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Protein tyrosine phosphatase activity enhancement is induced upon Fcɛreceptor activation of mast cells

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
346
Identifiers
DOI: 10.1016/0014-5793(94)00471-4
Keywords
  • Rbl-2H3 Line
  • Immunological Signal Transduction
  • Rat Mucosal Mast Cell
Disciplines
  • Biology

Abstract

Abstract Immunological stimulation of rat mucosal type mast cells (line RBL-2H3) by clustering the type I Fc ɛ receptor (Fc ɛRI) causes a fast and transient tyrosine phosphorylation of several proteins. This implied the involvement of both, protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPases) in that process. In order to identify the PTPases involved in these very early steps coupling Fc ɛRI stimulus to cell response, we undertook the purification and characterization of PTPases present in RBL-2H3 cells. In one of the cells' membranal fractions, a PTPase activity was found to be enhanced 2- to 3-fold upon cell stimulation by Fc ɛRI clustering. Characterization of this activity implies its involvement in control of the FC ɛRI signalling cascade.

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