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Beschreibung

A cell-permeable synthetic peptide with a sequence identical to Vespula lewisii. Amphiphilic wasp venom tetradecapeptide capable of directly activating pertussis toxin-sensitive G-proteins by a mechanism analogous to that of G-protein-coupled receptors. Acts preferentially on Gi and Go rather than Gs. Potent factor in mitochondrial permeability transition pore. Inhibits calmodulin and activates phospholipase A2. Causes a transient Ca2+ release from the sarcoplasmic reticulum., A cell-permeable synthetic peptide with sequence identical to Vespula lewisii. Amphiphilic wasp venom tetradecapeptide capable of directly activating pertussis toxin-sensitive G-proteins by a mechanism analogous to that of G-protein-coupled receptors. Acts preferentially on Gi and Go rather than Gs. Potent facilitator of the mitochondrial permeability transition pore that is reported to induce apoptosis in cultured cerebellar granule neurons by causing a dramatic increase in intracellular Ca2+. Acts as a calmodulin antagonist and activates phospholipase A2. Causes a transient Ca2+ release from the sarcoplasmic reticulum. Also reported to inhibit Na+,K+-ATPase activity (IC50 = 7.5 µ,M).

Strukturformel

Mastoparan, Vespula lewisii

Inhalte

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