CDH5

CDH5, or vascular endothelial calreticulin, alias VE-cadherin/Cadherin-5, is a member of the type II classical calreticulin family encoded by the CDH5 gene and is expressed predominantly in vascular endothelial cells.The mechanism of action of CDH5 involves the mediation of homogeneous adhesion between endothelial cells through its extracellular structural domains and interaction with CDH5 molecules of neighbouring cells to form stable adhesive junctions. interacting with CDH5 molecules in neighbouring cells through its extracellular structural domains to form stable adhesion junctions. This adhesion is essential for maintaining vascular integrity and regulating vascular permeability. In addition, CDH5 binds to α-linker proteins to form connections to the cytoskeleton, which are involved in the regulation of endothelial cell polarity and vascular lumen formation.

The function of CDH5 also involves interactions with proteins, such as KRIT1 and PAR-1, which work together to maintain the stability and function of the endothelium.The biological significance of CDH5 is mainly reflected in its role in regulating the biology of vascular endothelial cells. It is involved in a variety of physiological processes, including neovascularisation, vascular stabilisation and inflammatory responses. During tumourigenesis and development, the abnormal expression level and function of CDH5 are closely related to tumour angiogenesis, tumour cell invasion and metastasis. In addition, CDH5 is involved in endothelial cell barrier function and cell signalling, affecting cell proliferation, migration and differentiation. Therefore, CDH5 is an important target in the study and treatment of vascular-related diseases, for example, it has potential applications in anti-angiogenic therapy and tumour therapy.