Histamine stimulates phosphorylation of adherens junction proteins and alters their link to vimentin
Autor: | Sandra S. Shasby, Dana R. Ries, D. Michael Shasby, Michael C. Winter |
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Rok vydání: | 2002 |
Předmět: |
Pulmonary and Respiratory Medicine
Beta-catenin Endothelium Physiology Vascular permeability Vimentin Adherens junction chemistry.chemical_compound Antigens CD Physiology (medical) medicine Humans Phosphorylation Cells Cultured Cytoskeleton beta Catenin biology Cadherin Membrane Proteins Adherens Junctions Cell Biology Cadherins Precipitin Tests Actins Cell biology Endothelial stem cell Cytoskeletal Proteins medicine.anatomical_structure Desmoplakins chemistry Biochemistry Trans-Activators biology.protein Endothelium Vascular gamma Catenin alpha Catenin Histamine |
Zdroj: | American Journal of Physiology-Lung Cellular and Molecular Physiology. 282:L1330-L1338 |
ISSN: | 1522-1504 1040-0605 |
DOI: | 10.1152/ajplung.00329.2001 |
Popis: | 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 beta- and alpha-catenin to cortical actin but also by gamma-catenin to the intermediate filament vimentin. In mature human umbilical vein cultures, the VE-cadherin immunoprecipitate contained equivalent amounts of alpha- and beta-catenin, 130% as much beta- as gamma-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 alpha-, beta-, or gamma-catenin that immunoprecipitated with VE-cadherin. Within 60 s, histamine simulated a doubling in the phosphorylation of VE-cadherin and beta- and gamma-catenin. The VE-cadherin immunoprecipitate contained kinase activity that phosphorylated VE-cadherin and gamma-catenin in vitro. |
Databáze: | OpenAIRE |
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