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Anti-hESC mAb Hesca-2 Binds to a Glycan Epitope Commonly Found on Carcinomas

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MG Shoreibah1, CL Jackson1, PW Price1, R Meagher2, AK Godwin3, Q Cai3, JC Gildersleeve4
1Abeome Corporation, Athens, GA 30605
2University of Georgia Dept. of Genetics, Athens, GA 30602
3Fox Chase Cancer Center, Philadelphia, PA 19111-2497
4National Cancer Institute, Frederick, MD 21702-1201


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Abstract

Hesca-2, a monoclonal antibody (mAb) IgM raised to the human embryonic stem cell (hESC) line BG-01v, binds with high affinity (nM) to the disaccharide epitope [Gal1- 3GlcNAc] on a glycan microarray. This glycan epitope, found on glycoproteins, glycolipids and free oligosaccharides in milk, is recognized by a number of human galectins particularly galectin-7. It was expressed on pluripotent progenitor hESC cells in culture, but not in various differentiated cells derived from hESC-based on immunofluorescence microscopy (IFM). Interestingly, this glycan epitope is also associated with carcinomas including pancreatic, stomach, colorectal and ovarian. Hesca-2 cross-reacts in IFM studies with several human ovarian cancer cell lines and is cytotoxic to them based on the release of cytosolic enzyme lactatedehydrogenase (LDH) into the media. Hesca-2 also has an negligible cytotoxic activity at low concentrations on hESCs in culture and a more dramatic and different effect on the cells at higher concentrations that may be due to cytoprotection or proliferation. The mechanism of this activity clearly requires multimeric binding in that Fab fragments do not show a comparable response. Future studies should explore the precise mechanism(s) involved in these observed disparate activities; in particular, assessing what affect the soluble glycan ligands (recognized by Hesca-2) have on the proliferation, adhesion, etc. of hESCs. There is an intriguing possibility that the glycan ligands recognized by Hesca-2 and galectin-7 (or another galectin) could be involved in processes critical for both stem cell and cancer cell survival or proliferation.

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