Thrombin-cleaved syndecan-3/-4 ectodomain fragments mediate endothelial barrier dysfunction.

ABSTRACT:

Objective

The endothelial glycocalyx constitutes part of the endothelial barrier but its degradation leaves endothelial cells exposed to transmigrating cells and circulating mediators that can damage the barrier or promote intercellular gaps. Syndecan proteins are key components of the endothelial glycocalyx and are shed during disease states where expression and activity of proteases such as thrombin are elevated. We tested the ability of thrombin to cleave the ectodomains of syndecans and whether the products could act directly on endothelial cells to alter barrier function.

Approach and results

Using transmission electron microscopy, we illustrated the presence of glycocalyx in human lung microvasculature. We confirmed expression of all syndecan subtypes on the endothelia

SUBMITTER: Jannaway M 

PROVIDER: S-EPMC6519803 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature