Purification and characterization of a human sialoglycoprotein antigen expressed in immature thymocytes and fetal tissues

L. Cecco, H. M. Bond, P. Bonelli, F. Tuccillo, M. Cerra, P. Tassone, R. Sorice, A. Lamberti, G. Morrone, S. Venuta

Research output: Contribution to journalArticlepeer-review


The monoclonal antibody UN1 was previously produced in our laboratory on the basis of selective reactivity with human thymocytes and has been classified as unclustered by the 5th and 6th International Work shop and Conference on Human Leukocyte Differentiation Antigens. The antigen recognized by mAb UN1 was found to be expressed on the cell surface of immature human thymocytes, a subpopulation of peripheral T lymphocytes and on several fetal tissues including thymus. The UN1 antigen is purified from children's thymus by ionexchange and affinity chromatography. Two-dimensional electrophoresis shows that the purified antigen displays microheterogeneity appearing as multiple spots over a pI range 4.4-5.0 at 100-120 kDa. Treatment with neuraminidase results in a retarded migration in SDS-PAGE, an increase in isoelectric point and a reduction in carbohydrate content, indicating a substantial content of sialic acid. Glycosidase digestion and lectin-binding analysis indicate that the carbohydrate residues are essentially O-linked. A preliminary analysis has detected the UN1 antigen in human breast carcinoma tissues but not in normal breast. The biochemical features and the pattern of expression of the UN1 antigen indicate that this molecule may have the characteristics typical of the family of cell-membrane-associated mucin-like glycoproteins; a number of these molecules are thought to have a role in cell-cell interaction, tumor progression and metastasis.

Original languageEnglish
Pages (from-to)528-535
Number of pages8
JournalTissue Antigens
Issue number5
Publication statusPublished - 1998


  • Breast carcinoma
  • Mucin
  • Sialoglycoprotein
  • Thymic antigen

ASJC Scopus subject areas

  • Immunology
  • Cell Biology


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