We describe a human integral cell surface glycoprotein (Mr 142 kD), recognized by monoclonal antibody M2B3. This glycoprotein is absent from resting peripheral blood lymphocytes, but becomes expressed in significant levels with mitogen activation. The M2B3 glycoprotein is present on epithelial cells in the basal layer of epidermal and esophageal tissue as well as in several fresh tumors examined. In addition, it is present on smooth muscle tissue throughout the gastrointestinal tract, but is absent from smooth muscle from several other tissue sources, skeletal muscle and cardiac muscle. The M2B3 glycoprotein is similar, but not identical, in apparent Mr to a transformation-associated glycoprotein, Q14. Further, the M2B3 and Q14 species are related antigenically. Nonetheless, M2B3 and Q14 are distinct glycoproteins based on clear differences in cell distribution and in partial peptide mapping. The M2B3 antigen described herein is sulfated on tyrosine, and represents one of the few cell surface proteins described to date that is sulfated on tyrosine residues. Our studies suggest the function of the M2B3 glycoprotein is likely to be associated with cell proliferation of cell adhesion.
|Original language||English (US)|
|Number of pages||11|
|State||Published - Jan 1992|
All Science Journal Classification (ASJC) codes
- Molecular Biology