Molecular Cloning of the CA125 Ovarian Cancer Antigen

By B. W. Yin, K. Lloyd. Journal of Biological Chemistry, 2001

610 citations recorded by the source corpus.

CA125 is an ovarian cancer antigen that is the basis for a widely used serum assay for the monitoring of patients with ovarian cancer; however, detailed information on its biochemical and molecular nature is lacking. We now report the isolation of a long, but partial, cDNA that corresponds to the CA125 antigen. A rabbit polyclonal antibody produced to purified CA125 antigen was used to screen a λZAP cDNA library from OVCAR-3 cells inEscherichia coli. The longest insert from the 54 positive isolated clones had a 5797-base pair sequence containing a stop codon and a poly(A) sequence but no clear 5′ initiation sequence. The deduced amino acid sequence has many of the attributes of a mucin molecule and was designated CA125/MUC16 (gene MUC16). These features include a high serine, threonine, and proline content in an N-terminal region of nine partially conserved tandem repeats (156 amino acids each) and a C-terminal region non-tandem repeat sequence containing a possible transmembrane region and a potential tyrosine phosphorylation site. Northern blotting showed that the level of MUC16 mRNA correlated with the expression of CA125 in a panel of cell lines. The molecular cloning of the CA125 antigen will lead to a better understanding of its role in ovarian cancer.

Subfields: Immunology, Molecular Biology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/eea98920c0278b99a5d7b3f5562c4566e962c499

How researchers see this paper

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In Immunology

1. Richard D. Cummings
2. D. Kufe
3. T. Ju
4. S. Stowell

In Molecular Biology

1. Bryan T. J. Hennessy
2. Gordon B. Mills
3. Richard D. Cummings
4. D. Kufe
5. T. Ju
6. S. Stowell

In Radiology, Nuclear Medicine and Imaging

1. D. Kufe

Citations in the corpus

• The biology of ovarian cancer: new opportunities for translation (2009, background): “Adhesion is mediated by β integrins, CD44 and CA125 (Ref”
• Protein Glycosylation in Cancer (2015, background): “Molecular cloning of the CA125 ovarian cancer antigen: identification as a new mucin, MUC16.”
• TFOS DEWS II pathophysiology report. (2017, background): “They package and secrete the gel-forming mucin, MUC5AC [83], which, when fully glycosylated has a mass of up to 40 MDa [98,99].”
• Mucins in cancer: function, prognosis and therapy (2009, background): “110 ) was found — some 20 years after its discovery — to be encoded by a gene with an amino acid sequence containing tandem repeats with homology to SEA domains, a transmembrane domain and a 31-amino-acid cytoplasmic tai”
• Sialic acids in human health and disease (2008, neutral): “Secreted or proteolytically released carcinoma mucins bearing some of these unusual forms of sialylation can be detected in the bloodstream of cancer patients and are used as diagnostic and prognostic aids [109,110].”