The effect of elevated extracellular glucose on adherens junction proteins in cultured rat heart endothelial cells

Life Sciences ◽  
2004 ◽  
Vol 74 (17) ◽  
pp. 2085-2096 ◽  
Author(s):  
Hong-Zin Lee ◽  
Feng-Tsgh Yeh ◽  
Chun-Hsiung Wu
Keyword(s):  
Endothelial Cells ◽  
Rat Heart ◽  
Adherens Junction ◽  
Extracellular Glucose ◽  
Adherens Junction Proteins ◽  
Junction Proteins

scholarly journals Histamine stimulates phosphorylation of adherens junction proteins and alters their link to vimentin

2002 ◽  
Vol 282 (6) ◽  
pp. L1330-L1338 ◽  
Author(s):  
D. Michael Shasby ◽  
Dana R. Ries ◽  
Sandra S. Shasby ◽  
Michael C. Winter
Keyword(s):  
Endothelial Cells ◽  
Umbilical Vein ◽  
Adherens Junction ◽  
Vascular Endothelial ◽  
Cortical Actin ◽  
Human Umbilical Vein ◽  
Umbilical Vein Endothelial Cells ◽  
Adherens Junction Proteins ◽  
Junction Proteins

Histamine increases microvascular permeability by creating small transitory (100–400 nm) gaps between adjacent endothelial cells at sites of vascular endothelial (VE)-cadherin-based adhesion. We examined the effects of histamine on the proteins within the VE-cadherin-based adherens junction in primary human umbilical vein endothelial cells. VE-cadherin is linked not only by β- and α-catenin to cortical actin but also by γ-catenin to the intermediate filament vimentin. In mature human umbilical vein cultures, the VE-cadherin immunoprecipitate contained equivalent amounts of α- and β-catenin, 130% as much β- as γ-catenin, and 50% as much actin as vimentin. Within 60 s, histamine decreased the fraction of VE-cadherin in the insoluble portion of the cell lysate by 35 ± 1.5%. At the same time, histamine decreased the amount of vimentin that immunoprecipitated with VE-cadherin by 50 ± 6%. Histamine did not affect the amount of actin or the amount of α-, β-, or γ-catenin that immunoprecipitated with VE-cadherin. Within 60 s, histamine simulated a doubling in the phosphorylation of VE-cadherin and β- and γ-catenin. The VE-cadherin immunoprecipitate contained kinase activity that phosphorylated VE-cadherin and γ-catenin in vitro.

scholarly journals Activated Neutrophils Induce Hyperpermeability and Phosphorylation of Adherens Junction Proteins in Coronary Venular Endothelial Cells

1999 ◽  
Vol 274 (35) ◽  
pp. 24930-24934 ◽  
Author(s):  
John H. Tinsley ◽  
Mac H. Wu ◽  
Weiya Ma ◽  
Amy C. Taulman ◽  
Sarah Y. Yuan
Keyword(s):  
Endothelial Cells ◽  
Adherens Junction ◽  
Activated Neutrophils ◽  
Adherens Junction Proteins ◽  
Junction Proteins

scholarly journals Drosophila p120catenin plays a supporting role in cell adhesion but is not an essential adherens junction component

2003 ◽  
Vol 160 (3) ◽  
pp. 433-449 ◽  
Author(s):  
Steven H. Myster ◽  
Robert Cavallo ◽  
Charles T. Anderson ◽  
Donald T. Fox ◽  
Mark Peifer
Keyword(s):  
Cell Adhesion ◽  
Adherens Junctions ◽  
Adherens Junction ◽  
Null Alleles ◽  
Juxtamembrane Region ◽  
Genes Encoding ◽  
Positive Modulator ◽  
Adherens Junction Proteins ◽  
Junction Structure ◽  
Junction Proteins

Cadherin–catenin complexes, localized to adherens junctions, are essential for cell–cell adhesion. One means of regulating adhesion is through the juxtamembrane domain of the cadherin cytoplasmic tail. This region is the binding site for p120, leading to the hypothesis that p120 is a key regulator of cell adhesion. p120 has also been suggested to regulate the GTPase Rho and to regulate transcription via its binding partner Kaiso. To test these hypothesized functions, we turned to Drosophila, which has only a single p120 family member. It localizes to adherens junctions and binds the juxtamembrane region of DE-cadherin (DE-cad). We generated null alleles of p120 and found that mutants are viable and fertile and have no substantial changes in junction structure or function. However, p120 mutations strongly enhance mutations in the genes encoding DE-cadherin or Armadillo, the β-catenin homologue. Finally, we examined the localization of p120 during embryogenesis. p120 localizes to adherens junctions, but its localization there is less universal than that of core adherens junction proteins. Together, these data suggest that p120 is an important positive modulator of adhesion but that it is not an essential core component of adherens junctions.

Ectopic expression of gastrokine 1 in gastric cancer cells up-regulates tight and adherens junction proteins network

2015 ◽  
Vol 211 (8) ◽  
pp. 577-583 ◽  
Author(s):  
Emilia Rippa ◽  
Filomena Altieri ◽  
Chiara Stella Di Stadio ◽  
Giuseppina Miselli ◽  
Annalisa Lamberti ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Cancer Cells ◽  
Ectopic Expression ◽  
Adherens Junction ◽  
Gastric Cancer Cells ◽  
Gastrokine 1 ◽  
Adherens Junction Proteins ◽  
Junction Proteins

Altered expression and interaction of adherens junction proteins in the developing OLM of the Rho(−/−) mouse

2007 ◽  
Vol 85 (5) ◽  
pp. 714-720 ◽  
Author(s):  
Matthew Campbell ◽  
Marian Humphries ◽  
Paul Kenna ◽  
Peter Humphries ◽  
Brenda Brankin
Keyword(s):  
Adherens Junction ◽  
Altered Expression ◽  
Adherens Junction Proteins ◽  
Junction Proteins

scholarly journals Regulation of Adherens Junction Dynamics by Phosphorylation Switches

2012 ◽  
Vol 2012 ◽  
pp. 1-14 ◽  
Author(s):  
Cristina Bertocchi ◽  
Megha Vaman Rao ◽  
Ronen Zaidel-Bar
Keyword(s):  
Actin Cytoskeleton ◽  
Enzymatic Activity ◽  
Adherens Junctions ◽  
Adherens Junction ◽  
Adaptor Proteins ◽  
Cell Junction ◽  
Internal Forces ◽  
Adherens Junction Proteins ◽  
Junction Proteins

Adherens junctions connect the actin cytoskeleton of neighboring cells through transmembrane cadherin receptors and a network of adaptor proteins. The interactions between these adaptors and cadherin as well as the activity of actin regulators localized to adherens junctions are tightly controlled to facilitate cell junction assembly or disassembly in response to changes in external or internal forces and/or signaling. Phosphorylation of tyrosine, serine, or threonine residues acts as a switch on the majority of adherens junction proteins, turning “on” or “off” their interactions with other proteins and/or their enzymatic activity. Here, we provide an overview of the kinases and phosphatases regulating phosphorylation of adherens junction proteins and bring examples of phosphorylation events leading to the assembly or disassembly of adherens junctions, highlighting the important role of phosphorylation switches in regulating their dynamics.

scholarly journals Enhanced interaction between focal adhesion and adherens junction proteins: Involvement in sphingosine 1-phosphate-induced endothelial barrier enhancement

2009 ◽  
Vol 77 (3) ◽  
pp. 304-313 ◽  
Author(s):  
Xiaoguang Sun ◽  
Yasushi Shikata ◽  
Lichun Wang ◽  
Kazuyoshi Ohmori ◽  
Naoko Watanabe ◽  
...  
Keyword(s):  
Focal Adhesion ◽  
Adherens Junction ◽  
Endothelial Barrier ◽  
Sphingosine 1 Phosphate ◽  
Adherens Junction Proteins ◽  
Junction Proteins
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