Disease relevance of EMCN

• In particular we identified two novel genes not previously reported: endomucin (EMCN) and ubiquitin specific protease 33 (USP33) that appear to be over-expressed in B-ALL relative to their expression in T-ALL [1].
• We further analyzed the expression of endomucin in skin biopsy specimens from patients with inflammatory skin diseases, such as atopic dermatitis, psoriasis, lichen planus, cutaneous lupus erythematosus, and T cell lymphoma as well as with vascular skin tumors, such as hemangioma, pyogenic granuloma, angiolipoma, Kaposi's sarcoma, and angiosarcoma [2].

High impact information on EMCN

• Human endomucin: distribution pattern, expression on high endothelial venules, and decoration with the MECA-79 epitope [3].
• Endomucin is an endothelial sialomucin that was recently identified with the help of monoclonal antibodies raised against mouse endothelial cells [2].
• Expression of endomucin, a novel endothelial sialomucin, in normal and diseased human skin [2].
• We found endomucin expressed on the endothelium of each tissue, concluding that this novel molecule is a new endothelial-specific marker in the study of normal and diseased human skin [2].
• In normal human skin, endomucin was detected for the monoclonal antibody L6H10 by immunoblotting, and immunohistologic analysis of wax-embedded sections revealed that this glycoprotein is expressed on capillaries, venules, and lymphatic vessels [2].

Biological context of EMCN

• Human endomucin is predicted to encode a 261-aa, 27.5-kDa protein with a transmembrane sequence and multiple glycosylation sites [4].

Anatomical context of EMCN

• Our results also indicated that a 90-100 kDa endomucin species is preferentially decorated with L-selectin-reactive sugar chains, whereas an 80 kDa species represents conventional forms expressed in non-HEV-type vascular endothelial cells in lymph nodes [5].

Analytical, diagnostic and therapeutic context of EMCN

• Northern and in situ hybridization studies show that human endomucin expression is largely, if not uniquely, endothelial cell-specific [4].

References