Biochemical analysis of a human epithelial surface antigen: Differential cell expression and processing☆
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EpCAM: Structure and function in health and disease
2013, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :A number of proteases, including serine proteases trypsin and chymotrypsin, have been shown to be able to conduct this N-terminal cleavage of EpCAM [48], which occurs in a variety of epithelial cancer cell lines originating e.g. from colon, ovarian, and breast cancer [26]. Whether or not and to which extent N-terminal cleavage occurs depends on the presence and activity of the relevant proteases [26]. Although EpCAM's limited N-terminal proteolytic cleavage was discovered more than three decades ago and suggested to be of functional importance [48], the effects of this post-translational modification on EpCAM's structure and function are still unknown.
Detection of circulating tumor-associated antigen depends on the domains recognized by the monoclonal antibodies used: N-terminal trimmed EpCAM-levels are much higher than untrimmed forms
2012, Immunology LettersCitation Excerpt :Moreover, a splice variant called EpCAM-006 encodes a soluble form of the protein without its transmembrane region. Soluble forms of EpCAM can be detected in human plasma [12–16], which are a mix of shed extracellular EpCAM and the soluble protein encoded by the splice variant. However, relatively little is known about the significance of EpCAM levels in the blood [16–18].
Epithelial cell adhesion molecule: More than a carcinoma marker and adhesion molecule
2007, American Journal of PathologyPreparation of recombinant MK-1/Ep-CAM and establishment of an ELISA system for determining soluble MK-1/Ep-CAM levels in sera of cancer patients
2002, Journal of Immunological MethodsDetermination of Disulfide Bond Assignments and N-Glycosylation Sites of the Human Gastrointestinal Carcinoma Antigen GA733-2 (CO17-1A, EGP, KS1-4, KSA, and Ep-CAM)
2001, Journal of Biological ChemistryCitation Excerpt :The degree of posttranslational modification at Asn51 may be functionally and clinically important because it is close to the CO17-1A mAb epitope (10) and to the proteolysis sensitivity site. Interestingly, different ratios of cleaved/noncleaved species of GA733-2 antigen were observed from different epithelial cell lines (33). Although proteolytic regulation of the function of GA733-2 antigen has not been directly demonstrated, the possible correlation between proteolytic cleavage, glycosylation, and adhesion characteristics of the protein is an intriguing question for future studies.
Initial immunochemical characterization of MX35 ovarian cancer antigen
1997, Gynecologic Oncology
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This work was supported by a grant from the National Cancer Institute (CA 08478), the Paul Garrett Fund, and the Avon Program in Ovarian Cancer.