Protein kinase C regulates leukotriene B4 receptors in human neutrophils
Open Access
- 6 October 1986
- journal article
- Published by Wiley in FEBS Letters
- Vol. 206 (2) , 279-282
- https://doi.org/10.1016/0014-5793(86)80996-6
Abstract
Three protein kinase C (PKC) activators, viz. phorbol myristate acetate, mezerein, and rac‐1‐O‐myristoyl‐2‐acetylglycerol, inhibited human neutrophil binding of [3H] leukotriene B4 (LTB4) by reducing the number of high‐affinity receptors available to the arachidonic acid metabolite. The inhibitory effect occurred in whole cells and cytoplasts but not in isolated membranes; it appeared to involve the activation of PKC rather than direct competition for binding sites. PKC may govern cellular responsiveness by regulating the receptor‐linked bioactions of endogenous mediators like LTB4.Keywords
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