Overview
- Sobin, B.A. et al. (1954) J. Am. Chem. Soc. 76, 4053.
Protect from light.
Alomone Labs Anisomycin induces p38 SAPK phosphorylation in C6 glioma cells.Cells were grown to 70% confluence, serum starved for 3 h, and then stimulated with various concentrations of Anisomycin (#A-520) for 60 min. Cell proteins were resolved by SDS-PAGE and probed with antiphospho-p38 MAPK (upper panel) or with anti-p38 (lower panel) antibodies.
Anisomycin is a bacterial antibiotic isolated from Streptomyces griseolus, which inhibits protein synthesis by binding to 60S ribosomal subunits and blocking peptide bond formation, thereby preventing elongation and causing polysome stabilization. This action of Anisomycin monitored the cells for chromosomal DNA degradation and apoptosis.1-5
Anisomycin has been widely used as an extremely potent activator of kinase cascades in mammalian cells, especially the stress-activated protein kinase (SAPK2/p38MAPK), kinase subtypes and p46/54JNK.6-13
Synergizes with growth factors and phorbol esters, anisomycin superinduce c-fos and c-jun by a number mechanisms, one of which is its ability to act as a potent signalling agonist, producing strong, prolonged activation of the same nuclear responses as epidermal growth factor or tetradecanoyl phorbol acetate.14
Anisomycin stimulated serine phosphorylation of IRS-1 and IRS-2, reduced their ability to interact with the insulin receptor and by that blocked the insulin-induced tyrosine phosphorylation of IRS proteins.15
