This gene encodes a classical cadherin of the cadherin superfamily. The encoded preproprotein is proteolytically processed to generate the mature glycoprotein. This calcium-dependent cell-cell adhesion molecule is comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Functioning as a classical cadherin by imparting to cells the ability to adhere in a homophilic manner, this protein plays a role in endothelial adherens junction assembly and maintenance. This gene is located in a gene cluster in a region on the long arm of chromosome 16 that is involved in loss of heterozygosity events in breast and prostate cancer. [provided by RefSeq, Nov 2015]
Forensic Context
A study in mice demonstrated that the CDH5 is a general marker for endothelial cells, being highly expressed in all endothelial cell clusters within brown adipose tissue, including capillary, arterial, and venous subtypes [Behrens et al. DOI:10.1016/j.molmet.2025.102252]. A review of single-cell sequencing in murine and human myocardial infarction models further established that the CDH5 is a highly expressed marker for endothelial cells across all identified cardiac endothelial cell clusters [Bian et al. DOI:10.3892/mmr.2025.13680]. A study in mice demonstrated that seawater drowning-induced acute lung injury downregulates VE-cadherin, a key endothelial adherens junction protein, contributing to pulmonary vascular hyperpermeability, and this reduction was restored by CDC42 overexpression, which alleviated injury and reduced permeability [Chen et al. DOI:10.1016/j.lfs.2025.124109]. In human sepsis, lipopolysaccharide-induced endothelial barrier disruption suppresses VE-cadherin expression in vitro, and knockdown of the upregulated circRNA hsa_circ_0074158 significantly enhanced VE-cadherin expression, partially reversing the increased endothelial permeability [Liao et al. DOI:10.3389/fgene.2022.1002344].