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Am J Physiol Lung Cell Mol Physiol 282: L1330-L1338, 2002. First published January 12, 2002; doi:10.1152/ajplung.00329.2001
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Vol. 282, Issue 6, L1330-L1338, June 2002

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

D. Michael Shasby, Dana R. Ries, Sandra S. Shasby, and Michael C. Winter

Department of Internal Medicine, University of Iowa College of Medicine, Iowa City, Iowa 52242

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.

vascular endothelial cadherin; adhesion


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