Publications by authors named "W J Ardelt"
Although major advancements in antitumor treatment have been observed, several B cell-derived malignancies still remain incurable. A promising approach that involves targeting RNA either by the use of specific antisense oligonucleotides or cytostatic/cytotoxic ribonucleases (RNases) is being promoted. Two amphibian RNases, onconase (ONC; ranpirnase) and, more recently, r-amphinase (r-Amph), have already been tested, but thus far, mostly on solid tumors.
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- Antitumor ribonucleases are small basic proteins (10-28 kDa) that exhibit cytotoxic properties by cleaving RNA, allowing them to enter cells and degrade RNA after avoiding inhibition.
- Onconase, an amphibian ribonuclease, is particularly notable as it has undergone clinical trials; it is smaller, more stable, and more toxic than most RNase A homologues, effectively targeting multiple RNA types in cancer cells.
- Onconase shows promise as an adjunct therapy with other cancer treatments, as it can enhance the efficacy of chemotherapy and radiotherapy, necessitating further research to evaluate its clinical potential.
Onconase (Onc), a ribonuclease from oocytes of Northern Leopard frogs (Rana pipiens) is cytostatic and cytotoxic to a variety of tumor lines in vitro, inhibits growth of tumors in animal in vivo models and enhances sensitivity of tumor cells to a number of other cytotoxic agents with diverse mechanism of action. In Phase III clinical trials Onc demonstrated significant efficacy in patients with malignant mesothelioma that failed prior chemotherapy. We previously postulated that the antitumor activity of Onc and the observed synergisms with other antitumor modalities at least in part may be mediated by targeting RNA interference (RNAi).
View Article and Find Full Text PDFOnconase and amphinase, the antitumor ribonucleases from Rana pipiens oocytes.
Curr Pharm Biotechnol
June 2008
Rana pipiens oocytes contain two homologues of pancreatic ribonuclease A that are cytostatic and cytotoxic to human cancer cells. Extensively studied Onconase is in advanced Phase IIIb clinical trials against malignant mesothelioma, while Amphinase is a novel enzyme in pre-clinical development. Onconase is the smallest (104 amino acid residues) member of the ribonuclease A superfamily while Amphinase (114 residues) is the largest among amphibian ribonucleases.
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- Onconase is a ribonuclease with antitumor effects currently being tested for malignant mesothelioma, and a related ribonuclease named Amphinase has been identified in Rana pipiens oocytes.
- All four variants of Amphinase show significant cytotoxic and cytostatic effects against various leukemia cell lines, similar to Onconase, particularly by promoting cell cycle arrest and apoptosis.
- The effectiveness of Amphinase depends on its ribonuclease activity, suggesting it may also hold potential as a cancer treatment in clinical settings.