Agonist Activation of F-Actin-Mediated Eosinophil Shape Change and Mediator Release Is Dependent on Rac2
Author(s) -
Paige Lacy,
Lian Willetts,
John D. Kim,
Andrea N. Lo,
B. Daniël Lam,
E. MacLean,
Redwan Moqbel,
Marc E. Rothenberg,
Nives Zimmermann
Publication year - 2011
Publication title -
international archives of allergy and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.696
H-Index - 100
eISSN - 1423-0097
pISSN - 1018-2438
DOI - 10.1159/000322597
Subject(s) - eosinophil peroxidase , degranulation , superoxide , eosinophil , platelet activating factor , respiratory burst , immunology , chemistry , biology , microbiology and biotechnology , receptor , biochemistry , asthma , enzyme
Tissue recruitment and activation of eosinophils contribute to allergic symptoms by causing airway hyperresponsiveness and inflammation. Shape changes and mediator release in eosinophils may be regulated by mammalian Rho-related guanosine triphosphatases. Of these, Rac2 is essential for F-actin formation as a central process underlying cell motility, exocytosis, and respiratory burst in neutrophils, while the role of Rac2 in eosinophils is unknown.We set out to determine the role of Rac2 in eosinophil mediator release and F-actin-dependent shape change in response to chemotactic stimuli.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom