PubMed:9145315 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/9145315","sourcedb":"PubMed","sourceid":"9145315","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/9145315","text":"Characterization of the ETSA-21 antigen, a glycosylphosphatidyl-inositol anchor glycoprotein identified in breast cancer cells using monoclonal antibody B21.\nMab B21 is a monoclonal antibody (Mab) that recognizes an epithelial tumor surface antigen (ETSA-B21) from diverse human tumor cell lines including breast, ovary, uterus, and their cognate carcinoma tissues. A lower reactivity has been observed in normal breast tissue and benign hyperplesia. In this study, the characteristics of the ETSA-B21 antigen have been examined in greater detail in the MCF-7, SK-BR-3, and MDA-MB-453 breast cancer cell lines. Treatment with phosphatidylinositol-phospholipase C, but no neuraminidase were found to partially remove the ETSA-B21 signal from the cell surface as revealed by immunofluorescence microscopy. Inhibition of the N-glycosylation pathway by tunicamycin resulted in a decreased ETSA-B21 signal on the cell membrane. In addition, the antigen-antibody complex was internalized in breast cancer cells as demonstrated by an acidic was internalization assay evaluated using immunofluorescence. In conclusion, this study suggests that ETSA-B21 is a GPI anchor N-glycosylated protein promoting specific antibody internalization in breast cancer cells.","tracks":[{"project":"bionlp-st-epi-2011-training","denotations":[{"id":"T1","span":{"begin":626,"end":662},"obj":"Protein"}],"attributes":[{"subj":"T1","pred":"source","obj":"bionlp-st-epi-2011-training"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"bionlp-st-epi-2011-training","color":"#ec9399","default":true}]}]}}