Open AccessThe tight junctions protein Claudin-5 limits endothelial cell motility
Author(s) -
Zhen-Guo Yang,
Shuilong Wu,
Federica Fontana,
Yanyu Li,
Wei Xiao,
Zhangdai Gao,
Alice Krudewig,
Markus Affolter,
HeinzGeorg Belting,
Salim AbdelilahSeyfried,
Jingjing Zhang
Publication year - 2020
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.248237
Subject(s) - claudin , biology , microbiology and biotechnology , dorsal aorta , vasculogenesis , tight junction , endothelial stem cell , zebrafish , motility , paracellular transport , anatomy , in vitro , stem cell , permeability (electromagnetism) , biochemistry , progenitor cell , haematopoiesis , gene , membrane
Steinberg's differential adhesion hypothesis suggests that adhesive mechanisms are important for sorting of cells and tissues during morphogenesis (Steinberg, 2007). During zebrafish vasculogenesis, endothelial cells sort into arterial and venous vessel beds but it is unknown whether this involves adhesive mechanisms. Claudins are tight junction proteins regulating the permeability of epithelial and endothelial tissue barriers. Previously, the roles of Claudins during organ development have exclusively been related to their canonical functions in determining paracellular permeability. Here, we use atomic force microscopy to quantify Claudin-5-dependent adhesion and find that this strongly contributes to the adhesive forces between arterial endothelial cells. Based on genetic manipulations, we reveal a non-canonical role of Claudin-5a during zebrafish vasculogenesis, which involves the regulation of adhesive forces between adjacent dorsal aortic endothelial cells. In vitro and in vivo studies demonstrate that loss of Claudin-5 results in increased motility of dorsal aorta endothelial cells and in a failure of the dorsal aorta to lumenize. Our findings uncover a novel role of Claudin-5 in limiting arterial endothelial cell motility, which goes beyond its traditional sealing function during embryonic development.