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Am J Physiol Cell Physiol 277: C1021-C1028, 1999;
0363-6143/99 $5.00
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Vol. 277, Issue 6, C1021-C1028, December 1999

INVITED REVIEW
Role of protein phosphatases in the regulation of human mast cell and basophil function

Matthew J. Peirce1, Michael R. Munday2, and Peter T. Peachell1

1 Section of Molecular Pharmacology and Pharmacogenetics, University of Sheffield, Sheffield S10 2JF; and 2 Department of Pharmaceutical and Biological Chemistry, School of Pharmacy, University of London, London WC1N 1AX, United Kingdom

Many extracellular stimuli mediate physiological change in target cells by altering the phosphorylation state of proteins. These alterations result from the dynamic interplay of protein kinases, which mediate phosphorylations, and protein phosphatases, which catalyse dephosphorylations. The antigen-mediated aggregation of high-affinity receptors for IgE on mast cells and basophils triggers rapid changes in the phosphorylation of many proteins and culminates in the generation of inflammatory mediators involved in allergic inflammatory diseases such as asthma. Although protein kinases have an established role in this process, less is known about the involvement of protein phosphatases. This imbalance has been redressed in recent years by the availability of phosphatase inhibitors, such as okadaic acid, that facilitate investigations of the role of protein phosphatases in intact cells. Here we review a number of studies in which inhibitors of protein phosphatases have been used to shed light on the potential importance of these enzymes in the regulation of human mast cell and human basophil function.

okadaic acid; calyculin A; cyclosporin; FK506; dephosphorylation; histamine release


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