Alterations in granule matrix and cell surface of focal adhesion kinase-deficient mast cells

Alterations in granule matrix and cell surface of focal adhesion kinase-deficient mast cells

Author Vial, Daniel Google Scholar
Oliver, Constance Google Scholar
Jamur, Maria Célia Google Scholar
Pastor, Maria Verônica Dávilla Google Scholar
Trindade, Edvaldo da Silva Autor UNIFESP Google Scholar
Berenstein, Elisa Google Scholar
Zhang, Juan Google Scholar
Siraganian, Reuben P. Google Scholar
Institution NIDR
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Abstract Focal adhesion kinase (FAK) is a nonreceptor protein tyrosine kinase that plays an important role in many cellular processes and is tyrosine phosphorylated after FcepsilonRI aggregation in mast cells. In mice, null mutation of the fak gene results in a lethal phenotype in which the embryos fail to develop past day 8.5 of gestation. To study the role of FAK in these mast cells, 8.5-day embryos were isolated and placed in culture with IL-3 and stem cell factor (SCF). Although FAK was not required for the development of mast cells in culture, the FAK(-/-) embryo-derived mast cells had several distinct characteristics. Compared with the controls, the mast cells that lack FAK were less metachromatic and by electron microscopy had granules that appeared largely electron lucid, although their histamine content was unchanged. The FAK-deficient mast cells had a reduction in the content of chondroitin/dermatan sulfate, the major glycosaminoglycan component of the granular matrix. The FAK-deficient cells had fewer microvilli that were fused with each other, giving the cell surface a ruffled appearance. There was also a Mold increase in the number of cells highly expressing beta(7) integrin. However, signal transduction from the high affinity IgE receptor for the secretion of histamine was similar in the wild-type, heterozygote, and the FAK-deficient cells. The FcepsilonRI-induced tyrosine phosphorylation of paxillin, Crk-associated tyrosine kinase substrate (CAS), and mitogen-activated protein kinase proteins was independent of FAK. These results indicate that FAK plays a role in regulating the glycosaminoglycan content of the secretory granules and influences the cell surface morphology of mast cells.
Language English
Date 2003-12-01
Published in Journal Of Immunology. Bethesda: Amer Assoc Immunologists, v. 171, n. 11, p. 6178-6186, 2003.
ISSN 0022-1767 (Sherpa/Romeo, impact factor)
Publisher Amer Assoc Immunologists
Extent 6178-6186
Access rights Closed access
Type Article
Web of Science ID WOS:000186767200067

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