Ionizing radiation modules of the expression and tyrosine phosphorylation of the focal adhesion‐associated proteins focal adhesion kinase (FAK) and its substrates p130cas and paxillin in A549 human lung carcinoma cellsin vitro

2003 ◽  
Vol 79 (9) ◽  
pp. 721-731 ◽  
Author(s):  
C. Beinke ◽  
D. Van Beuningen ◽  
N. Cordes
Keyword(s):  
Ionizing Radiation ◽  
Focal Adhesion Kinase ◽  
Tyrosine Phosphorylation ◽  
Focal Adhesion ◽  
Lung Carcinoma ◽  
Human Lung ◽  
Associated Proteins ◽  
Human Lung Carcinoma

scholarly journals Mechanosensitive tyrosine phosphorylation of paxillin and focal adhesion kinase in tracheal smooth muscle

1999 ◽  
Vol 276 (1) ◽  
pp. C250-C258 ◽  
Author(s):  
Dachun Tang ◽  
Dolly Mehta ◽  
Susan J. Gunst
Keyword(s):  
Smooth Muscle ◽  
Focal Adhesion Kinase ◽  
Tyrosine Phosphorylation ◽  
Focal Adhesion ◽  
Cell Structure ◽  
Muscle Length ◽  
Tracheal Smooth Muscle ◽  
Protein Activation ◽  
Associated Proteins

We investigated the role of the integrin-associated proteins focal adhesion kinase (FAK) and paxillin as mediators of mechanosensitive signal transduction in tracheal smooth muscle. In muscle strips contracted isometrically with ACh, we observed higher levels of tyrosine phosphorylation of FAK and paxillin at the optimal muscle length ( L o) than at shorter muscle lengths of 0.5 or 0.75 L o. Paxillin phosphorylation was also length sensitive in muscles activated by K+ depolarization and adjusted rapidly to changes in muscle length imposed after contractile activation by either ACh or K+depolarization. Ca2+ depletion did not affect the length sensitivity of paxillin and FAK phosphorylation in muscles activated with ACh, indicating that the mechanotransduction process can be mediated by a Ca2+-independent pathway. Since Ca2+-depleted muscles do not generate significant active tension, this suggests that the mechanotransduction mechanism is sensitive to muscle length rather than tension. We conclude that FAK and paxillin participate in an integrin-mediated mechanotransduction process in tracheal smooth muscle. We propose that this pathway may initiate alterations in smooth muscle cell structure and contractility via the remodeling of actin filaments and/or via the mechanosensitive regulation of signaling molecules involved in contractile protein activation.

scholarly journals Two distinct bombesin receptor subtypes are expressed and functional in human lung carcinoma cells.

1991 ◽  
Vol 266 (28) ◽  
pp. 18771-18779
Author(s):  
M.H. Corjay ◽  
D.J. Dobrzanski ◽  
J.M. Way ◽  
J. Viallet ◽  
H. Shapira ◽  
...  
Keyword(s):  
Lung Carcinoma ◽  
Human Lung ◽  
Carcinoma Cells ◽  
Receptor Subtypes ◽  
Lung Carcinoma Cells ◽  
Human Lung Carcinoma ◽  
Bombesin Receptor
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