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Isolation and characterization of a cDNA encoding the KS1/4 epithelial carcinoma marker.

M S Perez and L E Walker
J Immunol May 15, 1989, 142 (10) 3662-3667;
M S Perez
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L E Walker
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Abstract

The mAb KS1/4 recognizes a novel cell surface glycoprotein on a variety of epithelial carcinomas which may be a useful target Ag for antibody-directed diagnostic and therapeutic approaches. Here we report the isolation and characterization of a full length cDNA clone coding for the KS1/4 Ag, as well as, physical and biochemical studies on the antigen derived from an adenocarcinoma of the lung cell line. Affinity purification of the KS1/4 Ag reveals three glycosylated species by NaDodSO4 PAGE with molecular weights of 42, 40, and 35 kDa. The 42- and 40-kDa species are similar at the protein level, differing by their degree of glycosylation, and the 35-kDa protein results from a dibasic proteolytic cleavage of the larger m.w. species. Although both the 42- and 40-kDa forms are found on the cell surface, the 40-kDa protein appears to be the predominant species. A cDNA clone containing the complete KS1/4 coding sequence and the 5'- and 3'-non-translated regions was isolated from a library constructed from the human adenocarcinoma of the lung derived cell line, UCLA-P3. The cDNA clone contains an open reading frame of 314 amino acids which includes a putative signal sequence of 23 amino acids. Northern blot analysis shows a single RNA species of 1.5-kb. Sequence analysis of the 5' and 3' noncoding regions of the KS1/4 cDNA revealed homologies to known proto-oncogenes and inflammatory mediators.

  • Copyright © 1989 by American Association of Immunologists

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The Journal of Immunology
Vol. 142, Issue 10
15 May 1989
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Isolation and characterization of a cDNA encoding the KS1/4 epithelial carcinoma marker.
M S Perez, L E Walker
The Journal of Immunology May 15, 1989, 142 (10) 3662-3667;

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Isolation and characterization of a cDNA encoding the KS1/4 epithelial carcinoma marker.
M S Perez, L E Walker
The Journal of Immunology May 15, 1989, 142 (10) 3662-3667;
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Print ISSN 0022-1767        Online ISSN 1550-6606