scholarly journals Epidermal Growth Factor Receptor Activation Differentially Regulates Claudin Expression and Enhances Transepithelial Resistance in Madin-Darby Canine Kidney Cells

2003 ◽  
Vol 279 (5) ◽  
pp. 3543-3552 ◽  
Author(s):  
Amar B. Singh ◽  
Raymond C. Harris
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Receptor Activation ◽  
Kidney Cells ◽  
Madin Darby Canine Kidney ◽  
Epidermal Growth ◽  
Darby Canine Kidney ◽  
Canine Kidney

Neutrophil elastase induces mucin production by ligand-dependent epidermal growth factor receptor activation

2002 ◽  
Vol 283 (3) ◽  
pp. L531-L540 ◽  
Author(s):  
Kazuhiro Kohri ◽  
Iris F. Ueki ◽  
Jay A. Nadel
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Neutrophil Elastase ◽  
Growth Factor Receptor ◽  
Receptor Activation ◽  
Cell Culture Supernatant ◽  
Mucin Production ◽  
Egfr Activation ◽  
Epidermal Growth

Neutrophil products are implicated in hypersecretory airway diseases. To determine the mechanisms linking a proteolytic effect of human neutrophil elastase (HNE) and mucin overproduction, we examined the effects of HNE on MUC5AC mucin production in human airway epithelial (NCI-H292) cells. Stimulation with HNE for 5–30 min induced MUC5AC production 24 h later, which was prevented by HNE serine active site inhibitors, implicating a proteolytic effect of HNE. MUC5AC induction was preceded by epidermal growth factor receptor (EGFR) tyrosine phosphorylation and was prevented by selective EGFR tyrosine kinase inhibitors, implicating EGFR activation. HNE-induced MUC5AC production was inhibited by a neutralizing transforming growth factor-α (TGF-α, an EGFR ligand) antibody and by a neutralizing EGFR antibody but not by oxygen free radical scavengers, further implicating TGF-α and ligand-dependent EGFR activation in the response. HNE decreased pro-TGF-α in NCI-H292 cells and increased TGF-α in cell culture supernatant. From these results, we conclude that HNE-induced MUC5AC mucin production occurs via its proteolytic activation of an EGFR signaling cascade involving TGF-α.

mLin-7 is localized to the basolateral surface of renal epithelia via its NH2 terminus

2000 ◽  
Vol 278 (3) ◽  
pp. F464-F475 ◽  
Author(s):  
Samuel W. Straight ◽  
David Karnak ◽  
Jean-Paul Borg ◽  
Emmanuel Kamberov ◽  
Heidi Dare ◽  
...  
Keyword(s):  
Amino Acids ◽  
Growth Factor ◽  
Receptor Tyrosine Kinase ◽  
Growth Factor Receptor ◽  
Kidney Cells ◽  
Madin Darby Canine Kidney ◽  
Renal Epithelia ◽  
Renal Epithelial Cells ◽  
Darby Canine Kidney ◽  
Canine Kidney

In Caenorhabditis elegans, the basolateral localization of the Let-23 growth factor receptor tyrosine kinase requires the expression of three genes: lin-2, lin-7, and lin-10. Mammalian homologs of these three genes have been identified, and a complex of their protein products exists in mammalian neurons. In this paper, we examine the interaction of these mammalian proteins in renal epithelia. Coprecipitation experiments demonstrated that mLin-2/CASK binds to mLin-7, and immunofluorescent labeling showed that these proteins colocalized at the basolateral surface of Madin-Darby canine kidney cells and renal epithelia. Although labeling intensity varied markedly among different renal epithelial cells, those cells strongly expressing mLin-7 also showed intense mLin-2/CASK labeling. We have also demonstrated that mLin-2/CASK binding requires amino acids 12–32 of mLin-7 and have shown that this region of mLin-7 is also necessary for the targeting of mLin-7 to the basolateral surface. Furthermore, the overexpression of mLin-2/CASK mutants in Madin-Darby canine kidney cells caused endogenous mLin-7 to mislocalize. In summary, the NH2 terminus of mLin-7 is crucial for its basolateral localization, likely through its interaction with mLin-2/CASK.

scholarly journals Phosphatidylinositol-4,5-bisphosphate regulates epidermal growth factor receptor activation

2010 ◽  
Vol 461 (3) ◽  
pp. 387-397 ◽  
Author(s):  
Ioannis E. Michailidis ◽  
Radda Rusinova ◽  
Anastasios Georgakopoulos ◽  
Yibang Chen ◽  
Ravi Iyengar ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Receptor Activation ◽  
Epidermal Growth
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