E-cadherin mediates adherens junction organization through protein kinase C

1994 ◽  
Vol 107 (12) ◽  
pp. 3615-3621 ◽  
Author(s):  
J.E. Lewis ◽  
P.J. Jensen ◽  
K.R. Johnson ◽  
M.J. Wheelock
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Adherens Junctions ◽  
Adherens Junction ◽  
Human Keratinocytes ◽  
Kinase C ◽  
E Cadherin

Cultured human keratinocytes maintained in 30 microM Ca2+ do not form adherens junctions; however, when the extracellular Ca2+ concentration is raised to 1 mM, adherens junctions form very rapidly. The formation of a junction involves the coordinate organization of intracellular and extracellular components. Cadherins have been shown to mediate this coordinate organization. In this report we show that E-cadherin organizes the various junctional components by signalling through protein kinase C.

Abstract 4216: Protein kinase C ≤ overexpression is associated with loss of membrane-associated E-cadherin and β-catenin in T47D xenograft breast tumors

2012 ◽  
Author(s):  
Bethany E. Perez White ◽  
Huiping Zhao ◽  
Madhuchhanda Kundu ◽  
Mary Ellen Molloy ◽  
Debra A. Tonetti
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Breast Tumors ◽  
Kinase C ◽  
E Cadherin

Patented natural avocado sugars modulate the HBD-2 expression in human keratinocytes through the involvement of protein kinase C and protein tyrosine kinases

2009 ◽  
Vol 302 (3) ◽  
pp. 201-209 ◽  
Author(s):  
Iole Paoletti ◽  
Elisabetta Buommino ◽  
Laura Tudisco ◽  
Caroline Baudouin ◽  
Philippe Msika ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tyrosine Kinases ◽  
Human Keratinocytes ◽  
Protein Tyrosine Kinases ◽  
Protein Tyrosine ◽  
Kinase C

scholarly journals Involvement of integrin-induced activation of protein kinase C in the formation of adherens junctions

2007 ◽  
Vol 12 (5) ◽  
pp. 651-662 ◽  
Author(s):  
Misa Ozaki ◽  
Hisakazu Ogita ◽  
Yoshimi Takai
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Adherens Junctions ◽  
Kinase C

Protein kinase C regulates endocytosis and recycling of E-cadherin

2002 ◽  
Vol 283 (2) ◽  
pp. C489-C499 ◽  
Author(s):  
Tam Luan Le ◽  
Shannon R. Joseph ◽  
Alpha S. Yap ◽  
Jennifer L. Stow
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Esters ◽  
Recycling Endosomes ◽  
Kinase C ◽  
Pkc Isozymes ◽  
Pkc Activation ◽  
Darby Canine Kidney ◽  
E Cadherin

E-cadherin is a major component of adherens junctions in epithelial cells. We showed previously that a pool of cell surface E-cadherin is constitutively internalized and recycled back to the surface. In the present study, we investigated the potential role of protein kinase C (PKC) in regulating the trafficking of surface E-cadherin in Madin-Darby canine kidney cells. Using surface biotinylation and immunofluorescence, we found that treatment of cells with phorbol esters increased the rate of endocytosis of E-cadherin, resulting in accumulation of E-cadherin in apically localized early or recycling endosomes. The recycling of E-cadherin back to the surface was also decreased in the presence of phorbol esters. Phorbol ester-induced endocytosis of E-cadherin was blocked by specific inhibitors, implicating novel PKC isozymes, such as PKC-ε in this pathway. PKC activation led to changes in the actin cytoskeleton facilitating E-cadherin endocytosis. Depolymerization of actin increased endocytosis of E-cadherin, whereas the PKC-induced uptake of E-cadherin was blocked by the actin stabilizer jasplakinolide. Our findings show that PKC regulates vital steps of E-cadherin trafficking, its endocytosis, and its recycling.

scholarly journals Absence of Down-Regulation and Translocation of The η Isoform of Protein Kinase C in Normal Human Keratinocytes

1996 ◽  
Vol 106 (4) ◽  
pp. 790-794 ◽  
Author(s):  
Akiko Murakami ◽  
Kazuhiro Chida ◽  
Yasutoshi Suzuki ◽  
Hidehiko Kikuchi ◽  
Shinobu Imajoh-Ohmi ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Human Keratinocytes ◽  
Down Regulation ◽  
Kinase C ◽  
Normal Human Keratinocytes ◽  
Normal Human

scholarly journals Dephosphorylation of the catenins p120 and p100 in endothelial cells in response to inflammatory stimuli

1999 ◽  
Vol 338 (2) ◽  
pp. 471-478 ◽  
Author(s):  
Marianne J. RATCLIFFE ◽  
Caroline SMALES ◽  
James M. STADDON
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Tight Junction ◽  
Adherens Junction ◽  
Receptor Activation ◽  
Protein Kinase C Inhibitors ◽  
Kinase C ◽  
Inflammatory Stimuli ◽  
Tight Junction Permeability

Inflammatory mediators such as histamine and thrombin increase the tight-junction permeability of endothelial cells. Tight-junction permeability may be independently controlled, but is dependent on the adherens junction, where adhesion is achieved through homotypic interaction of cadherins, which in turn are associated with cytoplasmic proteins, the catenins. p120, also termed p120cas/p120ctn, and its splice variant, p100, are catenins. p120, originally discovered as a substrate of the tyrosine kinase Src, is also a target for a protein kinase C-stimulated pathway in epithelial cells, causing its serine/threonine dephosphorylation. The present study shows that pharmacological activation of protein kinase C stimulated a similar pathway in endothelial cells. Activation of receptors for agents such as histamine (H1), thrombin and lysophosphatidic acid in the endothelial cells also caused serine/threonine dephosphorylation of p120 and p100, suggesting physiological relevance. However, protein kinase C inhibitors, although blocking the effect of pharmacological activation of protein kinase C, did not block the effects due to receptor activation. Calcium mobilization and the myosin-light-chain-kinase pathway do not participate in p120/p100 signalling. In conclusion, endothelial cells possess protein kinase C-dependent and -independent pathways regulating p120/p100 serine/threonine phosphorylation. These data describe a new connection between inflammatory agents, receptor-stimulated signalling and pathways potentially influencing intercellular adhesion in endothelial cells.

189 Existence of kinase domains (M kinases) of protein kinase C isozymes in human keratinocytes

1996 ◽  
Vol 12 (2) ◽  
pp. 213
Author(s):  
C. Esaki ◽  
M. Seishima ◽  
K. Osada ◽  
Y. Kitajima
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Human Keratinocytes ◽  
Kinase C

scholarly journals Phorbol ester binding and protein kinase C activity in normal and transformed human keratinocytes

1987 ◽  
Vol 172 (1) ◽  
pp. 146-157 ◽  
Author(s):  
G.T. Snoek ◽  
J. Boonstra ◽  
M. Ponec ◽  
S.W. de Laat
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Human Keratinocytes ◽  
Kinase C ◽  
Protein Kinase C Activity

Protein kinase C δ and η differently regulate the expression of loricrin and Jun family proteins in human keratinocytes

2010 ◽  
Vol 394 (1) ◽  
pp. 106-111 ◽  
Author(s):  
Nagisa Kamioka ◽  
Tomoko Akahane ◽  
Yoko Kohno ◽  
Toshio Kuroki ◽  
Masafumi Iijima ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Human Keratinocytes ◽  
Kinase C
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