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The CA 125 Gene: A Newly Discovered Extension of the Glycosylated N-Terminal Domain Doubles the Size of This Extracellular Superstructure

O’Brien T.J.a · Beard J.B.a · Underwood L.J.b · Shigemasa K.c
aDepartment of Obstetrics and Gynecology, and bDepartment of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, Ark., USA; cDepartment of Obstetrics and Gynecology, Hiroshima University School of Medicine, Hiroshima, Japan Tumor Biol 2002;23:154–169 (DOI:10.1159/000064032)

Abstract

CA 125 is a well-established marker for patients diagnosed with ovarian carcinoma. It is clearly elaborated in serous cystadenocarcinomas and less likely to be expressed in mucinous tumors. It has been 20 years since CA 125 was first recognized and it is only in recent years (the past 2) that some progress has been made toward cloning the gene, providing the basis for an understanding of the functional role of this molecule in embryonic development and neoplastic transformation. It is now clear that CA 125 is a large glycoprotein which is anchored to the epithelium by a transmembrane domain and is released into the extracellular space by enzymatic cleavage. Here, we describe a further major extension to the glycosylated extracellular amino terminal domain of this molecule. These additional data in association with our previous understanding of this molecule will provide the basis for our ability to understand the physiologic function of this molecule in biologic development and pathologic transformation.

 

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