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Regulated secretion is impaired in AtT-20 endocrine cells stably transfected with botulinum neurotoxin type A light chain
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Botulinum neurotoxin type A (BoNT/A) inhibits neurotransmitter release by specific cleavage of SNAP-25, a synaptosome-associated protein also expressed in the ACTH secretory cell line AtT-20. Expression of light chain BoNT/A (L-BoNT/A) gene transfected into AtT-20 cells resulted in a cleaved form of SNAP-25 indistinguishable from that generated by bona fide BoNT/A. L-BoNT/A-transfected cells showed no difference in replication rate, viability, or phenotype, compared with control AtT-20 cells. In contrast, L-BoNT/A-transfected cells could not be induced to secrete ACTH upon stimulation by 8-bromo-cAMP or KCl. In addition, alpha-latrotoxin induced ACTH release from control cells, but not from L-BoNT/A-transfected cells. These experiments suggest an important role for SNAP-25 in regulated secretion from AtT-20 cells and underline the usefulness of this cell system as a tool for the study of the molecular mechanism of peptide hormone secretion.
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AGUADO TOMÀS, Fernando, et al. Regulated secretion is impaired in AtT-20 endocrine cells stably transfected with botulinum neurotoxin type A light chain. Journal of Biological Chemistry. 1997. Vol. 272, num. 41, pags. 26005-26008. ISSN 0021-9258. [consulted: 18 of June of 2026]. Available at: https://hdl.handle.net/2445/177587