title: Extracellular matrix, junctional integrity and matrix metalloproteinase interactions in endothelial permeability regulation.
abstract: Vascular endothelial permeability is maintained by the regulated apposition of adherens and tight junctional proteins whose organization is controlled by several pharmacological and physiological mediators. Endothelial permeability changes are associated with: (1) the spatial redistribution of surface cadherins and occludin, (2) stabilization of focal adhesive bonds and (3) the progressive activation of matrix metalloproteinases (MMPs). In response to peroxide, histamine and EDTA, endothelial cells sequester VE-cadherin and alter its cytoskeletal binding. Simultaneously, these mediators enhance focal adhesion to the substratum. Oxidants, cytokines and pharmacological mediators also trigger the activation of matrix metalloproteinases (MMPs) in a cytoskeleton and tyrosine phosphorylation dependent manner to degrade occludin, a well-characterized tight junction element. These related in vitro phenomena appear to co-operate during inflammation, to increase endothelial permeability, structurally stabilize cells while also remodelling cell junctions and substratum.
authors.affiliation: Molecular and Cellular Physiology, LSU Health Sciences Center Shreveport, LA 71130, USA. jalexa@lsumc.edu
authors.forename: J S
authors.initials: JS
authors.lastname: Alexander
authors.forename: John W
authors.initials: JW
authors.lastname: Elrod
mesh_terms: D000818:Animals; D002199:Capillary Permeability / Q000502:physiology; D004730:Endothelium, Vascular / Q000378:metabolism*; D005109:Extracellular Matrix / Q000378:metabolism*; D006801:Humans; D007365:Intercellular Junctions / Q000502:physiology*; D020782:Matrix Metalloproteinases / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism
chemical_list: D008565:Membrane Proteins; D020782:Matrix Metalloproteinases