Hsp27 anti-sense oligonucleotides sensitize the microtubular cytoskeleton of Chinese hamster ovary cells grown at low pH to 42°C-induced reorganization

References

• Wahl ML, Coss RA, Bobyock SB, Leeper DB, Owen CS. Thermotolerance and intracel-lular pH in two Chinese hamster cell lines adapted to growth at low pH. J Cell Physiol 1996; 166: 438–45.
   Google Scholar
• Wahl ML, Bobyock SB, Leeper DB, Owen CS. Effects of 42°C hyperthermia on intracellular pH in ovarian carcinoma cells during acute or chronic exposure to low extracellular pH. Int J Radiat Oncol Biol Phys 1997; 39: 205–12.
   PubMed Web of Science ®Google Scholar
• Coss RA, Messinger JA, Wahl ML, Wachsberger PR, Leeper DB, Owen CS. Bicarbonate-dependent proton extrusion in Chinese hamster ovary (CHO) cells adapted to growth at pH 6.7. Int J Hypertherrnia 1997; 13: 325–36.
   Google Scholar
• Chu GL, Dewey WC. The role of low intracellular or extracellular pH in sensitization to hyperthermia. Radiat Res 1988; 114: 154–67.
   PubMed Web of Science ®Google Scholar
• Hahn GM, Shiu EC. Adaptation to low pH modifies thermal and thermo-chemical responses of mammalian cells. Int J Hypertherrnia 1986; 2: 379–87.
   PubMedGoogle Scholar
• Cook J, Fox M. Effects of chronic pH 6.6 on growth, intracellular pH, and response to 42°C hyperthermia of Chinese hamster ovary cell. Cancer Res 1988; 48: 2417–20.
   Google Scholar
• Owen CS, Pooler PM, Wahl ML, Coss RA, Leeper DB. Altered proton extrusion in cells adapted to growth at low extracellular pH. J Cell Physiol 1997; 173: 397–405.
   Google Scholar
• Coss RA, Sistrun S, Storck C, Wachsberger PR. Response of the cytoskeleton and nuclear matrix to 42°C in Chinese hamster ovary (CHO) cells adapted to growth at pH 6.7. Hypertherrnic Oncol 1996; 2: 678–9.
   Google Scholar
• Coss RA, Sedar AW, Sistrun SS, Storck CW, Wang PH, Wachsberger PR. Hsp27 protect the cytoskeleton and nucleus from the effects of 42°C at pH 6.7 in CHO cells adapted to growth at pH 6.7. Int j Hypertherrnia 2002; 18: 216–32.
   Google Scholar
• Wachsberger PR, Landry J, Storck C, Davis K, O'Hara MD, Owen CS, Leeper DB, Coss RA. Mammalian cells adapted to growth at pH 6.7 have elevated H5P27 levels and are resistant to cisplatin. Int j Hypertherrnia 1997; 13: 251–5.
   Google Scholar
• Lindquist S. The heat-shock response. Annu Rev Biochern 1986; 55: 1151–91.
   PubMed Web of Science ®Google Scholar
• Lindquist S, Craig EA. The heat-shock proteins. Annu Rev Genet 1988; 22: 631–77.
   PubMed Web of Science ®Google Scholar
• Jolly C, Morimoto RI. Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J Natl Cancer Inst 2000; 92: 1564–72.
   PubMed Web of Science ®Google Scholar
• Charette SJ, Lavoie JN, Lambert H, Landry J. Inhibition of Daxx-mediated apoptosis by heat shock protein 27. Mol Cell Biol 2000; 20: 7602–12.
   PubMed Web of Science ®Google Scholar
• Jaattela M. Escaping cell death: survival proteins in cancer. Exp Cell Res 1999; 248: 30–43.
   PubMed Web of Science ®Google Scholar
• Parcellier A, Gurbuxani S, Schmitt E, Solary E, Garrido C. Heat shock proteins, cellular chaperones that modulate mitochondrial cell death pathways. Biochern Biophys Res Commun 2003; 304: 505–12.
   Google Scholar
• Lin PS. Cytoskeleton and modified cellular heat sensitivity. In: Henle KJ, ed., Therrnotolerance, Vol. II, Boca Raton: CRC Press, 1987; 83–104.
   Google Scholar
• Laszlo A. The effects of hyperthermia on mammalian cell structure and function. Cell Proliferation 1992; 25: 59–87.
   PubMed Web of Science ®Google Scholar
• Coss RA, Linnemans WAM. The effects of hyperthermia on the cytoskeleton. Int J Hypertherrnia 1996; 12: 173–96.
   PubMed Web of Science ®Google Scholar
• Wachsberger PR, Coss RA. Acrylamide sensitization of the heat response of the cytoske-leton and cytotoxicity in attaching and well-spread synchronous Chinese hamster ovary cells. Cell Motil Cytoskeleton 1989; 13: 67–82.
   PubMedGoogle Scholar
• Wachsberger PR, Coss RA. Effects of hyperthermia on the cytoskeleton and cell survival in G1 and S phase Chinese hamster ovary cells. Int J Hypertherrnia 1990; 6: 67–85.
   PubMed Web of Science ®Google Scholar
• Landry J, Chretien P, Lambert H, Hickey E, Weber LA. Heat shock resistance conferred by expression of the human Hsp27 gene in rodent cells. J Cell Biol 1989; 109: 7–15.
   Google Scholar
• Lavoie JN, Gingras-Breton G, Tanguay RM, Landry J. Induction of Chinese hamster Hsp27 gene expression in mouse cells confers resistance to heat shock. Hsp27 stabilization of the microfilament organization. J Biol Chem 1993; 268: 3420–9.
   Google Scholar
• Richards EH, Hickey E, Weber L, Masters JRW. Effect of overexpression of the small heat shock protein Hsp27 on the heat and drug sensitivities of human testis tumor cells. Cancer Res 1996; 56: 2446–51.
   PubMed Web of Science ®Google Scholar
• Lavoie JN, Hickey E, Weber LA, Landry J. Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat-shock protein 27. J Biol Chem 1993; 268: 24210–4.
   PubMed Web of Science ®Google Scholar
• Mourner N, Arrigo AP. Actin cytoskeleton and small heat shock proteins: how do they interact? Cell Stress Chaperones 2002; 7: 167–76.
   PubMedGoogle Scholar
• Miron T, Vancompernolle K, Vanderkerckhove J, Wilchek M, Geiger B. A 25-kD inhibitor of actin polymerization is a low molecular mass heat-shock protein. J Cell Biol 1991; 114: 255–61.
   Google Scholar
• Landry J, Chretien P, Laszlo A, Lambert H. Phosphorylation of H5P27 during development and decay of thermotolerance in Chinese hamster cells. J Cell Physiol 1991; 147: 93–101.
   PubMed Web of Science ®Google Scholar
• Benndorf R, Hayess S, Ryazantsev S, Wieske M, Behlke J, Lutsch G. Phosphorylation and supramolecular organization of murine small heat shock protein Hsp25 abolish its actin polymerization-inhibiting activity. J Biol Chem 1994; 269: 20780–4.
   PubMed Web of Science ®Google Scholar
• Lavoie JN, Lambert H, Hickey E, Weber LE, Landry J. Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. Mol and Cell Biol 1995; 15: 505–16.
   Google Scholar
• Kato K, Hasgawa K, Goto S, Inaguma Y. Dissociation as a result of phosphorylation of an aggregated form of the small stress protein Hsp27. J Biol Chem 1994; 269: 11274–8.
   PubMed Web of Science ®Google Scholar
• Guay J, Lambert H, Gingras-Breton G, Lavoie JN, Huot J, Landry J. Regulation of actin filament dynamics by p38 map-kinase-mediated phosphorylation of heat shock protein 27. J Cell Sci 1997; 110: 357–68.
   Google Scholar
• Borrelli MJ, Bernock Li, Landry J, Spitz DR, Weber LA, Hickey E, Freeman ML, Corry PM. Stress protection by a fluorescent Hsp27 chimera that is independent of nuclear translocation or multimeric dissociation. Cell Stress Chaperones 2002; 7: 281–96.
   PubMedGoogle Scholar
• Coss RA, Dewey WC, Bamburg JR. Effects of hyperthermia on dividing Chinese hamster ovary cells and on microtubules in vitro. Cancer Res 1982; 42: 1059–71.
   Google Scholar
• Coss RA, Alden ME, Wachsberger PR, Smith NN. Response of the microtubular cyto-skeleton following hyperthermia as a prognostic indicator of survival of Chinese hamster ovary cells. Int J Radiat Oncol Biol Phys 1996; 34: 403–10.
   PubMedGoogle Scholar
• Hino M, Kurogi K, Okubo MA, Murata-Hori M, Hosoya H. Small heat shock protein 27 (H5P27) associates with tubulin/microtubules in HeLa cells. Biochern Biophys Res Comm 2000; 271: 164–9.
   PubMed Web of Science ®Google Scholar
• Arai H, Atomi Y. Chaperone activity of alpha B-crystallin suppresses tubulin aggregation through complex formation. Cell Struct Funct 1997; 22: 539–44.
   PubMed Web of Science ®Google Scholar
• Day RM, Gupta JS, MacRae TH. A small heat shock/alpha-crystallin protein from encysted Artemia embryos suppresses tubulin denaturation. Cell Stress Chaperones 2003; 8: 183–93.
   Google Scholar
• Atomi Y, Fujita Y, Ohto E, Tanaka M, Sakurai T, Katayama E. Role of aB-crystallin for cytoskeleton tubulin/microtubule: to keep dynamic property in muscle and glioma cells. Proc 1st Int Cong Stress Responses Biol Med 2003; Quebec City, Canada, 42.
   Google Scholar
• Wickstrom E. Prospects for ant isense nucleic acid therapy of cancer and AIDS. New York: Wiley-Liss, Inc, 1991.
   Google Scholar
• Murray JAH. Antisense RNA and DNA. New York: Wiley-Liss, Inc, 1992.
   Google Scholar
• Crooke ST, Lebleu B. Antisense research and applications. Boca Raton FL: CRC Press, 1993.
   Google Scholar
• Akhtar S. Delivery Strategies for Antisense Oligonucleotide Therapeutics. Boca Raton FL: CRC Press, 1995.
   Google Scholar
• Wickstrom E, Tyson FL. Differential oligonucleotide activity in cell culture versus mouse models. Ciba Found Symp 1997; 209: 124–37.
   PubMedGoogle Scholar
• Agrawal S. Oligonucleotide therapeutic approach: Near clinical development. New York: Humana Press, 1996.
   Google Scholar
• Smith JB, Wickstrom E. Antisense c-myc and immunostimulatory oligonucleotide inhibition of tumorigenesis in a murine B-cell lymphoma transplant model. J Natl Cancer Inst 1998; 90: 1146–54.
   PubMed Web of Science ®Google Scholar
• Wickstrom E, ed. Clinical trials of genetic therapy with antisense DNA and DNA vectors. New York: Marcel Dekker, Inc., 1998.
   Google Scholar
• Oesterreich S, Weng CN, Qiu M, Hilsenbeck SG, Osborne CK, Fuqua SA. The small heat shock protein hsp27 is correlated with growth and drug resistance in human breast cancer cell lines. Cancer Res 1993; 53: 4443–8.
   PubMed Web of Science ®Google Scholar
• Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochern 1976; 72: 248–54.
   PubMed Web of Science ®Google Scholar
• de Ondarza J, Hootman SR. Confocal microscopic analysis of intracellular pH regulation in isolated guinea pig pancreatic ducts. Am J Physiol 1997; 272: G124–34.
   Google Scholar
• Garrido C, Bruey JM, Fromentin A, Hammann A, Arrigo AP, Solary E. H5P27 inhibits cytochrome c-dependent activation of procaspase-9. FASEB J 1999; 13: 2061–70.
   PubMed Web of Science ®Google Scholar
• Pandey P, Farber R, Nakazawa A, Kumar S, Bharti A, Nalin C, Weichselbaum R, Kufe D, Kharbanda S. Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase-3. Oncogene 2000; 19: 1975–81.
   Google Scholar
• Bruey JM, Ducasse C, Bonniaud P, Ravagnan L, Susin SA, Diaz-Latoud C, Gurbuxani S, Arrigo AP, Kroemer G, Solary E, Garrido C. Hsp27 negatively regulates cell death by interacting with cytochrome c. Nat Cell Biol 2000; 2: 645–52.
   PubMed Web of Science ®Google Scholar
• Concannon CG, Orrenius S, Samali A. Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c. Gene Expr 2001; 9: 195–201.
   Google Scholar
• Concannon CG, Gorman AM, Samali A. On the role of Hsp27 in regulating apoptosis. Apoptosis 2002; 8: 61–70.
   Google Scholar
• LaCasse EC, Baird S, Korneluk RG, MacKenzie AE. The inhibitors of apoptosis (IAPs) and their emerging role in cancer. Oncogene 1998; 17: 3247–59.
   PubMed Web of Science ®Google Scholar
• Jaattela M. Heat shock proteins as cellular lifeguards. Ann Med 1999; 31: 261–71.
   PubMed Web of Science ®Google Scholar
• Cande C, Cohen I, Daugas E, Ravagnan L, Larochette N, Zamzami N, Kroemer G. Apoptosis-inducing factor (AIF): a novel caspase-independent death effector released from mitochondria. Biochirnie 2002; 84: 215–22.
   Google Scholar
• Saleh A, Srinivasula SM, Balkir L, Robbins PD, Alnemri ES. Negative regulation of the Apaf-1 apoptosome by Hsp70. Nature Cell Biol 2000; 21: 476–83.
   Google Scholar
• Morimoto RI. Heat shock: the role of transient inducible responses in cell damage, transformation, and differentiation. Cancer Cells 1991; 3: 295–301.
   PubMed Web of Science ®Google Scholar
• Fuller KJ, Issels RD, Slosman DO, Guillet JG, Soussi T, Polla BS. Cancer and the heat shock response. Eur J Cancer 1994; 30A: 1884–91.
   PubMed Web of Science ®Google Scholar
• Coss RA, Storck CW, Wachsberger PR, Reilly J, Leeper DB, Berd D, Wahl ML. Acute extracellular acidification reduces intracellular pH, 42°C-induction of heat shock proteins and clonal survival of human melanoma cells grown at pH 6.7. Int J Hypertherrnia 2004; 20: 93–106.
   Google Scholar
• Ciocca DR, Oesterreich S, Chamness GC, McGuire WL, Fuqua SA. Biological and clinical implications of heat shock protein 27,000 (Hsp27): a review. J Natl Cancer Inst 1993; 85: 1558–70.
   Google Scholar
• Burd R, Lavorgna SN, Daskalakis C, Wachsberger PR, Wahl ML, Biaglow JE, Stevens CW, Leeper DB. Tumor oxygenation and acidification are increased in melanoma xenografts after exposure to hyperglycemia and meta-iodo-benzylguanidine. Radiat Res 2003; 159: 328–35.
   PubMed Web of Science ®Google Scholar
• Coss RA, Storck CW, Daskalakis C, Berd D, Wahl ML. Intracellular acidification abrogates the heat shock response and compromises survival of human melanoma cells. Mol Cancer Ther 2003; 2: 383–8.
   Google Scholar