Abstract
A new teleocidin analog was isolated from the fermentation medium of Streptomyces sp. MM216-87F4 and its structure was elucidated as 14-O-(N-acetylglucosaminyl) teleocidin A (GlcNAc-TA). GlcNAc-TA induces the translocation of protein kinases Cα and θ fused with enhanced green fluorescent protein (PKCα-EGFP and PKCθ-EGFP) to the plasma membrane in stable transfectants, and reduces intracellular calcium mobilization induced by agonists of G-protein coupled receptors in various cell lines without causing irritation of the mouse ear. Further, GlcNAc-TA sensitizes the release of excitatory neuropeptides substance P induced by capsaicin from primary-cultured dorsal root ganglion (DRG) neurons of the rat and GlcNAc-TA alone also triggers substance P release in a dose-dependent manner. This study provides the first observation that a teleocidin analog without a free hydroxyl group at C-14 acts as a PKC activator and directly induces the release of excitatory neuropeptide.
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Nakae, K., Hosokawa, N., Sawa, R. et al. A New Teleocidin Analog from Streptomyces sp. MM216-87F4 Induces Substance P Release from Rat Dorsal Root Ganglion Neurons. J Antibiot 59, 11–17 (2006). https://doi.org/10.1038/ja.2006.3
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DOI: https://doi.org/10.1038/ja.2006.3
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