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Volumn 9, Issue 4, 2004, Pages 369-377

Heat shock treatment protects osmotic stress-induced dysfunction of the blood-brain barrier through preservation of tight junction proteins

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; BRAIN EXTRACT; EVANS BLUE; HEAT SHOCK PROTEIN 72; MANNITOL; OCCLUDIN; PROTEIN ZO1;

EID: 12744273443     PISSN: 13558145     EISSN: None     Source Type: Journal    
DOI: 10.1379/CSC-45R1.1     Document Type: Article
Times cited : (25)

References (41)
  • 2
    • 0032572603 scopus 로고    scopus 로고
    • Stress (heat shock) proteins: Molecular chaperones in cardiovascular biology and disease
    • Benjamin IJ, McMillan DR. 1998. Stress (heat shock) proteins: molecular chaperones in cardiovascular biology and disease. Circ Res 83: 117-132.
    • (1998) Circ Res , vol.83 , pp. 117-132
    • Benjamin, I.J.1    McMillan, D.R.2
  • 3
    • 0033675121 scopus 로고    scopus 로고
    • Attenuation of sepsis-induced apoptosis by heat shock pretreatment in rats
    • Chen HW, Hsu C, Lue SI, Yang RC. 2000. Attenuation of sepsis-induced apoptosis by heat shock pretreatment in rats. Cell Stress Chaperones 5: 188-195.
    • (2000) Cell Stress Chaperones , vol.5 , pp. 188-195
    • Chen, H.W.1    Hsu, C.2    Lue, S.I.3    Yang, R.C.4
  • 4
    • 0034781332 scopus 로고    scopus 로고
    • Hyperthermic pretreatment decreases microvascular protein leakage and attenuates hypotension in anaphylactic shock in rats
    • Chen SC, Lu TS, Lee HL, Lue SI, Yang RC. 2001. Hyperthermic pretreatment decreases microvascular protein leakage and attenuates hypotension in anaphylactic shock in rats. Microvasc Res 61: 152-159.
    • (2001) Microvasc Res , vol.61 , pp. 152-159
    • Chen, S.C.1    Lu, T.S.2    Lee, H.L.3    Lue, S.I.4    Yang, R.C.5
  • 5
    • 0024431368 scopus 로고
    • Transient hyperthermia protects against subsequent forebrain ischemic cell damage in the rat
    • Chopp M, Chen H, Ho KL, Dereski MO, Brown E, Hetzel FW, Welch KM. 1989. Transient hyperthermia protects against subsequent forebrain ischemic cell damage in the rat. Neurology 39: 1396-1398.
    • (1989) Neurology , vol.39 , pp. 1396-1398
    • Chopp, M.1    Chen, H.2    Ho, K.L.3    Dereski, M.O.4    Brown, E.5    Hetzel, F.W.6    Welch, K.M.7
  • 7
    • 0032491391 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton
    • Fanning AS, Jameson BJ, Jesaitis LA, Anderson JM. 1998. The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton. J Biol Chem 273: 29745-29753.
    • (1998) J Biol Chem , vol.273 , pp. 29745-29753
    • Fanning, A.S.1    Jameson, B.J.2    Jesaitis, L.A.3    Anderson, J.M.4
  • 8
    • 0028110309 scopus 로고
    • Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions
    • Furuse M, Itoh M, Hirase T, Nagafuchi A, Yonemura S, Tsukita S. 1994. Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. J Cell Biol 127: 1617-1626.
    • (1994) J Cell Biol , vol.127 , pp. 1617-1626
    • Furuse, M.1    Itoh, M.2    Hirase, T.3    Nagafuchi, A.4    Yonemura, S.5    Tsukita, S.6
  • 9
    • 0032489875 scopus 로고    scopus 로고
    • ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin
    • Haskins J, Gu L, Wittchen ES, Hibbard J, Stevenson BR. 1998. ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin. J Cell Biol 141: 199-208.
    • (1998) J Cell Biol , vol.141 , pp. 199-208
    • Haskins, J.1    Gu, L.2    Wittchen, E.S.3    Hibbard, J.4    Stevenson, B.R.5
  • 10
    • 0034728761 scopus 로고    scopus 로고
    • Small heat shock protein 27 (HSP27) associates with tubulin/microtubules in HeLa cells
    • Hino M, Kurogi K, Okubo MA, Murata-Hori M, Hosoya H. 2000. Small heat shock protein 27 (HSP27) associates with tubulin/microtubules in HeLa cells. Biochem Biophys Res Commun 271: 164-169.
    • (2000) Biochem Biophys Res Commun , vol.271 , pp. 164-169
    • Hino, M.1    Kurogi, K.2    Okubo, M.A.3    Murata-Hori, M.4    Hosoya, H.5
  • 12
    • 0033552629 scopus 로고    scopus 로고
    • Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins
    • Itoh M, Furuse M, Morita K, Kubota K, Saitou M, Tsukita S. 1999. Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J Cell Biol 147: 1351-1363.
    • (1999) J Cell Biol , vol.147 , pp. 1351-1363
    • Itoh, M.1    Furuse, M.2    Morita, K.3    Kubota, K.4    Saitou, M.5    Tsukita, S.6
  • 14
    • 0031149928 scopus 로고    scopus 로고
    • Blood-brain barrier permeability during the development of experimental bacterial meningitis in the rat
    • Kim KS, Wass CA, Cross AS. 1997. Blood-brain barrier permeability during the development of experimental bacterial meningitis in the rat. Exp Neurol 145: 253-257.
    • (1997) Exp Neurol , vol.145 , pp. 253-257
    • Kim, K.S.1    Wass, C.A.2    Cross, A.S.3
  • 15
    • 0027156626 scopus 로고
    • The blood brain barrier in human leukodystrophies and allied diseases. Ultrastructural and morphometric studies on the capillaries in brain biopsies
    • Kondo A, Suzuki K. 1993. The blood brain barrier in human leukodystrophies and allied diseases. Ultrastructural and morphometric studies on the capillaries in brain biopsies. Clin Neuropathol 12: 169-174.
    • (1993) Clin Neuropathol , vol.12 , pp. 169-174
    • Kondo, A.1    Suzuki, K.2
  • 16
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist S. 1986. The heat-shock response. Annu Rev Biochem 55: 1151-1191.
    • (1986) Annu Rev Biochem , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 18
    • 0032555355 scopus 로고    scopus 로고
    • Protein phosphatase inhibitors and heat preconditioning prevent Hsp27 dephosphorylation, F-actin disruption and deterioration of morphology in ATP-depleted endothelial cells
    • Loktionova SA, Kabakov AE. 1998. Protein phosphatase inhibitors and heat preconditioning prevent Hsp27 dephosphorylation, F-actin disruption and deterioration of morphology in ATP-depleted endothelial cells. FEBS Lett 433: 294-300.
    • (1998) FEBS Lett , vol.433 , pp. 294-300
    • Loktionova, S.A.1    Kabakov, A.E.2
  • 19
    • 0026082677 scopus 로고
    • Stabilization of actin filaments at early times after adenovirus infection and in heat-shocked cells
    • Macejak DG, Luftig RB. 1991. Stabilization of actin filaments at early times after adenovirus infection and in heat-shocked cells. Virus Res 19: 31-45.
    • (1991) Virus Res , vol.19 , pp. 31-45
    • Macejak, D.G.1    Luftig, R.B.2
  • 20
    • 0033582334 scopus 로고    scopus 로고
    • Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands
    • Morita K, Furuse M, Fujimoto K, Tsukita S. 1999. Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc Natl Acad Sci U S A 96: 511-516.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 511-516
    • Morita, K.1    Furuse, M.2    Fujimoto, K.3    Tsukita, S.4
  • 21
    • 0036556697 scopus 로고    scopus 로고
    • Actin cytoskeleton and small heat shock proteins: How do they interact?
    • Mounier N, Arrigo AP. 2002. Actin cytoskeleton and small heat shock proteins: how do they interact? Cell Stress Chaperones 7: 167-176.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 167-176
    • Mounier, N.1    Arrigo, A.P.2
  • 22
    • 0029937874 scopus 로고    scopus 로고
    • Induction of heat shock protein 70 protects intestinal epithelial IEC-18 cells from oxidant and thermal injury
    • Musch MW, Ciancio MJ, Sarge K, Chang EB. 1996. Induction of heat shock protein 70 protects intestinal epithelial IEC-18 cells from oxidant and thermal injury. Am J Physiol 270: C429-C436.
    • (1996) Am J Physiol , vol.270
    • Musch, M.W.1    Ciancio, M.J.2    Sarge, K.3    Chang, E.B.4
  • 23
    • 0032934863 scopus 로고    scopus 로고
    • A comparison of blood-brain barrier and blood-nerve barrier endothelial cell markers
    • Orte C, Lawrenson JG, Finn TM, Reid AR, Allt G. 1999. A comparison of blood-brain barrier and blood-nerve barrier endothelial cell markers. Anat Embryol (Berl) 199(6): 509-517.
    • (1999) Anat Embryol (Berl) , vol.199 , Issue.6 , pp. 509-517
    • Orte, C.1    Lawrenson, J.G.2    Finn, T.M.3    Reid, A.R.4    Allt, G.5
  • 24
    • 0024465396 scopus 로고
    • Heat shock and the sorting of luminal ER proteins
    • Pelham HR. 1989. Heat shock and the sorting of luminal ER proteins. EMBO J 8: 3171-3176.
    • (1989) EMBO J , vol.8 , pp. 3171-3176
    • Pelham, H.R.1
  • 25
    • 0036935830 scopus 로고    scopus 로고
    • Junctional complexes of the blood-brain barrier: Permeability changes in neuroinflammation
    • Petty MA, Lo EH. 2002. Junctional complexes of the blood-brain barrier: permeability changes in neuroinflammation. Prog Neurobiol 68: 311-323.
    • (2002) Prog Neurobiol , vol.68 , pp. 311-323
    • Petty, M.A.1    Lo, E.H.2
  • 26
    • 0033974507 scopus 로고    scopus 로고
    • Osmotic opening of the blood-brain barrier: Principles, mechanism, and therapeutic applications
    • Rapoport SI. 2000. Osmotic opening of the blood-brain barrier: principles, mechanism, and therapeutic applications. Cell Mol Neurobiol 20: 217-230.
    • (2000) Cell Mol Neurobiol , vol.20 , pp. 217-230
    • Rapoport, S.I.1
  • 27
    • 0029566972 scopus 로고
    • Induction of HSP-70 after hyperosmotic opening of the blood-brain barrier in the rat
    • Richmon JD, Fukuda K, Sharp FR, Noble LJ. 1995. Induction of HSP-70 after hyperosmotic opening of the blood-brain barrier in the rat. Neurosci Lett 202: 1-4.
    • (1995) Neurosci Lett , vol.202 , pp. 1-4
    • Richmon, J.D.1    Fukuda, K.2    Sharp, F.R.3    Noble, L.J.4
  • 28
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in Drosophila
    • Ritossa F. 1962. A new puffing pattern induced by temperature shock and DNP in Drosophila. Experientia 18: 571-573.
    • (1962) Experientia , vol.18 , pp. 571-573
    • Ritossa, F.1
  • 29
    • 2642680857 scopus 로고    scopus 로고
    • Alzheimer disease: DNA fragmentation indicates increased neuronal vulnerability, but not apoptosis
    • Stadelmann C, Bruck W, Bancher C, Jellinger K, Lassmann H. 1998. Alzheimer disease: DNA fragmentation indicates increased neuronal vulnerability, but not apoptosis. J Neuropathol Exp Neurol 57: 456-464.
    • (1998) J Neuropathol Exp Neurol , vol.57 , pp. 456-464
    • Stadelmann, C.1    Bruck, W.2    Bancher, C.3    Jellinger, K.4    Lassmann, H.5
  • 30
    • 0016373748 scopus 로고
    • Protein synthesis in salivary glands of Drosophila melanogaster: Relation to chromosome puffs
    • Tissieres A, Mitchell HK, Tracy UM. 1974. Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs. J Mol Biol 85: 389-398.
    • (1974) J Mol Biol , vol.85 , pp. 389-398
    • Tissieres, A.1    Mitchell, H.K.2    Tracy, U.M.3
  • 31
    • 0014768365 scopus 로고
    • Simple method for quantitation of enhanced vascular permeability
    • Udaka K, Takeuchi Y, Movat HZ. 1970. Simple method for quantitation of enhanced vascular permeability. Proc Soc Exp Biol Med 133: 1384-1387.
    • (1970) Proc Soc Exp Biol Med , vol.133 , pp. 1384-1387
    • Udaka, K.1    Takeuchi, Y.2    Movat, H.Z.3
  • 32
    • 0032533212 scopus 로고    scopus 로고
    • Dexamethasone protection of rat intestinal epithelial cells against oxidant injury is mediated by induction of heat shock protein 72
    • Urayama S, Musch MW, Retsky J, Madonna MB, Straus D, Chang EB. 1998. Dexamethasone protection of rat intestinal epithelial cells against oxidant injury is mediated by induction of heat shock protein 72. J Clin Investig 102: 1860-1865.
    • (1998) J Clin Investig , vol.102 , pp. 1860-1865
    • Urayama, S.1    Musch, M.W.2    Retsky, J.3    Madonna, M.B.4    Straus, D.5    Chang, E.B.6
  • 34
    • 0033521140 scopus 로고    scopus 로고
    • Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3
    • Wittchen ES, Haskins J, Stevenson BR. 1999. Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3. J Biol Chem 274: 35179-35185.
    • (1999) J Biol Chem , vol.274 , pp. 35179-35185
    • Wittchen, E.S.1    Haskins, J.2    Stevenson, B.R.3
  • 35
    • 0028466527 scopus 로고
    • Molecular chaperones: Heat-shock proteins, foldases, and matchmakers
    • Wynn RM, Davie JR, Cox RP, Chuang DT. 1994. Molecular chaperones: heat-shock proteins, foldases, and matchmakers. J Lab Clin Med 124: 31-36.
    • (1994) J Lab Clin Med , vol.124 , pp. 31-36
    • Wynn, R.M.1    Davie, J.R.2    Cox, R.P.3    Chuang, D.T.4
  • 36
    • 0034963988 scopus 로고    scopus 로고
    • Induction of the HSP110/105 family in the rat hippocampus in cerebral ischemia and ischemic tolerance
    • Yagita Y, Kitagawa K, Ohtsuki T, Tanaka S, Hori M, Matsumoto M. 2001. Induction of the HSP110/105 family in the rat hippocampus in cerebral ischemia and ischemic tolerance. J Cereb Blood Flow Metab 21: 811-819.
    • (2001) J Cereb Blood Flow Metab , vol.21 , pp. 811-819
    • Yagita, Y.1    Kitagawa, K.2    Ohtsuki, T.3    Tanaka, S.4    Hori, M.5    Matsumoto, M.6
  • 37
    • 0033768644 scopus 로고    scopus 로고
    • Potential protective effect of NF-kappaB activity on the polymicrobial sepsis of rats preconditioning heat shock treatment
    • Yang RC, Chen HW, Lu TS, Hsu C. 2000. Potential protective effect of NF-kappaB activity on the polymicrobial sepsis of rats preconditioning heat shock treatment. Clin Chim Acta 302: 11-22.
    • (2000) Clin Chim Acta , vol.302 , pp. 11-22
    • Yang, R.C.1    Chen, H.W.2    Lu, T.S.3    Hsu, C.4
  • 39
  • 40
    • 0028243784 scopus 로고
    • The effect of hyperthermic treatment on electroencephalographic recovery after interruption of respiration in rats
    • Yang SL, Jing SH, Chen SS, Chen TJ, Yang RC. 1994. The effect of hyperthermic treatment on electroencephalographic recovery after interruption of respiration in rats. Exp Brain Res 99: 431-434.
    • (1994) Exp Brain Res , vol.99 , pp. 431-434
    • Yang, S.L.1    Jing, S.H.2    Chen, S.S.3    Chen, T.J.4    Yang, R.C.5
  • 41
    • 0026566298 scopus 로고
    • Stress proteins and myocardial protection
    • Yellon DM, Latchman DS. 1992. Stress proteins and myocardial protection. J Mol Cell Cardiol 24: 113-124.
    • (1992) J Mol Cell Cardiol , vol.24 , pp. 113-124
    • Yellon, D.M.1    Latchman, D.S.2


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