Login Register Cart 0
Generic placeholder image

Current Molecular Medicine

Editor-in-Chief

ISSN (Print): 1566-5240
ISSN (Online): 1875-5666

Back
Journal Home About Journal Editorial Board Journal Insight Current Issue Volumes/Issues
Subscribe Translate in Chinese
Research Article

Examination of the Role of miR-23a in the Development of Thermotolerance

Author(s): Rabih Roufayel and Seifedine Kadry*

Volume 20, Issue 3, 2020

Page: [194 - 201] Pages: 8

DOI: 10.2174/1566524019666191021111028

Price: $65

Abstract

Background: Thermotolerance is an acquired state of increased heat resistance that occurs following exposure to non-lethal proteotoxic stress. A large body of evidences implicates that molecular chaperon members belonging to the heat shock protein family could be acting as potential mediators of the thermotolerant state.

Objective: Recent evidence has demonstrated heat shock proteins HSP90, HSP70 and HSP27 have inhibited heat-induced cell death by intervening at various steps in stressinduced apoptotic pathways. Previous studies have shown that HSP70 prevented heatinduced apoptosis by preventing the NOXA dependent decrease in MCL-1 levels leading to both BAX activation and cytochrome c release from mitochondria. We have also demonstrated that HSP70 expressing cells have enhanced levels of miR-23a prevent heat-induced increase in NOXA levels and suppress apoptosis.

Methods: Stably transfected cell lines expressing either a control shRNA or a miR-23a targeting shRNA are quantified using both RT-PCR and semi-quantitative RT-PCR to determine the effect of different hyperthermic exposure treatment on miR-23a and Noxa mRNA expression levels.

Results: This study shows that thermotolerant-induced pre-heat shock treatment is capable of increasing miR-23a levels. Furthermore, stable cell clones expressing a miR- 23a targeting shRNA having reduced miR-23a levels are incapable of developing a thermotolerance state, leading to apoptosis.

Conclusion: These results demonstrate the novel finding that miR-23a is an important factor in the development of the thermotolerant state.

Keywords: Thermotolerance, apoptosis, heat shock protein, hyperthermia, HSP70, NOXA, miR-23ª.

« Previous Next »
[1]
Raaphorst GP, Romano SL, Mitchell JB, Bedford JS, Dewey WC. Intrinsic differences in heat and/or X-ray sensitivity of seven mammalian cell lines cultured and treated under identical conditions. Cancer Res 1979; 39(2 Pt 1): 396-401.
[PMID: 761211]
[2]
Bauer KD, Henle KJ. Arrhenius analysis of heat survival curves from normal and thermotolerant CHO cells. Radiat Res 1979; 78(2): 251-63.
[http://dx.doi.org/10.2307/3575042] [PMID: 451155]
[3]
Dewey WC, Hopwood LE, Sapareto SA, Gerweck LE. Cellular responses to combinations of hyperthermia and radiation. Radiology 1977; 123(2): 463-74.
[http://dx.doi.org/10.1148/123.2.463] [PMID: 322205]
[4]
Liu RY, Li X, Li L, Li GC. Expression of human hsp70 in rat fibroblasts enhances cell survival and facilitates recovery from translational and transcriptional inhibition following heat shock. Cancer Res 1992; 52(13): 3667-73.
[PMID: 1377596]
[5]
Gerner EW, Schneider MJ. Induced thermal resistance in HeLa cells. Nature 1975; 256(5517): 500-2.
[http://dx.doi.org/10.1038/256500a0] [PMID: 1160994]
[6]
Palzer RJ, Heidelberger C. Studies on the quantitative biology of hyperthermic killing of HeLa cells. Cancer Res 1973; 33(2): 415-21.
[PMID: 4688889]
[7]
Sapareto SA, Hopwood LE, Dewey WC, Raju MR, Gray JW. Effects of hyperthermia on survival and progression of Chinese hamster ovary cells. Cancer Res 1978; 38(2): 393-400.
[PMID: 563767]
[8]
Li GC, Werb Z. Correlation between synthesis of heat-shock proteins and development of thermotolerance in chinesehamster fibroblasts. P Natl Acad Sci-Biol 1982; 79: 3218-22.
[9]
Nussenzweig ABP, Li GC. The role of heat shock proteins in thermotolerance Advances in Molecular and Cell Biology. JAI Press 1997; pp. 261-85.
[10]
Landry J, Bernier D, Chrétien P, Nicole LM, Tanguay RM, Marceau N. Synthesis and degradation of heat shock proteins during development and decay of thermotolerance. Cancer Res 1982; 42(6): 2457-61.
[PMID: 7074623]
[11]
Subjeck JR, Sciandra JJ, Johnson RJ. Heat shock proteins and thermotolerance; a comparison of induction kinetics. Br J Radiol 1982; 55(656): 579-84.
[http://dx.doi.org/10.1259/0007-1285-55-656-579] [PMID: 7116088]
[12]
Li GC, Hahn GM. Ethanol-induced tolerance to heat and to adriamycin. Nature 1978; 274(5672): 699-701.
[http://dx.doi.org/10.1038/274699a0] [PMID: 673004]
[13]
Johnston RN, Kucey BL. Competitive inhibition of hsp70 gene expression causes thermosensitivity. Science 1988; 242(4885): 1551-4.
[http://dx.doi.org/10.1126/science.3201244] [PMID: 3201244]
[14]
Laszlo A, Li GC. Heat-resistant variants of Chinese hamster fibroblasts altered in expression of heat shock protein. Proc Natl Acad Sci USA 1985; 82(23): 8029-33.
[http://dx.doi.org/10.1073/pnas.82.23.8029] [PMID: 3865213]
[15]
Landry J, Chrétien 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(1): 7-15.
[http://dx.doi.org/10.1083/jcb.109.1.7] [PMID: 2745558]
[16]
Li GC, Li LG, Liu YK, Mak JY, Chen LL, Lee WM. Thermal response of rat fibroblasts stably transfected with the human 70-kDa heat shock protein-encoding gene. Proc Natl Acad Sci USA 1991; 88(5): 1681-5.
[http://dx.doi.org/10.1073/pnas.88.5.1681] [PMID: 1705702]
[17]
Han G, Yang H, Wang Y, et al. Effects of in ovo feeding of L-leucine on amino acids metabolism and heat-shock protein-70, and -90 mRNA expression in heat-exposed chicks. Poult Sci 2019; 98(3): 1243-53.
[http://dx.doi.org/10.3382/ps/pey444] [PMID: 30265371]
[18]
Mosser DD, Caron AW, Bourget L, Denis-Larose C, Massie B. Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis. Mol Cell Biol 1997; 17(9): 5317-27.
[http://dx.doi.org/10.1128/MCB.17.9.5317] [PMID: 9271409]
[19]
Mosser DD, Martin LH. Induced thermotolerance to apoptosis in a human T lymphocyte cell line. J Cell Physiol 1992; 151(3): 561-70.
[http://dx.doi.org/10.1002/jcp.1041510316] [PMID: 1295903]
[20]
Roufayel R, Johnston DS, Mosser DD. The elimination of miR-23a in heat-stressed cells promotes NOXA-induced cell death and is prevented by HSP70. Cell Death Dis 2014; 5e: 1546.
[http://dx.doi.org/10.1038/cddis.2014.484] [PMID: 25429623]
[21]
Uehara Y, Temma K, Kobayashi Y, Irie N, Yamaguchi T. Reduction of thermotolerance by heat shock protein 90 inhibitors in murine erythroleukemia cells. Biol Pharm Bull 2018; 41(9): 1393-400.
[http://dx.doi.org/10.1248/bpb.b18-00190] [PMID: 30175776]
[22]
Roufayel R, Kadry S. Expression of miR-23a by apoptotic regulators in human cancer: A review. Cancer Biol Ther 2017; 18(5): 269-76.
[http://dx.doi.org/10.1080/15384047.2017.1310342] [PMID: 28453394]
[23]
Garzon R, Marcucci G, Croce CM. Targeting microRNAs in cancer: rationale, strategies and challenges. Nat Rev Drug Discov 2010; 9(10): 775-89.
[http://dx.doi.org/10.1038/nrd3179] [PMID: 20885409]
[24]
Lima RT, Busacca S, Almeida GM, Gaudino G, Fennell DA, Vasconcelos MH. MicroRNA regulation of core apoptosis pathways in cancer. Eur J Cancer 2011; 47(2): 163-74.
[http://dx.doi.org/10.1016/j.ejca.2010.11.005] [PMID: 21145728]
[25]
Mosser DD, Morimoto RI. Molecular chaperones and the stress of oncogenesis. Oncogene 2004; 23(16): 2907-18.
[http://dx.doi.org/10.1038/sj.onc.1207529] [PMID: 15077153]

Rights & Permissions Print Cite
Article Metrics
7
1
© 2024 Bentham Science Publishers | Privacy Policy