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In mature human umbilical vein cultures, the VE-cadherin immunoprecipitate contained equivalent amounts of \u03b1- and \u03b2-catenin, 130% as much \u03b2- as \u03b3-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 \u00b1 1.5%. At the same time, histamine decreased the amount of vimentin that immunoprecipitated with VE-cadherin by 50 \u00b1 6%. Histamine did not affect the amount of actin or the amount of \u03b1-, \u03b2-, or \u03b3-catenin that immunoprecipitated with VE-cadherin. Within 60 s, histamine simulated a doubling in the phosphorylation of VE-cadherin and \u03b2- and \u03b3-catenin. The VE-cadherin immunoprecipitate contained kinase activity that phosphorylated VE-cadherin and \u03b3-catenin in vitro.<\/jats:p>","DOI":"10.1152\/ajplung.00329.2001","type":"journal-article","created":{"date-parts":[[2015,3,3]],"date-time":"2015-03-03T20:17:18Z","timestamp":1425413838000},"page":"L1330-L1338","source":"Crossref","is-referenced-by-count":87,"title":["Histamine stimulates phosphorylation of adherens junction proteins and alters their link to vimentin"],"prefix":"10.1152","volume":"282","author":[{"given":"D. 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