Researchers at University of Kentucky College of Medicine Report Findings in Cancer Gene Therapy (Proteasomal regulation of caspase-8 in cancer cell apoptosis)
By a News Reporter-Staff News Editor at Cancer Gene Therapy Week -- Investigators publish new report on Biotechnology. According to news originating from Lexington, Kentucky, by NewsRx correspondents, research stated, "Previous studies demonstrated that proteasome inhibition sensitizes TRAIL resistant prostate cancer cells to TRAIL-mediated apoptosis via stabilization of the active p18 subunit of caspase-8. The present study investigated the impact of proteasome inhibition on caspase-8 stability, ubiquitination, trafficking, and activation in cancer cells."
Our news journalists obtained a quote from the research from the University of Kentucky College of Medicine, "Using caspase-8 deficient neuroblastoma (NB7) cells for reconstituting non-cleavable mutant forms of caspase-8, we demonstrated that the non-cleavable forms of caspase-8 are capable of inducing apoptosis comparably to wild-type caspase-8, in response to proteasome inhibitor and GST-TRAIL. Moreover in the LNCaP human prostate cancer cells, caspase-8 polyubiquitination occurs after TRAIL stimulation and caspase-8 processing. Subcellular fractionation analysis revealed caspase-8 activity in both cytosol and plasma membrane fractions in both NB7 reconstituted caspase-8 cell lines, as well the LNCaP prostate cancer cells. The present results suggest that caspase-8 stabilization through proteasome inhibition leads to reactivation of the extrinsic pathway of apoptosis and identify E3 ligase mediating caspase-8 polyubiquitination, as a novel molecular target."
According to the news editors, the research concluded: "Inhibition of this E3 ligase in combination with TRAIL towards restoring apoptosis signaling activation may have potential therapeutic significance in resistant tumors."
For more information on this research see: Proteasomal regulation of caspase-8 in cancer cell apoptosis. Apoptosis, 2013;18(6):766-76. Apoptosis can be contacted at: Springer, 233 Spring Street, New York, NY 10013, USA. (Springer - www.springer.com; Apoptosis - www.springerlink.com/content/1360-8185/)
The news correspondents report that additional information may be obtained from M.V. Fiandalo, Dept. of Molecular and Cellular Biochemistry and the Markey Cancer Center, University of Kentucky College of Medicine, Combs Cancer Research Building, 306, 800 Rose Street, Lexington, KY 40536, United States. Additional authors for this research include S.R. Schwarze and N. Kyprianou (see also Biotechnology).
The publisher's contact information for the journal Apoptosis is: Springer, 233 Spring Street, New York, NY 10013, USA.
Keywords for this news article include: Biotechnology, Ligases, Kentucky, Caspases, Oncology, Lexington, Apoptosis, United States, Prostate Cancer, Peptide Hydrolases, Cancer Gene Therapy, Prostatic Neoplasms, Enzymes and Coenzymes, Cysteine Endopeptidases, North and Central America.
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