brevetoxin-a and Glioma

brevetoxin-a has been researched along with Glioma* in 2 studies

Other Studies

2 other study(ies) available for brevetoxin-a and Glioma

Article	Year
Artificial ladder-shaped polyethers that inhibit maitotoxin-induced Ca2+ influx in rat glioma C6 cells. Bioorganic & medicinal chemistry letters, 2012, Jun-01, Volume: 22, Issue:11 Maitotoxin (MTX) is a ladder-shaped polyether produced by the epiphytic dinoflagellate Gambierdiscus toxicus. It is known to elicit potent toxicity against mammals and induce influx of Ca(2+) into cells. An artificial ladder-shaped polyether possessing a 6/7/6/6/7/6/6 heptacyclic ring system, which was designed for elucidating interactions with transmembrane proteins, was found to be the most potent inhibitor against MTX-induced Ca(2+) influx that has ever been reported. Topics: Animals; Calcium; Dinoflagellida; Ethers, Cyclic; Glioma; Hydrophobic and Hydrophilic Interactions; Ion Transport; Marine Toxins; Membrane Proteins; Oxocins; Rats; Tumor Cells, Cultured	2012
Inhibition of maitotoxin-induced Ca2+ influx in rat glioma C6 cells by brevetoxins and synthetic fragments of maitotoxin. Journal of neurochemistry, 1998, Volume: 70, Issue:1 45Ca2+ influx in rat glioma C6 cells induced by 0.3 nM maitotoxin (MTX) was markedly inhibited by brevetoxin A (PbTx1) and brevetoxin B (PbTx2), with EC50 values of 16 and 13 microM, respectively. This inhibition was observed immediately after addition of MTX when monitored with fura-2, which suggests that PbTx2 directly blocks the action of MTX. This blockade by PbTx2 was not affected by tetrodotoxin, which excludes the involvement of voltage-sensitive sodium channels. The depolarizing effects of these brevetoxins were also not a likely cause of this inhibition, because melittin, a channel-forming peptide, did not significantly block MTX-induced 45Ca2+ influx. Instead, this inhibition was thought to be mediated by blockade of an MTX-binding site by the brevetoxins, based on the fact that these toxins, particularly PbTx2, closely mimic the partial structure of MTX. Synthetic fragments of MTX corresponding to the hydrophilic EF-GH rings (200 microM) and LM-NO rings (500 microM) of MTX significantly reduced MTX-elicited Ca2+ influx. The observation that the effects of MTX were inhibited by structural mimics of both its hydrophobic and hydrophilic portions implies that both portions of the MTX molecule recognize its target. Topics: Animals; Calcium; Calcium Channel Blockers; Electrophysiology; Fluorescent Dyes; Fura-2; Glioma; Marine Toxins; Molecular Conformation; Oxocins; Peptide Fragments; Rats; Tumor Cells, Cultured	1998

Article

Year

Artificial ladder-shaped polyethers that inhibit maitotoxin-induced Ca2+ influx in rat glioma C6 cells.

Bioorganic & medicinal chemistry letters, 2012, Jun-01, Volume: 22, Issue:11

Maitotoxin (MTX) is a ladder-shaped polyether produced by the epiphytic dinoflagellate Gambierdiscus toxicus. It is known to elicit potent toxicity against mammals and induce influx of Ca(2+) into cells. An artificial ladder-shaped polyether possessing a 6/7/6/6/7/6/6 heptacyclic ring system, which was designed for elucidating interactions with transmembrane proteins, was found to be the most potent inhibitor against MTX-induced Ca(2+) influx that has ever been reported.

Topics: Animals; Calcium; Dinoflagellida; Ethers, Cyclic; Glioma; Hydrophobic and Hydrophilic Interactions; Ion Transport; Marine Toxins; Membrane Proteins; Oxocins; Rats; Tumor Cells, Cultured

2012

Inhibition of maitotoxin-induced Ca2+ influx in rat glioma C6 cells by brevetoxins and synthetic fragments of maitotoxin.

Journal of neurochemistry, 1998, Volume: 70, Issue:1

45Ca2+ influx in rat glioma C6 cells induced by 0.3 nM maitotoxin (MTX) was markedly inhibited by brevetoxin A (PbTx1) and brevetoxin B (PbTx2), with EC50 values of 16 and 13 microM, respectively. This inhibition was observed immediately after addition of MTX when monitored with fura-2, which suggests that PbTx2 directly blocks the action of MTX. This blockade by PbTx2 was not affected by tetrodotoxin, which excludes the involvement of voltage-sensitive sodium channels. The depolarizing effects of these brevetoxins were also not a likely cause of this inhibition, because melittin, a channel-forming peptide, did not significantly block MTX-induced 45Ca2+ influx. Instead, this inhibition was thought to be mediated by blockade of an MTX-binding site by the brevetoxins, based on the fact that these toxins, particularly PbTx2, closely mimic the partial structure of MTX. Synthetic fragments of MTX corresponding to the hydrophilic EF-GH rings (200 microM) and LM-NO rings (500 microM) of MTX significantly reduced MTX-elicited Ca2+ influx. The observation that the effects of MTX were inhibited by structural mimics of both its hydrophobic and hydrophilic portions implies that both portions of the MTX molecule recognize its target.

Topics: Animals; Calcium; Calcium Channel Blockers; Electrophysiology; Fluorescent Dyes; Fura-2; Glioma; Marine Toxins; Molecular Conformation; Oxocins; Peptide Fragments; Rats; Tumor Cells, Cultured

1998