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- W2057943668 abstract "A short synthetic peptide (Pa) containing a structural motif (2-6-11 motif) present in a number of human extracellular matrix proteins was found to stimulate the production of cytokines IL-1alpha, IL-1beta, IL-6, and TNFalpha by human peripheral blood mononuclear cells. We have now investigated the signal transduction pathway involved in the elicitation of these immunomodulating properties on isolated human monocytes. Our results show that active peptide Pa provoked phosphoinositide hydrolysis, intracellular calcium elevation, and cAMP accumulation. Herbimycin A, an inhibitor of protein tyrosine kinases (PTK), markedly reduced these effects of peptide Pa. We have also found that this peptide stimulated CREB, NF-kappaB, and AP-1 DNA-binding activity. With the help of inhibitors of PTK (herbimycin A), phospholipase C (neomycin sulfate), protein kinase C (bis-indolyl maleimide), protein kinase A (H89), and the calmodulin antagonist W-7, as well as cholera toxin, an agent that increases intracellular cAMP, we showed that cytokine (IL-1alpha, IL-1-beta, IL-6, and TNFalpha) production could be modified by the signal transduction pathway triggered by peptide Pa on monocytes." @default.
- W2057943668 created "2016-06-24" @default.
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- W2057943668 date "1997-02-01" @default.
- W2057943668 modified "2023-09-23" @default.
- W2057943668 title "Signaling Pathway Triggered by a Short Immunomodulating Peptide on Human Monocytes" @default.
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- W2057943668 doi "https://doi.org/10.1006/abbi.1996.9832" @default.
- W2057943668 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9028864" @default.
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