Mouse endocan

 

 


ESM1 Gene data base        ESM1 Protein data base


 

Communities with human endocan

Mouse endocan gene has been cloned first in Lille, revealing a unique gene spanning 12 kb and organized in 3 exons, similarly to the human esm1 gene. It encodes for a mature polypeptide of 165 aminoacids with 72% homology and well conserved structural domains (Depontieu et al).

Mouse endocan circulates at a concentration around 1 ng/mL quite similar to its human counterpart (Depontieu et al).

Mouse endocan was found expressed in endothelial tip cells from several retinal angiogenesis models (Strasser et al, del Toro et al), and in tumor endothelial cells from various syngenic and xenogenic tumors (Abid et al).

But with some own characterics

A first particularity was found by Abid et al in the way that contrary to its human counterpart, mouse endocan is spontaneously produced by non-endothelial cells in lung, kidney and spleen.

Yassine et al reported that mouse endocan is much less glycanated than its human counterpart. Both glycanated and non glycanated forms are found in sera from various mouse strains. Interestingly, the non glycanated endocan exhibits antitumoral activity by facilitating the leukocyte recruitment into the tumors, suggesting a proinflammatory role for non glycanated endocan.

By using endocan knockout (KO) mice, Rocha et al confirmed that endocan is required for optimal endothelial response to VEGF (less filopodia, and less cerebral edema in KO mice). Interestingly, endocan KO mice showed decreased leukocyte extravasation after intraperitoneal injection of IL-1, suggesting a proinflammatory role of mouse endocan.

Both Rocha’s and Yassine's observations may support the idea that the main physiological form of mouse endocan could be non glycanated, provided by non-endothelial cells, which is quite different from its human counterpart which is endothelial-derived, fully glycanated.

Conclusion

Each form has opposite effect: protumoral and anti-inflammatory for the glycanic form, antitumoral and proinflammatory for the non glycanated endocan polypeptide.Thus, the presence or absence of endocan's glycan appears to guide its function.