A role for tyrosine kinase activation in interleukin-1β induced nitric oxide production in the insulin producing cell line RINm-5F. Issue 1 (February 1994)

• Record Type: Journal Article
• Authors: Welsh, Nils
• Is Part Of: Bioscience reports. Volume 14:Issue 1(1994)
• Page Start: 43
• Page End: 50
• Publication Date: 1994-02
• Subjects: interleukin-1 -- nitric oxide -- insulin -- tyrosine kinase -- phosphatase; Molecular biology -- Periodicals; Cytology -- Periodicals; 572.8
• DOI: 10.1007/BF01901637
• Languages: English
• ISSNs: 0144-8463

Abstract

Abstract : The aim of this investigation was to study the putative role of protein phosphorylation in interleukin-1β (IL-1β) induced signal transduction in insulin producing cells. For this purpose, insulin producing RINm-5F cells were exposed to IL-1β for 7 hours with or without different agonists and antagonists to protein kinases and phosphatases and the production of nitrite was subsequently determined. It has been shown earlier that IL-1β will stimulate the production of nitrite in such cells. It was found that EDTA, TPA and staurosporine did not affect IL-1β induced nitrite production. However, the tyrosine kinase antagonist tyrphostin inhibited, whereas sodium orthovanadate, okadaic acid and cyclosporin A, all inhibitors of protein phosphatases, potentiated IL-1β induced nitrite release to the medium. The tyrosine kinase antagonist genistein potentiated at a low concentration and inhibited at a high concentration the IL-1β effect. It is concluded that protein phosphorylation events, mediated either by protein kinases or phosphatases on both tyrosine and serine/threonine residues, may mediate or antagonize IL-1 induced signal transduction in insulin producing cells.