A Hammerhead Ribozyme Cleaves Its Target RNA During RNA Preparation
- 1 January 1996
- journal article
- research article
- Published by Mary Ann Liebert Inc in Antisense and Nucleic Acid Drug Development
- Vol. 6 (2), 141-144
- https://doi.org/10.1089/oli.1.1996.6.141
Abstract
A chemically modified hammerhead ribozyme was designed to cleave the tax RNA of human T cell leukemia virus type I. This ribozyme was exogenously delivered to tax-transformed fibroblasts by DOTAP-mediated transfection. The analysis of RNA from ribozyme-transfected cells by RNase protection detected ribozyme cleavage products. However, control experiments revealed that the ribozyme did not cleave its target RNA intracellularly but during the course of the RNA isolation. This suggests that great care should be exercised when interpreting in vivo results of ribozyme cleavage.Keywords
This publication has 12 references indexed in Scilit:
- Cellular and Molecular Barriers to Gene Transfer by a Cationic LipidJournal of Biological Chemistry, 1995
- Ribozyme-mediated RNA degradation in nuclei suspensionNucleic Acids Research, 1995
- Multi-unit ribozyme-mediated cleavage of bcr-abl mRNA in myeloid leukemiasBlood, 1995
- Efficient hammerhead ribozyme-mediated cleavage of the structured heapatitis B virus encapsidation signalin vitroand in cell extracts, but not in intact cellsNucleic Acids Research, 1995
- In vitro and in vivo comparison of hammerhead, hairpin, and hepatitis delta virus self-processing ribozyme cassettes.Journal of Biological Chemistry, 1994
- Inhibition of gene expression with ribozymesCellular and Molecular Neurobiology, 1994
- Lipofectin‐aided cell delivery of ribozyme targeted to human urokinase receptor mRNAFEBS Letters, 1994
- High activity and stability of hammerhead ribozymes containing 2'-modified pyrimidine nucleosides and phosphorothioates.Journal of Biological Chemistry, 1994
- Preformed ribozyme destroys tumour necrosis factor mRNA in human cellsJournal of Molecular Biology, 1992
- Mechanisms of the inhibition of reverse transcription by antisense oligonucleotides.Proceedings of the National Academy of Sciences, 1992