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Summary

Activation of protein kinase C by biologically active phorbol esters (4β-phorbol 12,13-dibutyrate or 4β-phorbol 12-myristate,13-acetate) promotes the expression of the inducible form of nitric oxide synthase in primary cultures of peritoneal macrophages and hepatocytes. The induction process is clearly observed after short (hours) incubation periods with phorbol esters, and is antagonized by endotoxins and some cytokines, recognized by their ability to induce nitric oxide synthase, such as the lipopolysaccharides from the outer wall of Gram negative bacteria. The co-stimulatory effect among cytokines, growth factors, tumor promoters and endotoxins reveal a complex regulatory mechanism in the control of the nitric oxide synthase expression.

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Hortelano, S., Genaro, A.M., Díaz-Guerra, M.J.M., Boscá, L. (1994). Induction of Nitric Oxide Synthase after Protein Kinase C Activation by Phorbol Esters. In: Municio, A.M., Miras-Portugal, M.T. (eds) Cell Signal Transduction, Second Messengers, and Protein Phosphorylation in Health and Disease. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1879-2_5

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  • DOI: https://doi.org/10.1007/978-1-4615-1879-2_5

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