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Proliferation-associated nuclear antigen Ki-S1 is identical with topoisomerase II alpha. Delineation of a carboxy-terminal epitope with peptide antibodies

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  • F Boege, Medizinische Poliklinik, University of Würzburg, Germany., Germany
  • A Andersen
  • S Jensen, Denmark
  • R Zeidler, Medizinische Poliklinik, University of Würzburg, Germany.
  • ,
  • H Kreipe, Medizinische Poliklinik, University of Würzburg, Germany., Germany

Proliferation-linked expression of the nuclear Ki-S1 antigen is a significant prognostic indicator in mammary carcinomas. Here, we show staining of a protein of 170 kd by Ki-S1 antibody in immunoblots of Saccharomyces cerevisiae expressing human topoisomerase II alpha but not in the parental strain. In HL-60 cells containing both isoforms of human topoisomerase II, Ki-S1 antibody binds selectively to the 170-kd isoenzyme in a similar fashion as peptide-antibodies directed against amino acid residues 1 to 15 or 1512 to 1530 of human topoisomerase II alpha. Conversely, antibodies directed against carboxyl-terminal sequences of human topoisomerase II beta selectively stain a 180-kd protein. The immunoreactive pattern of V8 endoproteinase restriction digests of human topoisomerase II alpha was identical for Ki-S1-antibody and peptide-antibodies directed against residues 1512 to 1530 but different for peptide-antibodies directed against residues 1 to 15. The Rf values of the smallest fragment commonly recognized by Ki-S1 antibody and the carboxy terminus-specific peptide-antibody place the Ki-S1 epitope within the last 495 carboxyl-terminal amino acid residues of topoisomerase II alpha.

Original languageEnglish
JournalAmerican Journal of Pathology
Volume146
Issue6
Pages (from-to)1302-8
Number of pages7
ISSN0002-9440
Publication statusPublished - Jun 1995

    Research areas

  • Animals, Antigens, Neoplasm, Blotting, Western, DNA Topoisomerases, Type II, DNA-Binding Proteins, Epitope Mapping, Epitopes, Humans, Immunoglobulin G, Isoenzymes, Nuclear Proteins, Rabbits, Recombinant Proteins, Journal Article, Research Support, Non-U.S. Gov't

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