47 amino acids which is hemolytic, cytotoxic and neurotoxic [13].

Gene context of Pyrularia

• Dopamine, a physiological inhibitor of prolactin release that closes calcium channels, decreased prolactin release stimulated by Pyrularia thionin [11].
• We have chosen the Pyrularia pubera thionin, a 47-residue peptide with four internal disulfides and a remarkable resistance to most proteases, as a representative member of this type of cysteine-rich peptides and have shown that a combination of partial reduction and cyanylation readily allows the determination of its disulfide bonds [14].

References