scholarly journals Tyrosine Phosphorylation of Focal Adhesion Kinase and Paxillin Regulates the Signaling Mechanism of the Rapid Nongenomic Action of Dexamethasone on Actin Cytoskeleton

1999 ◽  
Vol 5 (11) ◽  
pp. 731-742 ◽  
Author(s):  
Sevasti B. Koukouritaki ◽  
Achille Gravanis ◽  
Christos Stournaras
1999 ◽  
Vol 5 (6) ◽  
pp. 382-392 ◽  
Author(s):  
S. B. Koukouritaki ◽  
E. A. Vardaki ◽  
E. A. Papakonstanti ◽  
E. Lianos ◽  
C. Stournaras ◽  
...  

1994 ◽  
Vol 269 (41) ◽  
pp. 25247-25250
Author(s):  
C Zhang ◽  
M P Lambert ◽  
C Bunch ◽  
K Barber ◽  
W S Wade ◽  
...  

2002 ◽  
Vol 70 (7) ◽  
pp. 3804-3815 ◽  
Author(s):  
Giorgio Santoni ◽  
Roberta Lucciarini ◽  
Consuelo Amantini ◽  
Jordan Jacobelli ◽  
Elisabetta Spreghini ◽  
...  

ABSTRACT The signaling pathways triggered by adherence of Candida albicans to the host cells or extracellular matrix are poorly understood. We provide here evidence in C. albicans yeasts of a p105 focal adhesion kinase (Fak)-like protein (that we termed CaFak), antigenically related to the vertebrate p125Fak, and its involvement in integrin-like-mediated fungus adhesion to vitronectin (VN) and EA.hy 926 human endothelial cell line. Biochemical analysis with different anti-chicken Fak antibodies identified CaFak as a 105-kDa protein and immunofluorescence and cytofluorimetric analysis on permeabilized cells specifically stain C. albicans yeasts; moreover, confocal microscopy evidences CaFak as a cytosolic protein that colocalizes on the membrane with the integrin-like VN receptors upon yeast adhesion to VN. The protein tyrosine kinase (PTK) inhibitors genistein and herbimycin A strongly inhibited C. albicans yeast adhesion to VN and EA.hy 926 endothelial cells. Moreover, engagement of αvβ3 and αvβ5 integrin-like on C. albicans either by specific monoclonal antibodies or upon adhesion to VN or EA.hy 926 endothelial cells stimulates CaFak tyrosine phosphorylation that is blocked by PTK inhibitor. A role for CaFak in C. albicans yeast adhesion was also supported by the failure of VN to stimulate its tyrosine phosphorylation in a C. albicans mutant showing normal levels of CaFak and VNR-like integrins but displaying reduced adhesiveness to VN and EA.hy 926 endothelial cells. Our results suggest that C. albicans Fak-like protein is involved in the control of yeast cell adhesion to VN and endothelial cells.


Digestion ◽  
1999 ◽  
Vol 60 (2) ◽  
pp. 153-160 ◽  
Author(s):  
Karlheinz Kiehne ◽  
Karl H. Herzig ◽  
Ulrich R. Fölsch

Sign in / Sign up

Export Citation Format

Share Document