nach oben

Translational Stroke Research

Erschienen in:

01.12.2013 | Original Article

MicroRNAs Regulate the Chaperone Network in Cerebral Ischemia

verfasst von: Yi-Bing Ouyang, Rona G. Giffard

Erschienen in: Translational Stroke Research | Ausgabe 6/2013

Einloggen, um Zugang zu erhalten

Abstract

The highly evolutionarily conserved 70 kDa heat shock protein (HSP70) family was first understood for its role in protein folding and response to stress. Subsequently, additional functions have been identified for it in regulation of organelle interaction, of the inflammatory response, and of cell death and survival. Overexpression of HSP70 family members is associated with increased resistance to and improved recovery from cerebral ischemia. MicroRNAs (miRNAs) are important posttranscriptional regulators that interact with multiple target messenger RNAs (mRNA) coordinately regulating target genes, including chaperones. The members of the HSP70 family are now appreciated to work together as networks to facilitate organelle communication and regulate inflammatory signaling and cell survival after cerebral ischemia. This review will focus on the new concept of the role of the chaperone network in the organelle network and its novel regulation by miRNA.

Ouyang Y-B et al. microRNAs: innovative targets for cerebral ischemia and stroke. Curr Drug Targets. 2013;14(1):90–101.PubMed

Ouyang Y-B et al. Selective dysfunction of hippocampal CA1 astrocytes contributes to delayed neuronal damage after transient forebrain ischemia. J Neurosci. 2007;27(16):4253–60.PubMed

Xu L et al. Astrocyte targeted overexpression of Hsp72 or SOD2 reduces neuronal vulnerability to forebrain ischemia. Glia. 2010;58(9):1042–9.PubMed

Okuyama S et al. Anti-inflammatory and neuroprotective effects of auraptene, a citrus coumarin, following cerebral global ischemia in mice. Eur J Pharmacol. 2013;699(1–3):118–23.PubMed

Xiong X et al. Increased brain injury and worsened neurological outcome in interleukin-4 knockout mice after transient focal cerebral ischemia. Stroke. 2011;42(7):2026–32.PubMed

Giffard RG et al. Regulation of apoptotic and inflammatory cell signaling in cerebral ischemia: the complex roles of heat shock protein 70. Anesthesiology. 2008;109(2):339–48. doi:10.1097/ALN.0b013e31817f4ce0.PubMed

Ouyang Y-B et al. Overexpressing GRP78 influences Ca²⁺ handling and function of mitochondria in astrocytes after ischemia-like stress. Mitochondrion. 2011;11(2):279–86.PubMed

Ouyang Y-B, Giffard R. ER–mitochondria crosstalk during cerebral ischemia: molecular chaperones and ER–mitochondrial calcium transfer. Int J Cell Biol. 2012;2012:493934.PubMed

Mayer MP, Bukau B. Hsp70 chaperone systems: diversity of cellular functions and mechanism of action. Biol Chem. 1998;379(3):261–8.PubMed

10.

Kiang JG, Tsokos GC. Heat shock protein 70 kDa: molecular biology, biochemistry, and physiology. Pharmacol Ther. 1998;80(2):183–201.PubMed

11.

Hoehn B et al. Overexpression of HSP72 after induction of experimental stroke protects neurons from ischemic damage. J Cereb Blood Flow Metab. 2001;21(11):1303–9.PubMed

12.

Lee WC et al. Heat shock protein 72 overexpression protects against hyperthermia, circulatory shock, and cerebral ischemia during heatstroke. J Appl Physiol. 2006;100(6):2073–82.PubMed

13.

Plumier JC et al. Transgenic mice expressing the human inducible Hsp70 have hippocampal neurons resistant to ischemic injury. Cell Stress Chaperones. 1997;2(3):162–7.PubMed

14.

Rajdev S et al. Mice overexpressing rat heat shock protein 70 are protected against cerebral infarction. Ann Neurol. 2000;47(6):782–91.PubMed

15.

van der Weerd L et al. Neuroprotective effects of HSP70 overexpression after cerebral ischaemia—an MRI study. Exp Neurol. 2005;195(1):257–66.PubMed

16.

Xu L et al. Overexpression of mitochondrial Hsp70/Hsp75 in rat brain protects mitochondria, reduces oxidative stress, and protects from focal ischemia. J Cereb Blood Flow Metab. 2009;29(2):365–74.PubMed

17.

Yenari MA et al. Gene therapy with HSP72 is neuroprotective in rat models of stroke and epilepsy. Ann Neurol. 1998;44(4):584–91.PubMed

18.

Zheng Z et al. Anti-inflammatory effects of the 70kDa heat shock protein in experimental stroke. J Cereb Blood Flow Metab. 2008;28(1):53–63.PubMed

19.

Ouyang Y-B et al. Overexpression of inducible heat shock protein 70 and its mutants in astrocytes is associated with maintenance of mitochondrial physiology during glucose deprivation stress. Cell Stress Chaperones. 2006;11(2):180–6.PubMed

20.

Sun Y et al. The carboxyl-terminal domain of inducible Hsp70 protects from ischemic injury in vivo and in vitro. J Cereb Blood Flow Metab. 2005;26(7):937–50.PubMed

21.

Xu L et al. Heat shock protein 72 (Hsp72) improves long term recovery after focal cerebral ischemia in mice. Neurosci Lett. 2011;488(3):279–82.PubMed

22.

Barreto GE et al. Effects of heat shock protein 72 (Hsp72) on evolution of astrocyte activation following stroke in the mouse. Exp Neurol. 2012;238(2):284–96.PubMed

23.

Giffard RG et al. Chaperones, protein aggregation, and brain protection from hypoxic/ischemic injury. J Exp Biol. 2004;207(18):3213–20.PubMed

24.

Giffard RG, Yenari MA. Many mechanisms for Hsp70 protection from cerebral ischemia. J Neurosurg Anesthesiol. 2004;16(1):53–61.PubMed

25.

Kelly S et al. Gene transfer of HSP72 protects cornu ammonis 1 region of the hippocampus neurons from global ischemia: influence of Bcl-2. Ann Neurol. 2002;52(2):160–7.PubMed

26.

Yenari MA et al. Antiapoptotic and anti-inflammatory mechanisms of heat-shock protein protection. Ann N Y Acad Sci. 2005;1053(1):74–83.PubMed

27.

Sheppard P et al. Quantitative characterization and analysis of the dynamic NF-kB response in microglia. BMC Bioinforma. 2011;12:276.

28.

Wadhwa R, Taira K, Kaul SC. An Hsp70 family chaperone, mortalin/mthsp70/PBP74/Grp75: what, when, and where? Cell Stress Chaperones. 2002;7(3):309–16.PubMed

29.

Massa SM et al. Cloning of rat grp75, an hsp70-family member, and its expression in normal and ischemic brain. J Neurosci Res. 1995;40(6):807–19.PubMed

30.

Voloboueva LA et al. Overexpression of mitochondrial Hsp70/Hsp75 protects astrocytes against ischemic injury in vitro. J Cereb Blood Flow Metab. 2008;28(5):1009–16.PubMed

31.

White R, Ouyang Y-B, Giffard R. Hsp75/mortalin and protection from ischemic brain injury. In: Kaul SC, Wadhwa R, editors. Mortalin biology: life, stress and death. Amsterdam: Springer; 2012. p. 179–90.

32.

Zhang L-H et al. Association of elevated GRP78 expression with increased astrocytoma malignancy via Akt and ERK pathways. Brain Research. 2011;1371:23–31.PubMed

33.

Pfaffenbach KT, Lee AS. The critical role of GRP78 in physiologic and pathologic stress. Curr Opin Cell Biol. 2011;23(2):150–6.PubMed

34.

Wang M et al. Role of the unfolded protein response regulator GRP78/BiP in development, cancer, and neurological disorders. Antioxid Redox Signal. 2009;11(9):2307–16.PubMed

35.

Gonzalez Gronow M et al. GRP78: a multifunctional receptor on the cell surface. Antioxid Redox Signal. 2009;11(9):2299–306.PubMed

36.

Wang M et al. Essential role of the unfolded protein response regulator GRP78/BiP in protection from neuronal apoptosis. Cell Death Differ. 2010;17(3):488–98.PubMed

37.

Li J et al. The unfolded protein response regulator GRP78/BiP is required for endoplasmic reticulum integrity and stress-induced autophagy in mammalian cells. Cell Death Differ. 2008;15(9):1460–71.PubMed

38.

Oida Y et al. Induction of BiP, an ER-resident protein, prevents the neuronal death induced by transient forebrain ischemia in gerbil. Brain Res. 2008;1208:217–24.PubMed

39.

Kudo T et al. A molecular chaperone inducer protects neurons from ER stress. Cell Death Differ. 2008;15(2):364–75.PubMed

40.

Ouyang Y-B et al. miR-181 regulates GRP78 and influences outcome from cerebral ischemia in vitro and in vivo. Neurobiol Dis. 2012;45(1):555–63.PubMed

41.

Barabasi A-L, Oltvai ZN. Network biology: understanding the cell’s functional organization. Nat Rev Genet. 2004;5(2):101–13.PubMed

42.

Csermely P. Strong links are important, but weak links stabilize them. Trends Biochem Sci. 2004;29(7):331–4.PubMed

43.

Sőti C et al. Molecular chaperones as regulatory elements of cellular networks. Curr Opin Cell Biol. 2005;17(2):210–5.PubMed

44.

Csermely P, Vigh L, editors. Molecular aspects of the stress response: chaperones, membranes and networks. Berlin: Springer; 2007.

45.

Brostrom MA, Brostrom CO. Calcium dynamics and endoplasmic reticular function in the regulation of protein synthesis: implications for cell growth and adaptability. Cell Calcium. 2003;34(4–5):345–63.PubMed

46.

Sitia R, Braakman I. Quality control in the endoplasmic reticulum protein factory. Nature. 2003;426(6968):891–4.PubMed

47.

Wang H-J et al. Calcium regulates the association between mitochondria and a smooth subdomain of the endoplasmic reticulum. J Cell Biol. 2000;150(6):1489–98.PubMed

48.

Deniaud A et al. Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis. Oncogene. 2007;27(3):285–99.PubMed

49.

Hetz C. ER stress signaling and the BCL-2 family of proteins: from adaptation to irreversible cellular damage. Antioxid Redox Signal. 2007;9(12):2345–55.PubMed

50.

Hom JR et al. Thapsigargin induces biphasic fragmentation of mitochondria through calcium-mediated mitochondrial fission and apoptosis. J Cell Physiol. 2007;212(2):498–508.PubMed

51.

Scorrano L et al. BAX and BAK regulation of endoplasmic reticulum Ca²⁺: a control point for apoptosis. Science. 2003;300(5616):135–9.PubMed

52.

Beal MF. Energetics in the pathogenesis of neurodegenerative diseases. Trends Neurosci. 2000;23(7):298–304.PubMed

53.

Kroemer G, Reed JC. Mitochondrial control of cell death. Nat Med. 2000;6(5):513–9.PubMed

54.

Murphy KM, Streips UN, Lock RB. Bax membrane insertion during Fas(CD95)-induced apoptosis precedes cytochrome c release and is inhibited by Bcl-2. Oncogene. 1999;18(44):5991–9.PubMed

55.

Ravagnan L, Roumier T, Kroemer G. Mitochondria, the killer organelles and their weapons. J Cell Physiol. 2002;192(2):131–7.PubMed

56.

Voloboueva LA, Giffard RG. Inflammation, mitochondria, and the inhibition of adult neurogenesis. J Neurosci Res. 2011;89(12):1989–96.PubMed

57.

Voloboueva LA et al. Mitochondrial protection attenuates inflammation-induced impairment of neurogenesis in vitro and in vivo. J Neurosci. 2010;30(37):12242–51.PubMed

58.

Kirichok Y, Krapivinsky G, Clapham DE. The mitochondrial calcium uniporter is a highly selective ion channel. Nature. 2004;427(6972):360–4.PubMed

59.

Nicholls DG, Budd SL. Mitochondria and neuronal survival. Physiol Rev. 2000;80(1):315–60.PubMed

60.

Bernardi P. Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol Rev. 1999;79(4):1127–55.PubMed

61.

Rizzuto R, Pozzan T. Microdomains of intracellular Ca²⁺: molecular determinants and functional consequences. Physiol Rev. 2006;86(1):369–408.PubMed

62.

Camici O, Corazzi L. Phosphatidylserine translocation into brain mitochondria: involvement of a fusogenic protein associated with mitochondrial membranes. Mol Cell Biochem. 1997;175(1–2):71–80.PubMed

63.

Colombini M. VDAC: the channel at the interface between mitochondria and the cytosol. Mol Cell Biochem. 2004;256–257(1–2):107–15.PubMed

64.

Patterson R, Boehning D, Snyder S. Inositol 1,4,5-trisphosphate receptors as signal integrators. Annual Rev Biochem. 2004;73:437–65.

65.

Rostovtseva T, Tan W, Colombini M. On the role of VDAC in apoptosis: fact and fiction. J Bioenerg Biomembr. 2005;37(3):129–42.PubMed

66.

Vyssokikh M, Brdiczka D. VDAC and peripheral channelling complexes in health and disease. Mol Cell Biochem. 2004;256–257(1–2):117–26.PubMed

67.

Rizzuto R et al. Microdomains with high Ca²⁺ close to IP3-sensitive channels that are sensed by neighboring mitochondria. Science. 1993;262(5134):744–7.PubMed

68.

Rizzuto R et al. Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca²⁺ responses. Science. 1998;280(5370):1763–6.PubMed

69.

Szabadkai G et al. Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca²⁺ channels. J Cell Biol. 2006;175(6):901–11.PubMed

70.

Liu Y et al. Effect of GRP75/mthsp70/PBP74/mortalin overexpression on intracellular ATP level, mitochondrial membrane potential and ROS accumulation following glucose deprivation in PC12 cells. Mol Cell Biochem. 2005;268(1–2):45–51.PubMed

71.

Hayashi T, Su T-P. Sigma-1 receptor chaperones at the ER–mitochondrion interface regulate Ca²⁺ signaling and cell survival. Cell. 2007;131(3):596–610.PubMed

72.

Sun F-C et al. Localization of GRP78 to mitochondria under the unfolded protein response. Biochem J. 2006;396(1):31–9.PubMed

73.

Szabadkai G, Rizzuto R. Chaperones as parts of organelle networks. In: Csermely P, Vigh L, editors. Molecular aspects of the stress response: chaperones, membranes and networks. Berlin: Springer; 2007.

74.

Foyouzi-Youssefi R et al. Bcl-2 decreases the free Ca2+ concentration within the endoplasmic reticulum. Proc Natl Acad Sci. 2000;97(11):5723–8.PubMed

75.

Ouyang Y-B et al. miR-181 targets multiple Bcl-2 family members and influences apoptosis and mitochondrial function in astrocytes. Mitochondrion. 2012;12(2):213–9.PubMed

76.

Kim N, Kim J, Yenari M. Anti-inflammatory properties and pharmacological induction of Hsp70 after brain injury. Inflammopharmacology. 2012;20(3):177–85.PubMed

77.

Chamorro A et al. The immunology of acute stroke. Nat Rev Neurol. 2012;8(7):401–10.PubMed

78.

Ouyang YB. Inflammation and stroke. Neurosci Lett. 2013;548:1–3.PubMed

79.

Iadecola C, Anrather J. The immunology of stroke: from mechanisms to translation. Nat Med. 2011;17(7):796–808.PubMed

80.

Kamel H, Iadecola C. Brain–immune interactions and ischemic stroke: clinical implications. Arch Neurol. 2012;69(5):576–81.PubMed

81.

Tarkowski E et al. Early intrathecal production of interleukin-6 predicts the size of brain lesion in stroke. Stroke. 1995;26(8):1393–8.PubMed

82.

Beamer NB et al. Interleukin-6 and interleukin-1 receptor antagonist in acute stroke. Ann Neurol. 1995;37(6):800–5.PubMed

83.

Fassbender K et al. Proinflammatory cytokines in serum of patients with acute cerebral ischemia: kinetics of secretion and relation to the extent of brain damage and outcome of disease. J Neurol Sci. 1994;122(2):135–9.PubMed

84.

Chamorro Á, Urra X, Planas AM. Infection after acute ischemic stroke: a manifestation of brain-induced immunodepression. Stroke. 2007;38(3):1097–103.PubMed

85.

Vila N et al. Proinflammatory cytokines and early neurological worsening in ischemic stroke. Stroke. 2000;31(10):2325–9.PubMed

86.

Vila N et al. Levels of anti-inflammatory cytokines and neurological worsening in acute ischemic stroke. Stroke. 2003;34(3):671–5.PubMed

87.

Andersson U, Tracey KJ. Neural reflexes in inflammation and immunity. J Exp Med. 2012;209(6):1057–68.PubMed

88.

Lafargue M et al. Stroke-induced activation of the α7 nicotinic receptor increases Pseudomonas aeruginosa lung injury. FASEB J. 2012;26(7):2919–29.PubMed

89.

del Zoppo GJ et al. Microglial activation and matrix protease generation during focal cerebral ischemia. Stroke. 2007;38(2):646–51.PubMed

90.

Pekny M, Nilsson M. Astrocyte activation and reactive gliosis. Glia. 2005;50(4):427–34.PubMed

91.

Rivest S. Regulation of innate immune responses in the brain. Nat Rev Immunol. 2009;9(6):429–39.PubMed

92.

Sofroniew M, Vinters H. Astrocytes: biology and pathology. Acta Neuropathologica. 2010;119(1):7–35.PubMed

93.

Wang Q, Tang XN, Yenari MA. The inflammatory response in stroke. J Neuroimmunol. 2007;184(1–2):53–68.PubMed

94.

Zheng Z, Yenari MA. Post-ischemic inflammation: molecular mechanisms and therapeutic implications. Neurol Res. 2004;26(8):884–92.PubMed

95.

Trendelenburg G. Acute neurodegeneration and the inflammasome: central processor for danger signals and the inflammatory response? J Cereb Blood Flow Metab. 2008;28(5):867–81.PubMed

96.

Hyakkoku K et al. Toll-like receptor 4 (TLR4), but not TLR3 or TLR9, knock-out mice have neuroprotective effects against focal cerebral ischemia. Neuroscience. 2010;171(1):258–67.PubMed

97.

Ziegler G et al. TLR2 has a detrimental role in mouse transient focal cerebral ischemia. Biochem Biophys Res Commun. 2007;359(3):574–9.PubMed

98.

Bulua AC et al. Mitochondrial reactive oxygen species promote production of proinflammatory cytokines and are elevated in TNFR1-associated periodic syndrome (TRAPS). J Exp Med. 2011;208(3):519–33.PubMed

99.

Naik E, Dixit VM. Mitochondrial reactive oxygen species drive proinflammatory cytokine production. J Exp Med. 2011;208(3):417–20.PubMed

100.

Nakahira K et al. Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome. Nat Immunol. 2011;12(3):222–30.PubMed

101.

Zhou R et al. A role for mitochondria in NLRP3 inflammasome activation. Nature. 2011;469(7329):221–5.PubMed

102.

Ortego M et al. HMG-CoA reductase inhibitors reduce I[kappa]B kinase activity induced by oxidative stress in monocytes and vascular smooth muscle cells. J Cardiovasc Pharmacol. 2005;45(5):468–75.PubMed

103.

Song YS, Lee Y-S, Chan PH. Oxidative stress transiently decreases the IKK complex (IKK[alpha], [beta], and [gamma]), an upstream component of NF-[kappa]B signaling, after transient focal cerebral ischemia in mice. J Cereb Blood Flow Metab. 2005;25(10):1301–11.PubMed

104.

Hoffmann A, Baltimore D. Circuitry of nuclear factor κB signaling. Immunol Rev. 2006;210(1):171–86.PubMed

105.

Harari OA, Liao JK. NF-κB and innate immunity in ischemic stroke. Ann N Y Acad Sci. 2010;1207(1):32–40.PubMed

106.

Ghosh S, Karin M. Missing pieces in the NF-κB puzzle. Cell. 2002;109(2):S81–96. Supplement 1.PubMed

107.

Hayden MS, Ghosh S. Shared principles in NF-κB signaling. Cell. 2008;132(3):344–62.PubMed

108.

Jones Q et al. Heat shock proteins protect against ischemia and inflammation through multiple mechanisms. Inflamm Allergy Drug Targets. 2011;10(4):247–59.PubMed

109.

Asea A. Heat shock proteins and toll-like receptors. In: Bauer S, Hartmann G, editors. Toll-like receptors (TLRs) and innate immunity. Berlin Heidelberg: Springer; 2008. p. 111–27.

110.

Feinstein DL et al. Heat shock protein 70 suppresses astroglial-inducible nitric-oxide synthase expression by decreasing NFκB activation. J Biol Chem. 1996;271(30):17724–32.PubMed

111.

Ran R et al. Hsp70 promotes TNF-mediated apoptosis by binding IKKγ and impairing NF-κB survival signaling. Genes Dev. 2004;18(12):1466–81.PubMed

112.

Voloboueva LA et al. Inflammatory response of microglial BV-2 cells includes a glycolytic shift and is modulated by mitochondrial glucose-regulated protein 75/mortalin. FEBS Lett. 2013;587(6):756–62.PubMed

113.

Nareika A et al. Sodium lactate increases LPS-stimulated MMP and cytokine expression in U937 histiocytes by enhancing AP-1 and NF-κB transcriptional activities. Am J Physiol Endocrinol Metab. 2005;289(4):E534–42.PubMed

114.

Morito, D. and K. Nagata. ER stress proteins in autoimmune and inflammatory diseases. Front Immunol., 2012;3:48.

115.

Bläß S et al. The stress protein BiP is overexpressed and is a major B and T cell target in rheumatoid arthritis. Arthritis Rheum. 2001;44(4):761–71.PubMed

116.

Bodman–Smith MD et al. BiP, a putative autoantigen in rheumatoid arthritis, stimulates IL–10–producing CD8–positive T cells from normal individuals. Rheumatology. 2003;42(5):637–44.PubMed

117.

Brownlie RJ et al. Treatment of murine collagen-induced arthritis by the stress protein BiP via interleukin-4-producing regulatory T cells: a novel function for an ancient protein. Arthritis Rheum. 2006;54(3):854–63.PubMed

118.

Corrigall VM et al. Inhibition of antigen-presenting cell function and stimulation of human peripheral blood mononuclear cells to express an antiinflammatory cytokine profile by the stress protein BiP: relevance to the treatment of inflammatory arthritis. Arthritis Rheum. 2004;50(4):1164–71.PubMed

119.

Corrigall VM et al. The human endoplasmic reticulum molecular chaperone BiP is an autoantigen for rheumatoid arthritis and prevents the induction of experimental arthritis. J Immunol. 2001;166(3):1492–8.PubMed

120.

Panayi GS, Corrigall VM. BiP regulates autoimmune inflammation and tissue damage. Autoimmun Rev. 2006;5(2):140–2.PubMed

121.

Kitamura M. Biphasic, bidirectional regulation of NF-kappaB by endoplasmic reticulum stress. Antioxid Redox Signal. 2009;11(9):2353–64.PubMed

122.

Okamura M et al. Suppression of cytokine responses by indomethacin in podocytes: a mechanism through induction of unfolded protein response. AmJ Physiol Renal Physiol. 2008;295(5):F1495–503.

123.

Kernagis DN, Laskowitz DT. Evolving role of biomarkers in acute cerebrovascular disease. Ann Neurol. 2012;71(3):289–303.PubMed

124.

Chopp M, Li Y. Apoptosis in focal cerebral ischemia. Acta Neurochir Suppl. 1996;66:21–6.PubMed

125.

Mattson MP, Culmsee C, Yu ZF. Apoptotic and antiapoptotic mechanisms in stroke. Cell Tissue Res. 2000;301(1):173–87.PubMed

126.

DeGracia D et al. Translation arrest and ribonomics in post-ischemic brain: layers and layers of players. J Neurochem. 2008;106(6):2288–301.PubMed

127.

DeGracia DJ, Hu BR. Irreversible translation arrest in the reperfused brain. J Cereb Blood Flow Metab. 2007;27(5):875–93.PubMed

128.

Sharp FR et al. HSP70 heat shock gene regulation during ischemia. Stroke. 1993;24(12 Suppl):I72–5.PubMed

129.

Vass K, Welch WJ, Nowak TS. Localization of 70-kDa stress protein induction in gerbil brain after ischemia. Acta Neuropathol. 1988;77(2):128–35.PubMed

130.

Kinouchi H et al. Induction of 70-kDa heat shock protein and hsp70 mRNA following transient focal cerebral ischemia in the rat. J Cereb Blood Flow Metab. 1993;13(1):105–15.PubMed

131.

Kinouchi H et al. Induction of heat shock hsp70 mRNA and HSP70 kDa protein in neurons in the ‘penumbra’ following focal cerebral ischemia in the rat. Brain Research. 1993;619(1–2):334–8.PubMed

132.

Nowak TS. Localization of 70 kDa stress protein mRNA induction in gerbil brain after ischemia. J Cereb Blood Flow Metab. 1991;11(3):432–9.PubMed

133.

Duan S-r et al. Ischemia induces endoplasmic reticulum stress and cell apoptosis in human brain. Neurosci Lett. 2010;475(3):132–5.PubMed

134.

Jeyaseelan K, Lim KY, Armugam A. MicroRNA expression in the blood and brain of rats subjected to transient focal ischemia by middle cerebral artery occlusion. Stroke. 2008;39(3):959–66.PubMed

135.

Liu D-Z et al. Brain and blood microRNA expression profiling of ischemic stroke, intracerebral hemorrhage, and kainate seizures. J Cereb Blood Flow Metab. 2010;30(1):92–101.PubMed

136.

Tan K et al. Expression profile of microRNAs in young stroke patients. PLoS ONE. 2009;4(11):e7689.PubMed

137.

Ren X-P et al. MicroRNA-320 is involved in the regulation of cardiac ischemia/reperfusion injury by targeting heat-shock protein 20. Circulation. 2009;119(17):2357–66.PubMed

138.

Yin C, Salloum FN, Kukreja RC. A novel role of microRNA in late preconditioning: upregulation of endothelial nitric oxide synthase and heat shock protein 70. Circ Res. 2009;104(5):572–5.PubMed

139.

Shan Z-X et al. Upregulated expression of miR-1/miR-206 in a rat model of myocardial infarction. Biochem Biophys Res Commun. 2009;381(4):597–601.PubMed

140.

Tang Y et al. MicroRNA-1 regulates cardiomyocyte apoptosis by targeting Bcl-2. Int Hear J. 2009;50(3):377–87.

141.

Yang B et al. The muscle-specific microRNA miR-1 regulates cardiac arrhythmogenic potential by targeting GJA1 and KCNJ2. Nat Med. 2007;13(4):486–91.PubMed

142.

Xu C et al. The muscle-specific microRNAs miR-1 and miR-133 produce opposing effects on apoptosis by targeting HSP60, HSP70 and caspase-9 in cardiomyocytes. J Cell Sci. 2007;120(17):3045–52.PubMed

143.

Lee S-T et al. MicroRNAs induced during ischemic preconditioning. Stroke. 2010;41(8):1646–51.PubMed

144.

Magenta A et al. miR-200c is upregulated by oxidative stress and induces endothelial cell apoptosis and senescence via ZEB1 inhibition. Cell Death Differ. 2011;18(10):1628–39.PubMed

Titel: MicroRNAs Regulate the Chaperone Network in Cerebral Ischemia
verfasst von: Yi-Bing Ouyang
Rona G. Giffard
Publikationsdatum: 01.12.2013
Verlag: Springer US
Erschienen in: Translational Stroke Research / Ausgabe 6/2013
Print ISSN: 1868-4483
Elektronische ISSN: 1868-601X
DOI: https://doi.org/10.1007/s12975-013-0280-3

Leitlinien kompakt für die Neurologie

Mit medbee Pocketcards sicher entscheiden.

^{Seit 2022 gehört die medbee GmbH zum Springer Medizin Verlag}

Kostenlos registrieren

Neu im Fachgebiet Neurologie

Hirnblutung unter DOAK und VKA ähnlich bedrohlich

17.05.2024 Direkte orale Antikoagulanzien Nachrichten

Kommt es zu einer nichttraumatischen Hirnblutung, spielt es keine große Rolle, ob die Betroffenen zuvor direkt wirksame orale Antikoagulanzien oder Marcumar bekommen haben: Die Prognose ist ähnlich schlecht.

Was nützt die Kraniektomie bei schwerer tiefer Hirnblutung?

17.05.2024 Hirnblutung Nachrichten

Eine Studie zum Nutzen der druckentlastenden Kraniektomie nach schwerer tiefer supratentorieller Hirnblutung deutet einen Nutzen der Operation an. Für überlebende Patienten ist das dennoch nur eine bedingt gute Nachricht.

Thrombektomie auch bei großen Infarkten von Vorteil

16.05.2024 Ischämischer Schlaganfall Nachrichten

Auch ein sehr ausgedehnter ischämischer Schlaganfall scheint an sich kein Grund zu sein, von einer mechanischen Thrombektomie abzusehen. Dafür spricht die LASTE-Studie, an der Patienten und Patientinnen mit einem ASPECTS von maximal 5 beteiligt waren.

Schwindelursache: Massagepistole lässt Otholiten tanzen

14.05.2024 Benigner Lagerungsschwindel Nachrichten

Wenn jüngere Menschen über ständig rezidivierenden Lagerungsschwindel klagen, könnte eine Massagepistole der Auslöser sein. In JAMA Otolaryngology warnt ein Team vor der Anwendung hochpotenter Geräte im Bereich des Nackens.

Update Neurologie

Bestellen Sie unseren Fach-Newsletter und bleiben Sie gut informiert.

Newsletter bestellen

Die Highlights vom Kongress des American College of Cardiology 2024

Springer Medizin

Abstract

Bitte loggen Sie sich ein, um Zugang zu diesem Inhalt zu erhalten

Weitere Artikel der Ausgabe 6/2013

Heat Shock Proteins in the Brain: Role of Hsp70, Hsp 27, and HO-1 (Hsp32) and Their Therapeutic Potential

Augmentation of Normal and Glutamate-Impaired Neuronal Respiratory Capacity by Exogenous Alternative Biofuels

mRNA Redistribution during Permanent Focal Cerebral Ischemia

Lysosomal Membrane Permeabilization as a Key Player in Brain Ischemic Cell Death: a “Lysosomocentric” Hypothesis for Ischemic Brain Damage

Fission and Fusion of the Neuronal Endoplasmic Reticulum