Monitoring of bystander effect of herpes simplex virus thymidine kinase/acyclovir system using fluorescence resonance energy transfer technique

Journal of Biomedical Nanotechnology

Volumn 8, Issue 1, 2012, Pages 74-79

  Xiong, Tao ^a,b   Li, Yongjun ^a   Ni, Fenge ^a   Zhang, Feng ^a  

^a YANGTZE UNIVERSITY   (China)

^b HUAZHONG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

Author keywords

Apoptosis; Bystander effect; Fluorescence Resonance Energy Transfer (FRET); HSV tk ACV

Indexed keywords

ANTI-TUMORS; APOPTOTIC; BYSTANDER EFFECTS; CANCER GENE THERAPY; CASPASE-3; CELL LINES; CYTOTOXIC; FLUORESCENCE RESONANCE ENERGY TRANSFER; HERPES SIMPLEX VIRUS; HSV-TK/ACV; IN-VIVO; MALIGNANT TUMORS; THYMIDINE KINASE;

CELL CULTURE; DRUG PRODUCTS; ENERGY TRANSFER; FLUORESCENCE; GENE THERAPY; GENE TRANSFER; VIRUSES;

CELL DEATH;

ACICLOVIR; CASPASE 3; GREEN FLUORESCENT PROTEIN; THYMIDINE KINASE;

ANTINEOPLASTIC ACTIVITY; APOPTOSIS; ARTICLE; BYSTANDER EFFECT; CANCER CELL CULTURE; CANCER GENE THERAPY; CONTROLLED STUDY; DRUG EFFECT; DRUG TARGETING; FLUORESCENCE RESONANCE ENERGY TRANSFER; GENE DIRECTED ENZYME PRODRUG THERAPY; HERPES SIMPLEX VIRUS; HUMAN; HUMAN CELL; INTRACELLULAR SIGNALING; NONVIRAL GENE DELIVERY SYSTEM; PLASMID; SUICIDE GENE;

ACYCLOVIR; ANTINEOPLASTIC AGENTS; ANTIVIRAL AGENTS; APOPTOSIS; CASPASE 3; CELL LINE, TUMOR; FLUORESCENCE RESONANCE ENERGY TRANSFER; GREEN FLUORESCENT PROTEINS; HUMANS; SIMPLEXVIRUS; THYMIDINE KINASE; TRANSFECTION; VIRAL PROTEINS;

EID: 84861466497     PISSN: 15507033     EISSN: 15507041     Source Type: Journal    
DOI: 10.1166/jbn.2012.1357     Document Type: Article

References (22)

1. E. R. Fearon, D. M. Pardoll, T. Itaya, P. Golumbek, H. I. Levitsky, J. W. Simons, H. Karasuyama, B. Vogelstein, and P. Frost, Interleukin-2 production by tumor cells bypasses T helper function in the generation of an antitumor response. Cell 60, 397 (1990).
2. 4 nanoconjugates. J. Biomed. Nanotechnol. 6, 683 (2010).
3. G. X. Xu, K. T. Yong, I. Roy, and A. Kopwitthaya, FGF2-labeled semiconductor nanocrystals as luminescent biolabels for imaging neuroblastoma cells. J. Biomed. Nanotechnol. 6, 641 (2010).
4. T. Elbayoumi and V. Weissig, Implications of intracellular distribution of nanovesicles for bioimaging studies. J. Biomed. Nanotechnol. 5, 620 (2009).
5. C. Engelmann, J. M. Heslan, M. Fabre, J. P. Lagarde, D. Klatzmann, and Y. Panis, Importance, mechanisms and limitations of the distant bystander effect in cancer gene therapy of experimental liver tumors. Cancer Lett. 179, 59 (2002).
6. I. Gautier, J. Coppey, and C. Durieux, Early apoptosis-related changes triggered by HSV-1 in individual neuronlike cells. Exp. Cell Res. 289, 174 (2003).
7. N. A. Mendoza-Sánchez, G. Ferro-Flores, B. E. Ocampo- García, E. Morales-Avila, F. M. Ramírez, L. M. León-Rodríguez, C. L. Santos-Cuevas, L. A. Medina, E. L. Rojas-Calderón, and M. A. Camacho-López, Lys3-bombesin conjugated to 99mTc-labelled gold nanoparticles for in vivo gastrin releasing peptide-receptor imaging. J. Biomed. Nanotechnol. 6, 375 (2010).
8. A. K. Tong, Z. Li, G. S. Jones, J. J. Russo, and J. Ju, Combinatorial fluorescence energy transfer tags for multiplex biological assays. Nat. Biotechnol. 19, 756 (2001).
9. Q. Li, X. Liu, and Y. He, Single molecule fluorescence imaging of DNA at agarose surfaces by total internal reflection fluorescence microscopy. J. Biomed. Nanotechnol. 5, 565 (2009).
10. X. Xu, A. L. Gerard, B. C. Huang, D. C. Anderson, D. G. Payan, and Y. Luo, Detection of programmed cell death using fluorescence energy transfer. Nucleic Acids Res. 26, 2034 (1998).
11. M. Rehm, H. Dussmann, R. U. Janicke, J. M. Tavare, D. Kogel, and J. H. Prehn, Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a rapid process. Role of caspase-3. J. Biol. Chem. 277, 24506 (2002).
12. Y. Liang, Z. Su, and X. N. Luo, A feature-preserving image retargeting based on multi-energy constraints. Adv. Sci. Lett. 4, 408 (2011).
13. T. Nagai and A. Miyawaki, A high-throughput method for development of FRET-based indicators for proteolysis. Biochem. Biophys. Res. Commun. 319, 72 (2004).
14. J. Neefjes and N. P. Dantuma, Fluorescent probes for proteolysis: Tools for drug discovery. Nat.Rev.Drug Discov. 3, 58 (2004).
15. M. Sebbagh, C. Renvoize, J. Hamelin, N. Riche, J. Bertoglio, and J. Breard, Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing. Nat. Cell Biol. 3, 346 (2001).
16. T. S. Karpova, C. T. Baumann, L. He, X. Wu, A. Grammer, P. Lipsky, G. L. Hager, and J. G. McNally, Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser. J. Microscope. 209, 56 (2003).
17. S. Magonov, J. Alexander, S. Jeong, and N. Kotov, High-resolution imaging of molecular and nanoparticles assemblies with kelvin force microscopy. J. Nanosci. Nanotechnol. 10, 7060 (2010).
18. T. Xiong, Z. Zhang, B. F. Liu, S. Zeng, Y. Chen, J. Chu, and Q. Luo, In vivo optical imaging of human adenoid cystic carcinoma cell metastasis. Oral Oncol. 41, 709 (2005).
19. A. Soling, A. Simm, and N. Rainov, Intracellular localization of herpes simplex virus type 1 thymidine kinase fused to different fluorescent proteins depends on choice of fluorescent tag. FEBS Lett. 527, 153 (2002).
20. G. S. Baird, D. A. Zacharias, and R. Y. Tsien, Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral. Proc. Natl. Acad. Sci. USA 97, 11984 (2000).
21. P. A. Robe, M. T. Nguyen-Khac, O. Jolois, B. Rogister, M. P. Merville, and V. Bours, Dexamethasone inhibits the HSVtk/ ganciclovir bystander effect in malignant glioma cells. BMC Cancer 5, 32 (2005).
22. H. M. Green and J. Alberola-Ila, Development of ERK activity sensors, an in vitro, FRET-based sensor of extracellular regulated kinase activity. BMC Chem. Biol. 5, 1 (2005).