Apoptin: nuclear switch triggers cancer cell death

Murphy, Ann

doi:10.1038/sj.gt.3300892

Cited by 5 publications

(1 citation statement)

References 7 publications

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“…A number of studies have been published that use cytotoxic genes to induce apoptosis in malignancies; for example, TRAIL, 25 apoptin, 26 Bcl-X S , 27 Caspase 3, 28 E2F-1, 29 FHIT, 30 and p16. 31 Among the proteins known to induce cell death, we focused on Bax for the following reasons: (1) it is a potent activator of the caspase cascade; (2) once Bax expression causes cytochrome c to be released from the mitochondria, cell death is imminent by a well described pathway; 32 and (3) Bcl-2 is known to be expressed at high levels in advanced prostate cancer which can prevent more upstream molecules from inducing apoptosis.…”

Section: Figure 5 Prostate-specific Bax Expression Induces Cell Deathmentioning

confidence: 99%

Prostate-specific expression of Bax delivered by an adenoviral vector induces apoptosis in LNCaP prostate cancer cells

et al. 2001

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Section: Figure 5 Prostate-specific Bax Expression Induces Cell Deathmentioning

confidence: 99%

Prostate-specific expression of Bax delivered by an adenoviral vector induces apoptosis in LNCaP prostate cancer cells

et al. 2001

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Apoptin Towards Safe and Efficient Anticancer Therapies

Backendorf

Noteborn

2014

Advances in Experimental Medicine and Biology

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The chicken anemia virus derived protein apoptin harbors cancer-selective cell killing characteristics, essentially based on phosphorylation-mediated nuclear transfer in cancer cells and efficient cytoplasmic degradation in normal cells. Here, we describe a growing set of preclinical experiments underlying the promises of the anti-cancer potential of apoptin. Various non-replicative oncolytic viral vector systems have revealed the safety and efficacy of apoptin. In addition, apoptin enhanced the oncolytic potential of adenovirus, parvovirus and Newcastle disease virus vectors. Intratumoral injection of attenuated Salmonella typhimurium bacterial strains and plasmid-based systems expressing apoptin resulted in significant tumor regression. In-vitro and in-vivo experiments showed that recombinant membrane-transferring PTD4- or TAT-apoptin proteins have potential as a future anticancer therapeutics. In xenografted hepatoma and melanoma mouse models PTD4-apoptin protein entered both cancer and normal cells, but only killed cancer cells. Combinatorial treatment of PTD4-apoptin with various (chemo)therapeutic compounds revealed an additive or even synergistic effect, reducing the side effects of the single (chemo)therapeutic treatment. Degradable polymeric nanocapsules harboring MBP-apoptin fusion-protein induced tumor-selective cell killing in-vitro and in-vivo and revealed the potential of polymer-apoptin protein vehicles as an anticancer agent.Besides its direct use as an anticancer therapeutic, apoptin research has also generated novel possibilities for drug design. The nuclear location domains of apoptin are attractive tools for targeting therapeutic compounds into the nucleus of cancer cells. Identification of cancer-related processes targeted by apoptin can potentially generate novel drug targets. Recent breakthroughs important for clinical applications are reported inferring apoptin-based clinical trials as a feasible reality.

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