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Characterization, isolation and amino terminal sequencing of a rat colon carcinoma-associated antigen

✍ Scribed by Corinne Chadeneau; Marc G. Denis; Hervé M. Blottière; Marc Grégoire; Jean-Yves Douillard; Khaled Meflah

Publisher
John Wiley and Sons
Year
1991
Tongue
French
Weight
798 KB
Volume
47
Category
Article
ISSN
0020-7136

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✦ Synopsis

Monoclonal antibodies have been raised against a cell line derived from a dimethylhydrazine-induced rat colon carcinoma. One of these antibodies (MAb E4) has previously been shown to react slightly with normal small intestine and colon, and not with other normal tissues as determined by immunohistochemistry. Using Western immunoblotting we confirmed this tumor specificity. Therefore, the M, of approx. 66,000 glycosylated antigen (pE4) recognized by MAb E4 appeared to be a potential marker of colon carcinoma. Fifteen human tumor cell lines were tested by flow cytometry for the expression of pE4. This antigen was not detected on these cells. In the rat colon carcinoma cell, pE4 was exclusively found on the cell membrane. pE4 was purified to near homogeneity by immunoaffinity chromatography. The first 20 Nterminal amino acids were identified. Comparison with the NBRF data bank did not reveal a complete homology with known sequenced proteins but similarities were found with the mouse L3T4 precursor, the env polyprotein of human immunodeficiency virus type I, flagellin from Haiobacterium halobium and the gp30 from hepatitis B surface antigen. Homology was always found in transmembranous or hydrophobic domains of these proteins. By indirect immunofluorescence analysis of adherent cells and size exclusion chromatography under native conditions, pE4 was found to interact with other molecules and perhaps to be involved in intercellular contact.

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