PMID- 10583594
OWN - NLM
STAT- MEDLINE
DCOM- 20000104
LR  - 20220309
IS  - 0019-2805 (Print)
IS  - 1365-2567 (Electronic)
IS  - 0019-2805 (Linking)
VI  - 98
IP  - 3
DP  - 1999 Nov
TI  - Both adhesion to immobilized vitronectin and FcepsilonRI cross-linking cause 
      enhanced focal adhesion kinase phosphorylation in murine mast cells.
PG  - 357-62
AB  - Murine mast cells adhere spontaneously to plate-bound vitronectin (VNPB) via 
      alphav-containing integrins, and this adhesive interaction results in an 
      augmented interleukin-3 (IL-3)-dependent mast-cell proliferation. In this report 
      we demonstrate that the activation of murine mast cells through alphav-integrin, 
      as well as through the high affinity immunoglobulin E (IgE) receptor 
      (FcepsilonRI), results in enhanced tyrosine phosphorylation of focal adhesion 
      kinase (FAK), a cytoplasmic protein tyrosine kinase involved in mitogenic and 
      oncogenic signal transduction. While mast cell adhesion to VNPB resulted in 
      enhanced FAK phosphorylation, treatment with soluble vitronectin (VNSOL) failed 
      to do so. Spontaneous mast cell adhesion to entactin (EN) did not induce tyrosine 
      phosphorylation of FAK, demonstrating that not all adhesive interactions lead to 
      the same sequence of biochemical events. Because FAK has intrinsic tyrosine 
      kinase activity, we examined whether activating mast cells via alphav-integrins, 
      or via FcepsilonRI-cross-linking stimulated the in vitro kinase activity of FAK. 
      Both pathways were found independently to activate FAK in mast cells and together 
      appeared additive. Protein kinase C depletion in mast cells and calcium depletion 
      in the medium caused decreased tyrosine phosphorylation of FAK, indicating that 
      optimal tyrosine phosphorylation of FAK is regulated by both pathways. These data 
      are consistent with the conclusion that the tyrosine phosphorylation of FAK 
      represents at least one example of a point of convergence in the intracellular 
      tyrosine phosphorylation cascades induced by alphav integrin-and 
      FcepsilonRI-mediated signal transduction pathways in mast cells.
FAU - Bhattacharyya, S P
AU  - Bhattacharyya SP
AD  - Laboratory of Allergic Diseases, National Institute of Allergy and Infectious 
      Diseases, National Institutes of Health, Bethesda, MD 20892-1881, USA.
FAU - Mekori, Y A
AU  - Mekori YA
FAU - Hoh, D
AU  - Hoh D
FAU - Paolini, R
AU  - Paolini R
FAU - Metcalfe, D D
AU  - Metcalfe DD
FAU - Bianchine, P J
AU  - Bianchine PJ
LA  - eng
PT  - Journal Article
PL  - England
TA  - Immunology
JT  - Immunology
JID - 0374672
RN  - 0 (Antigens, CD)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Integrin alphaV)
RN  - 0 (Receptors, IgE)
RN  - 0 (Vitronectin)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.10.2 (Focal Adhesion Kinase 1)
RN  - EC 2.7.10.2 (Focal Adhesion Protein-Tyrosine Kinases)
RN  - EC 2.7.10.2 (Ptk2 protein, mouse)
RN  - EC 2.7.11.13 (Protein Kinase C)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Animals
MH  - Antigens, CD/metabolism
MH  - Blotting, Western
MH  - Calcium/metabolism
MH  - Cell Adhesion
MH  - Cell Adhesion Molecules/*metabolism
MH  - Cell Line
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Focal Adhesion Kinase 1
MH  - Focal Adhesion Protein-Tyrosine Kinases
MH  - Integrin alphaV
MH  - Intracellular Fluid/metabolism
MH  - Luminescent Measurements
MH  - Mast Cells/metabolism/*physiology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Phosphorylation
MH  - Protein Kinase C/metabolism
MH  - Protein-Tyrosine Kinases/*metabolism
MH  - Receptor Cross-Talk
MH  - Receptors, IgE/*metabolism
MH  - *Signal Transduction
MH  - Vitronectin/*metabolism
PMC - PMC2326938
EDAT- 1999/12/03 00:00
MHDA- 1999/12/03 00:01
PMCR- 2000/11/01
CRDT- 1999/12/03 00:00
PHST- 1999/12/03 00:00 [pubmed]
PHST- 1999/12/03 00:01 [medline]
PHST- 1999/12/03 00:00 [entrez]
PHST- 2000/11/01 00:00 [pmc-release]
AID - imm883 [pii]
AID - 10.1046/j.1365-2567.1999.00883.x [doi]
PST - ppublish
SO  - Immunology. 1999 Nov;98(3):357-62. doi: 10.1046/j.1365-2567.1999.00883.x.