Human non-pregnancy ribonuclease with anti-Kaposi's sarcoma activity

Moza M A Al-Owais, Lars Hesse, Simon J Talbot, David J Adams

Research output: Contribution to journalArticlepeer-review

Abstract

Our demonstration of a 19kDa anti-Kaposi's sarcoma (KS) ribonuclease (RNase) in urine from a non-pregnant female may provide at least part of the explanation for the low incidence of KS in human females. N-terminal sequence analysis and isoelectric focusing of the purified RNase, coupled with the very low levels of anti-KS activity noted for recombinant forms of human eosinophil derived neurotoxin and human eosinophil cationic protein, suggest that the 19kDa enzyme is an eosinophilic protein whose potent anti-KS activity is dependent upon post-translational modifications that occur only in human cells.
Original languageEnglish
Pages (from-to)183-9
Number of pages7
JournalCancer letters
Volume176
Issue number2
Publication statusPublished - 2002

Keywords

  • Adenocarcinoma
  • Amino Acid Sequence
  • Blood Proteins
  • Blotting, Western
  • Breast Neoplasms
  • Dose-Response Relationship, Drug
  • Electrophoresis, Polyacrylamide Gel
  • Eosinophil Granule Proteins
  • Eosinophil-Derived Neurotoxin
  • Female
  • Humans
  • Isoelectric Focusing
  • Molecular Sequence Data
  • Plasmids
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary
  • Recombinant Proteins
  • Ribonucleases
  • Sarcoma, Kaposi
  • Sequence Analysis, DNA
  • Tumor Cells, Cultured

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