Phorbol ester activation of the isotypes of protein kinase C from bovine and rat brain.
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Animals↗
Biomedical subjects
W J Ryves
Publications and source records attributed to W J Ryves.
Investigation of the tissue distribution of the calcium independent kinase, Rx kinase; which is distinct from known isozymes of protein kinase C.
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Animals↗
TPA and resiniferatoxin-mediated activation of NADPH-oxidase. A possible role for Rx-kinase augmentation of PKC.
The non-tumour promoting irritant, resiniferatoxin, was capable of activating the NADPH-oxidase respiratory burst of starch-elicited, but not resident mouse peritoneal macrophages in vitro. Unlike TPA, the response was synergised by incubation with zymosan. The Rx-stimulated NADPH-oxidase activity in a cell-free assay was selectively enhanced in the presence of exogenous Rx-kinase rather than PKC and in the absence of Ca2+. Since resiniferatoxin is a poor activator of PKC, it is probable that the Ca2(+)-independent Rx-kinase plays a role in activation of the macrophage respiratory burst following stimulation by zymosan.
Animals↗
A phorbol ester and a daphnane ester stimulate a calcium-independent kinase activity from human mononuclear cells.
TPA and a non-promoting, pro-inflammatory ester RX were used to stimulate the forms of PKC isolated from human mononuclear cells. Three peaks of kinase activity corresponding to gamma, beta and alpha PKC were stimulated by TPA in the presence and absence of calcium and/or phosphatidylserine (PS) but were not activated by RX. A fourth peak eluted at high phosphate concentration was activated by TPA and RX in the presence of PS and the absence of calcium. Activity in this fraction was labile to freezing and thawing and was inhibited by staurosporine.
Alkaloids↗