Disease relevance of PODXL2

• The aim of our study was to investigate the fibrinolytic system in a group of healthy controls and vascular disease patients, before and after endoglycan administration "per os". All the patients had a reduced basal fibrinolytic activity [1].

High impact information on PODXL2

• Low force decelerates L-selectin dissociation from P-selectin glycoprotein ligand-1 and endoglycan [2].
• These catch-slip transitional bonds were also observed for L-selectin interacting with endoglycan, a newly identified PSGL-1-like ligand [2].
• Endoglycan, a member of the CD34 family, functions as an L-selectin ligand through modification with tyrosine sulfation and sialyl Lewis x [3].
• Since the distribution of endoglycan includes hematopoietic precursors and leukocyte subpopulations, in addition to endothelial cells, our findings suggest several potential settings for endoglycan-mediated adhesion events [3].
• However, endoglycan employs a different binding mechanism, interacting with L-selectin through sulfation on two tyrosine residues and O-linked sLex structures that are presented within its highly acidic amino-terminal region [3].

Biological context of PODXL2

• Thus, CD34, podocalyxin, and endoglycan comprise a family of sialomucins sharing both structural similarity and sequence homology, which are expressed by both endothelium and multipotent hematopoietic progenitors [4].

Anatomical context of PODXL2

• Endoglycan mRNA and protein were detected in both endothelial cells and CD34(+) bone marrow cells [4].
• With the subsequent identification of podocalyxin and endoglycan as related family members also expressed on early progenitor cells, attention is slowly shifting toward understanding how these molecules might contribute to progenitor function and behavior [5].
• Endoglycan, a heparan-dermatan sulphate association, is a highly purified heparinoid extracted from porcine intestinal mucosa [1].

Associations of PODXL2 with chemical compounds

• In addition, endoglycan contains several potential glycosaminoglycan attachment sites and is modified with chondroitin sulfate [4].
• Podocalyxin-like protein (PCLP) is a sialomucin-type membrane protein structurally related to CD34 and endoglycan [6].

References