Title : Characterization of posttranslational modifications of human
A33 antigen, a novel palmitoylated surface
glycoprotein of human gastrointestinal epithelium
Abstract :
- Monoclonal antibody ( mAb) A33 recognizes a differentiation antigen ( A33 ) expressed in normal human gastrointestinal epithelium and in 95% of human colon cancers
- Murine mAb A33 shows specific targeting of colon cancer in humans and a humanized A33 antibody is currently being evaluated in the clinic
- The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily
- Because mAb A33 recognizes a conformational epitope , only a partial characterization of the A33 antigen has been carried out to date
- In this report we show that the A33 antigen is (I) N-glycosylated, containing approximately 8 K of N-linked carbohydrate and there is no evidence for O-glycosylation, sialylation or glycophosphatidylinositol, and (ii) S-acylated in vitro, incorporating [3H] palmitic acid linked through a hydroxylamine-sensitive thioester bond
- The S-palmitoylation may be involved in regulating the internalization process initiated by binding of mAb A33 to cell surface A33 antigen
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