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 language | English |
|---|---|
| Pages (from-to) | 183-9 |
| Number of pages | 7 |
| Journal | Cancer letters |
| Volume | 176 |
| Issue number | 2 |
| Publication status | Published - 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