Artículo

Booth, L.; Roberts, J.L.; Ecroyd, H.; Tritsch, S.R.; Bavari, S.; Reid, S.P.; Proniuk, S.; Zukiwski, A.; Jacob, A.; Sepúlveda, C.S.; Giovannoni, F.; García, C.C.; Damonte, E.; González-Gallego, J.; Tuñón, M.J.; Dent, P. "AR-12 Inhibits Multiple Chaperones Concomitant With Stimulating Autophagosome Formation Collectively Preventing Virus Replication" (2016) Journal of Cellular Physiology. 231(10):2286-2302
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Abstract:

We have recently demonstrated that AR-12 (OSU-03012) reduces the function and ATPase activities of multiple HSP90 and HSP70 family chaperones. Combined knock down of chaperones or AR-12 treatment acted to reduce the expression of virus receptors and essential glucosidase proteins. Combined knock down of chaperones or AR-12 treatment inactivated mTOR and elevated ATG13 S318 phosphorylation concomitant with inducing an endoplasmic reticulum stress response that in an eIF2α—dependent fashion increased Beclin1 and LC3 expression and autophagosome formation. Over-expression of chaperones prevented the reduction in receptor/glucosidase expression, mTOR inactivation, the ER stress response, and autophagosome formation. AR-12 reduced the reproduction of viruses including Mumps, Influenza, Measles, Junín, Rubella, HIV (wild type and protease resistant), and Ebola, an effect replicated by knock down of multiple chaperone proteins. AR-12—stimulated the co-localization of Influenza, EBV and HIV virus proteins with LC3 in autophagosomes and reduced viral protein association with the chaperones HSP90, HSP70, and GRP78. Knock down of Beclin1 suppressed drug-induced autophagosome formation and reduced the anti-viral protection afforded by AR-12. In an animal model of hemorrhagic fever virus, a transient exposure of animals to low doses of AR-12 doubled animal survival from ∼30% to ∼60% and suppressed liver damage as measured by ATL, GGT and LDH release. Thus through inhibition of chaperone protein functions; reducing the production, stability and processing of viral proteins; and stimulating autophagosome formation/viral protein degradation, AR-12 acts as a broad-specificity anti-viral drug in vitro and in vivo. We argue future patient studies with AR-12 are warranted. J. Cell. Physiol. 231: 2286–2302, 2016. © 2016 Wiley Periodicals, Inc. © 2016 Wiley Periodicals, Inc.

Registro:

Documento: Artículo
Título:AR-12 Inhibits Multiple Chaperones Concomitant With Stimulating Autophagosome Formation Collectively Preventing Virus Replication
Autor:Booth, L.; Roberts, J.L.; Ecroyd, H.; Tritsch, S.R.; Bavari, S.; Reid, S.P.; Proniuk, S.; Zukiwski, A.; Jacob, A.; Sepúlveda, C.S.; Giovannoni, F.; García, C.C.; Damonte, E.; González-Gallego, J.; Tuñón, M.J.; Dent, P.
Filiación:Department of Biochemistry and Molecular Biology, Virginia Commonwealth University, Richmond, VA, United States
School of Biological Sciences and Illawarra Health and Medical Research Institute, University of Wollongong, NSW, Australia
Molecular and Translational Science, United States Army Medical Research Institute of Infectious Diseases (USAMRIID), Fort Detrick, Frederick, MD, United States
Arno Therapeutics, Flemington, NJ, United States
Department of Otolaryngology, University of Arizona Ear Institute, Tucson, AZ, United States
FCEN-UBA, Ciudad Universitaria, Pabellón 2 Piso 4, lab QB-17, Buenos Aires, Argentina
Institute of Biomedicine and CIBEREhd, University of León, León, Spain
Palabras clave:2 amino n [4 [5 (2 phenanthrenyl) 3 trifluoromethyl 1h pyrazol 1 yl]phenyl]acetamide; adenosine triphosphatase; antivirus agent; ar 12; beclin 1; chaperone; gamma glutamyltransferase; glucose regulated protein 78; glucosidase; heat shock protein 27; heat shock protein 70; heat shock protein 90; initiation factor 2alpha; lactate dehydrogenase; lc3 protein; mammalian target of rapamycin; pazopanib; small interfering RNA; sorafenib; unclassified drug; virus protein; virus receptor; animal experiment; Article; autophagosome; autophagy; cell killing; cell viability; controlled study; Coxsackievirus B4; cytolysis; Ebolavirus; endoplasmic reticulum stress; enzyme release; experimental rabbit; gene overexpression; gene silencing; human; human cell; Human immunodeficiency virus; immunofluorescence test; Influenza virus; Junin virus; macrophage; Measles virus; mouse; Mumps virus; nonhuman; priority journal; protein dephosphorylation; protein glycosylation; protein localization; protein phosphorylation; protein protein interaction; Rubella virus; virus replication; wild type
Año:2016
Volumen:231
Número:10
Página de inicio:2286
Página de fin:2302
DOI: http://dx.doi.org/10.1002/jcp.25431
Título revista:Journal of Cellular Physiology
Título revista abreviado:J. Cell. Physiol.
ISSN:00219541
CODEN:JCLLA
CAS:adenosine triphosphatase, 37289-25-1, 9000-83-3; gamma glutamyltransferase, 85876-02-4; glucosidase, 9033-06-1; lactate dehydrogenase, 9001-60-9; pazopanib, 444731-52-6, 635702-64-6; sorafenib, 284461-73-0
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219541_v231_n10_p2286_Booth

Referencias:

  • Anderson, K., Stott, E.J., Wertz, G.W., Intracellular processing of the human respiratory syncytial virus fusion glycoprotein: Amino acid substitutions affecting folding, transport and cleavage (1992) J Gen Virol, 73, pp. 1177-1188
  • Bolt, G., The measles virus (MV) glycoproteins interact with cellular chaperones in the endoplasmic reticulum and MV infection upregulates chaperone expression (2001) Arch Virol, 146, pp. 2055-2068
  • Booth, L., Cazanave, S.C., Hamed, H.A., Yacoub, A., Ogretmen, B., Chen, C.S., Grant, S., Dent, P., OSU-03012 suppresses GRP78/BiP expression that causes PERK-dependent increases in tumor cell killing (2012) Cancer Biol Ther, 13, pp. 224-236
  • Booth, L., Roberts, J.L., Cruickshanks, N., Grant, S., Poklepovic, A., Dent, P., Regulation of OSU-03012 toxicity by ER stress proteins and ER stress-inducing drugs (2014) Mol Cancer Ther, 13, pp. 2384-2398
  • Booth, L., Roberts, J.L., Tavallai, M., Nourbakhsh, A., Chuckalovcak, J., Carter, J., Poklepovic, A., Dent, P., OSU-03012 and viagra treatment inhibits the activity of multiple chaperone proteins and disrupts the blood-brain barrier: Implications for anti-cancer therapies (2015) J Cell Physiol, 230, pp. 1982-1998
  • Booth, L., Roberts, J.L., Cash, D.R., Tavallai, S., Jean, S., Fidanza, A., Cruz-Luna, T., Dent, P., GRP78/BiP/HSPA5/Dna K is a universal therapeutic target for human disease (2015) J Cell Physiol, 230, pp. 1661-1676
  • Booth, L., Shuch, B., Albers, T., Roberts, J.L., Tavallai, M., Proniuk, S., Zukiwski, A., Dent, P., Multi-kinase inhibitors can associate with heat shock proteins through their NH2-termini by which they suppress chaperone function (2016) Oncotarget, 7, pp. 12975-12996
  • Booth, L., Roberts, J.L., Tavallai, M., Webb, T., Leon, D., Chen, J., McGuire, W.P., Dent, P., The afatinib resistance of in vivo generated H1975 lung cancer cell clones is mediated by SRC/ERBB3/c-KIT/c-MET compensatory survival signaling (2016) Oncotarget, 7, pp. 19620-19630
  • Booth, L., Roberts, J.L., Tavallai, M., Chuckalovcak, J., Stringer, D.K., Koromilas, A.E., Boone, D.L., Dent, P., [Pemetrexed+Sorafenib] lethality is increased by inhibition of ERBB1/2/3-PI3K-NFκB compensatory survival signaling (2016) Oncotarget, 7, pp. 23608-23632
  • Buckheit, R.W., Jr., Swanstrom, R., Characterization of an HIV-1 isolate displaying an apparent absence of virion-associated reverse transcriptase activity (1991) AIDS Res Hum Retroviruses, 7, pp. 295-302
  • Carón, R.W., Yacoub, A., Li, M., Zhu, X., Mitchell, C., Hong, Y., Hawkins, W., Dent, P., Activated forms of H-RAS and K-RAS differentially regulate membrane association of PI3K, PDK-1, and AKT and the effect of therapeutic kinase inhibitors on cell survival (2005) Mol Cancer Ther, 4, pp. 257-270
  • Chang, J., Block, T.M., Guo, J.T., Antiviral therapies targeting host ER alpha-glucosidases: Current status and future directions (2013) Antiviral Res, 99, pp. 251-260
  • Dabo, S., Meurs, E.F., DsRNA-dependent protein kinase PKR and its role in stress, signaling and HCV infection (2012) Viruses, 4, pp. 2598-2635
  • De Clercq, E., Ebola virus (EBOV) infection: Therapeutic strategies (2015) Biochem Pharmacol, 93, pp. 1-10
  • Dimcheff, D.E., Faasse, M.A., McAtee, F.J., Portis, J.L., Endoplasmic reticulum (ER) stress induced by a neurovirulent mouse retrovirus is associated with prolonged BiP binding and retention of a viral protein in the ER (2004) J Biol Chem, 279, pp. 33782-33790
  • Earl, P.L., Moss, B., Doms, R.W., Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein (1991) J Virol, 65, pp. 2047-2055
  • Gao, M., Yeh, P.Y., Lu, Y.S., Hsu, C.H., Chen, K.F., Lee, W.C., Feng, W.C., Cheng, A.L., OSU-03012, a novel celecoxib derivative, induces reactive oxygen species-related autophagy in hepatocellular carcinoma (2008) Cancer Res, 68, pp. 9348-9357
  • Gober, M.D., Wales, S.Q., Aurelian, L., Herpes simplex virus type 2 encodes a heat shock protein homologue with apoptosis regulatory functions (2005) Front Biosci, 10, pp. 2788-2803
  • Goodwin, E.C., Lipovsky, A., Inoue, T., Magaldi, T.G., Edwards, A.P., Van Goor, K.E., Paton, A.W., DiMaio, D., BiP and multiple DNAJ molecular chaperones in the endoplasmic reticulum are required for efficient simian virus 40 infection (2011) MBio, 2, pp. e00101-e00111
  • Hogue, B.G., Nayak, D.P., Synthesis and processing of the influenza virus neuraminidase, a type II transmembrane glycoprotein (1992) Virology, 188, pp. 510-517
  • Lee, A.S., GRP78 induction in cancer: Therapeutic and prognostic implications (2007) Cancer Res, 67, pp. 3496-3499
  • Liu, J., Zhang, L., Zhu, X., Bai, J., Wang, L., Wang, X., Jiang, P., Heat shock protein 27 is involved in PCV2 infection in PK-15 cells (2014) Virus Res, 189, pp. 235-242
  • Luo, B., Lee, A.S., The critical roles of endoplasmic reticulum chaperones and unfolded protein response in tumorigenesis and anticancer therapies (2013) Oncogene, 32, pp. 805-818
  • Mathew, S.S., Della Selva, M.P., Burch, A.D., Modification and reorganization of the cytoprotective cellular chaperone Hsp27 during herpes simplex virus type 1 infection (2009) J Virol, 83, pp. 9304-9312
  • Mirazimi, A., Svensson, L., ATP is required for correct folding and disulfide bond formation of rotavirus VP7 (2000) J Virol, 74, pp. 8048-8052
  • Mohr, E.L., McMullan, L.K., Lo, M.K., Spengler, J.R., Bergeron, É., Albariño, C.G., Shrivastava-Ranjan, P., Flint, M., Inhibitors of cellular kinases with broad-spectrum antiviral activity for hemorrhagic fever viruses (2015) Antiviral Res, 120, pp. 40-47
  • Ni, M., Lee, A.S., ER chaperones in mammalian development and human diseases (2007) FEBS Lett, 581, pp. 3641-3651
  • Park, M.A., Yacoub, A., Rahmani, M., Zhang, G., Hart, L., Hagan, M.P., Calderwood, S.K., Dent, P., OSU-03012 stimulates PKR-like endoplasmic reticulum-dependent increases in 70-kDa heat shock protein expression, attenuating its lethal actions in transformed cells (2008) Mol Pharmacol, 73, pp. 1168-1184
  • Rathore, A.P.S., Ng, M.L., Vasudevan, S.G., Differential unfolded protein response during Chikungunya and Sindbis virus infection: CHIKV nsP4 suppresses eIF2α phosphorylation (2013) Virol J, 10, p. 36
  • Reid, S.P., Shurtleff, A.C., Costantino, J.A., Tritsch, S.R., Retterer, C., Spurgers, K.B., Bavari, S., HSPA5 is an essential host factor for Ebola virus infection (2014) Antiviral Res, 109, pp. 171-174
  • Roberts, J.L., Tavallai, M., Nourbakhsh, A., Fidanza, A., Cruz-Luna, T., Smith, E., Siembida, P., Dent, P., GRP78/Dna K is a target for Nexavar/Stivarga/Votrient in the treatment of human malignancies, viral infections and bacterial diseases (2015) J Cell Physiol, 230, pp. 2552-2578
  • Roux, L., Selective and transient association of Sendai virus HN glycoprotein with BiP (1990) Virology, 175, pp. 161-166
  • San-Miguel, B., Álvarez, M., Culebras, J.M., González-Gallego, J., Tuñón, M.J., N-acetyl-cysteine protects liver from apoptotic death in an animal model of fulminant hepatic failure (2006) Apoptosis, 11, pp. 1945-1957
  • Tavallai, M., Hamed, H.A., Roberts, J.L., Cruickshanks, N., Chuckalovcak, J., Poklepovic, A., Booth, L., Dent, P., Nexavar/Stivarga and viagra interact to kill tumor cells (2015) J Cell Physiol, 230, pp. 2281-2298
  • Tsai, Y.L., Zhang, Y., Tseng, C.C., Stanciauskas, R., Pinaud, F., Lee, A.S., Characterization and mechanism of stress-induced translocation of 78-kilodalton glucose-regulated protein (GRP78) to the cell surface (2015) J Biol Chem, 290, pp. 8049-8064
  • Tuñón, M.J., Sánchez-Campos, S., García-Ferreras, J., Álvarez, M., Jorquera, F., González-Gallego, J., Rabbit hemorrhagic viral disease: Characterization of a new animal model of fulminant liver failure (2003) J Lab Clin Med, 141, pp. 272-278
  • Tuñón, M.J., San-Miguel, B., Crespo, I., Jorquera, F., Santamaría, E., Álvarez, M., Prieto, J., González-Gallego, J., Melatonin attenuates apoptotic liver damage in fulminant hepatic failure induced by the rabbit hemorrhagic disease virus (2011) J Pineal Res, 50, pp. 38-45
  • Vashist, S., Urena, L., Gonzalez-Hernandez, M.B., Choi, J., de Rougemont, A., Rocha-Pereira, J., Neyts, J., Goodfellow, I., Molecular chaperone Hsp90 is a therapeutic target for noroviruses (2015) J Virol, 89, pp. 6352-6363
  • Xu, A., Bellamy, A.R., Taylor, J.A., BiP (GRP78) and endoplasmin (GRP94) are induced following rotavirus infection and bind transiently to an endoplasmic reticulum-localized virion component (1998) J Virol, 72, pp. 9865-9872
  • Yacoub, A., Park, M.A., Hanna, D., Hong, Y., Mitchell, C., Pandya, A.P., Harada, H., Dent, P., OSU-03012 promotes caspase-independent but PERK-, cathepsin B-, BID-, and AIF-dependent killing of transformed cells (2006) Mol Pharmacol, 70, pp. 589-603
  • Zhang, C., Kang, K., Ning, P., Peng, Y., Lin, Z., Cui, H., Cao, Z., Zhang, Y., Heat shock protein 70 is associated with CSFV NS5A protein and enhances viral RNA replication (2015) Virology, 482, pp. 9-18
  • Zhu, J., Huang, J.W., Tseng, P.H., Yang, Y.T., Fowble, J., Shiau, C.W., Shaw, Y.J., Chen, C.S., From the cyclooxygenase-2 inhibitor celecoxib to a novel class of 3-phosphoinositide-dependent protein kinase-1 inhibitors (2004) Cancer Res, 64, pp. 4309-4318

Citas:

---------- APA ----------
Booth, L., Roberts, J.L., Ecroyd, H., Tritsch, S.R., Bavari, S., Reid, S.P., Proniuk, S.,..., Dent, P. (2016) . AR-12 Inhibits Multiple Chaperones Concomitant With Stimulating Autophagosome Formation Collectively Preventing Virus Replication. Journal of Cellular Physiology, 231(10), 2286-2302.
http://dx.doi.org/10.1002/jcp.25431
---------- CHICAGO ----------
Booth, L., Roberts, J.L., Ecroyd, H., Tritsch, S.R., Bavari, S., Reid, S.P., et al. "AR-12 Inhibits Multiple Chaperones Concomitant With Stimulating Autophagosome Formation Collectively Preventing Virus Replication" . Journal of Cellular Physiology 231, no. 10 (2016) : 2286-2302.
http://dx.doi.org/10.1002/jcp.25431
---------- MLA ----------
Booth, L., Roberts, J.L., Ecroyd, H., Tritsch, S.R., Bavari, S., Reid, S.P., et al. "AR-12 Inhibits Multiple Chaperones Concomitant With Stimulating Autophagosome Formation Collectively Preventing Virus Replication" . Journal of Cellular Physiology, vol. 231, no. 10, 2016, pp. 2286-2302.
http://dx.doi.org/10.1002/jcp.25431
---------- VANCOUVER ----------
Booth, L., Roberts, J.L., Ecroyd, H., Tritsch, S.R., Bavari, S., Reid, S.P., et al. AR-12 Inhibits Multiple Chaperones Concomitant With Stimulating Autophagosome Formation Collectively Preventing Virus Replication. J. Cell. Physiol. 2016;231(10):2286-2302.
http://dx.doi.org/10.1002/jcp.25431