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Institut für Immunbiologie, Universität Freiburg, Stefan-Meier-Strasse 8, D-7800 Freiburg, Federal Republic of Germany [B. B., F. K., F. G., J. A. T., F. Br.]; Max Planck Institut für Immunbiologie, Stübeweg 51, D-7800 Freiburg, Federal Republic of Germany [F. B.]; and Institut de Biochemie, Université de Lausanne, Chemin des Boveresses 155, CH-1066 Epalinges, Switzerland [S. v K., W. Z.]
The carcinoembryonic antigen (CEA) gene family belongs to the immunoglobulin superfamily and can be subdivided into the CEA and pregnancy-specific glycoprotein subgroups. The basic structure of the encoded proteins consists of, in addition to a leader, one IgV-like and 2, 3, or 6 IgC-like domains. These domains are followed by varying COOH-terminal regions responsible for secretion, transmembrane anchoring, or insertion into the membrane by a glycosyl phosphatidylinositol tail. Here we report on the characterization of CGM6, a new member of the CEA gene subgroup, by complementary DNA cloning. The deduced coding region comprises 349 amino acids and consists of a leader, one IgV-like, two IgC-like domains, and a hydrophobic region, which is replaced by a glycosyl phosphatidylinositol moiety in the mature protein. CGM6 transcripts were only found thus far in leukocytes of chronic myeloid leukemia patients, in normal bone marrow, and in marginal amounts in normal granulocytes. The CGM6 gene product might, therefore, represent a myeloid marker. Analyses of CGM6 protein-expressing HeLa transfectants with monoclonal antibodies strongly indicate that the CGM6 gene codes for the CEA family member NCA-95.
1 This work was supported by a grant from the Dr. Mildred Scheel Stiftung für Krebsforschung.
2 To whom requests for reprints should be addressed.
Received 3/ 9/90. Accepted 7/13/90.
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