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Volumn 2015, Issue , 2015, Pages

Role of Exogenous Hsp72 on Liver Dysfunction during Sepsis

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE AMINOTRANSFERASE; ASPARTATE AMINOTRANSFERASE; CASPASE 3; CASPASE 9; HEAT SHOCK PROTEIN 72; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEIN BAX; PROTEIN BCL 2; RECOMBINANT PROTEIN;

EID: 84937010610     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2015/508101     Document Type: Article
Times cited : (8)

References (47)
  • 1
    • 0028361220 scopus 로고
    • Search for sepsis drugs goes on despite past failures
    • R. Stone, "Search for sepsis drugs goes on despite past failures," Science, vol. 264, no. 5157, pp. 365-367, 1994.
    • (1994) Science , vol.264 , Issue.5157 , pp. 365-367
    • Stone, R.1
  • 2
    • 0037451929 scopus 로고    scopus 로고
    • The epidemiology of sepsis in the United States from 1979 through 2000
    • G. S. Martin, D. M. Mannino, S. Eaton, and M. Moss, "The epidemiology of sepsis in the United States from 1979 through 2000," The New England Journal of Medicine, vol. 348, no. 16, pp. 1546-1554, 2003.
    • (2003) The New England Journal of Medicine , vol.348 , Issue.16 , pp. 1546-1554
    • Martin, G.S.1    Mannino, D.M.2    Eaton, S.3    Moss, M.4
  • 3
    • 0032879431 scopus 로고    scopus 로고
    • Inflammation, sepsis, and coagulation
    • C. T. Esmon, K. Fukudome, T. Mather et al., "Inflammation, sepsis, and coagulation," Haematologica, vol. 84, pp. 254-259, 1999.
    • (1999) Haematologica , vol.84 , pp. 254-259
    • Esmon, C.T.1    Fukudome, K.2    Mather, T.3
  • 5
    • 18844416582 scopus 로고    scopus 로고
    • Insulinprevents liver damage and preserves liver function in lipopolysaccharide-induced endotoxemic rats
    • M. G. Jeschke, H. Rensing, D. Kleinet al., "Insulinprevents liver damage and preserves liver function in lipopolysaccharide-induced endotoxemic rats," Journal of Hepatology, vol. 42, no. 6, pp. 870-879, 2005.
    • (2005) Journal of Hepatology , vol.42 , Issue.6 , pp. 870-879
    • Jeschke, M.G.1    Rensing, H.2    Klein, D.3
  • 6
    • 0034927828 scopus 로고    scopus 로고
    • Hepatic response to sepsis: Interaction between coagulation and inflammatory processes
    • J. F. Dhainaut, N. Marin, A. Mignon, and C. Vinsonneau, "Hepatic response to sepsis: interaction between coagulation and inflammatory processes," Critical Care Medicine, vol. 29, no. 7, supplement, pp. S42-S47, 2001.
    • (2001) Critical Care Medicine , vol.29 , Issue.7 , pp. S42-S47
    • Dhainaut, J.F.1    Marin, N.2    Mignon, A.3    Vinsonneau, C.4
  • 7
    • 84907840194 scopus 로고    scopus 로고
    • The role of the liver in sepsis
    • J. Yan, S. Li, and S. Li, "The role of the liver in sepsis," International Reviews of Immunology, vol. 33, no. 6, pp. 498-510, 2014.
    • (2014) International Reviews of Immunology , vol.33 , Issue.6 , pp. 498-510
    • Yan, J.1    Li, S.2    Li, S.3
  • 8
    • 84918768662 scopus 로고    scopus 로고
    • GSK-3beta inhibition attenuates CLP-induced liver injury by reducing inflammation and hepatic cell apoptosis
    • H. Zhang, W. Wang, H. Fang et al., "GSK-3beta inhibition attenuates CLP-induced liver injury by reducing inflammation and hepatic cell apoptosis," Mediators of Inflammation, vol. 2014, Article ID 629507, 10 pages, 2014.
    • (2014) Mediators of Inflammation , vol.2014
    • Zhang, H.1    Wang, W.2    Fang, H.3
  • 9
    • 0033675121 scopus 로고    scopus 로고
    • Attenuation of sepsis-induced apoptosis by heat shock pretreatment in rats
    • H.-W. Chen, C. Hsu, S.-I. Lue, and R.-C. Yang, "Attenuation of sepsis-induced apoptosis by heat shock pretreatment in rats," Cell Stress and Chaperones, vol. 5, no. 3, pp. 188-195, 2000.
    • (2000) Cell Stress and Chaperones , vol.5 , Issue.3 , pp. 188-195
    • Chen, H.-W.1    Hsu, C.2    Lue, S.-I.3    Yang, R.-C.4
  • 10
    • 79951672874 scopus 로고    scopus 로고
    • Increased stability of Bcl-2 in HSP70-mediated protection against apoptosis induced by oxidative stress
    • B. Jiang, P. Liang, G. Deng, Z. Tu, M. Liu, and X. Xiao, "Increased stability of Bcl-2 in HSP70-mediated protection against apoptosis induced by oxidative stress," Cell Stress and Chaperones, vol. 16, no. 2, pp. 143-152, 2011.
    • (2011) Cell Stress and Chaperones , vol.16 , Issue.2 , pp. 143-152
    • Jiang, B.1    Liang, P.2    Deng, G.3    Tu, Z.4    Liu, M.5    Xiao, X.6
  • 11
    • 0036284788 scopus 로고    scopus 로고
    • HSP70 protects against TNF-induced lethal inflammatory shock
    • W. van Molle, B. Wielockx, T. Mahieu et al., "HSP70 protects against TNF-induced lethal inflammatory shock," Immunity, vol. 16, no. 5, pp. 685-695, 2002.
    • (2002) Immunity , vol.16 , Issue.5 , pp. 685-695
    • Van Molle, W.1    Wielockx, B.2    Mahieu, T.3
  • 13
    • 35848961241 scopus 로고    scopus 로고
    • Regulation of heat shock protein 70 release in astrocytes: Role of signaling kinases
    • A. R. Taylor, M. B. Robinson, D. J. Gifondorwa, M. Tytell, and C. E. Milligan, "Regulation of heat shock protein 70 release in astrocytes: role of signaling kinases," Developmental Neurobiology, vol. 67, no. 13, pp. 1815-1829, 2007.
    • (2007) Developmental Neurobiology , vol.67 , Issue.13 , pp. 1815-1829
    • Taylor, A.R.1    Robinson, M.B.2    Gifondorwa, D.J.3    Tytell, M.4    Milligan, C.E.5
  • 14
    • 0037484291 scopus 로고    scopus 로고
    • Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlateswith itsmembrane delivery and release
    • A. H. Broquet, G. Thomas, J. Masliah, G. Trugnan, and M. Bachelet, "Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlateswith itsmembrane delivery and release," The Journal of Biological Chemistry, vol. 278, no. 24, pp. 21601-21606, 2003.
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.24 , pp. 21601-21606
    • Broquet, A.H.1    Thomas, G.2    Masliah, J.3    Trugnan, G.4    Bachelet, M.5
  • 15
  • 16
    • 0347384214 scopus 로고    scopus 로고
    • Elevated serum heat-shock protein 70 levels in patients with acute infection: Use of an optimized enzyme-linked immunosorbent assay
    • R. Njemini, M. Lambert, C. Demanet, and T. Mets, "Elevated serum heat-shock protein 70 levels in patients with acute infection: use of an optimized enzyme-linked immunosorbent assay," Scandinavian Journal of Immunology, vol. 58, no. 6, pp. 664-669, 2003.
    • (2003) Scandinavian Journal of Immunology , vol.58 , Issue.6 , pp. 664-669
    • Njemini, R.1    Lambert, M.2    Demanet, C.3    Mets, T.4
  • 17
    • 24944450708 scopus 로고    scopus 로고
    • Diabetic ketoacidosis increases extracellular levels of the major inducible 70-kDa heat shock protein
    • M. J. Oglesbee, A. V. Herdman, G. G. Passmore, and W. H. Hoffman, "Diabetic ketoacidosis increases extracellular levels of the major inducible 70-kDa heat shock protein," Clinical Biochemistry, vol. 38, no. 10, pp. 900-904, 2005.
    • (2005) Clinical Biochemistry , vol.38 , Issue.10 , pp. 900-904
    • Oglesbee, M.J.1    Herdman, A.V.2    Passmore, G.G.3    Hoffman, W.H.4
  • 18
    • 79951680104 scopus 로고    scopus 로고
    • Heat shock proteins as biomarkers for the rapid detection of brain and spinal cord ischemia: A review and comparison to other methods of detection in thoracic aneurysm repair
    • J. G. Hecker and M. McGarvey, "Heat shock proteins as biomarkers for the rapid detection of brain and spinal cord ischemia: a review and comparison to other methods of detection in thoracic aneurysm repair," Cell Stress & Chaperones, vol. 16, no. 2, pp. 119-131, 2011.
    • (2011) Cell Stress & Chaperones , vol.16 , Issue.2 , pp. 119-131
    • Hecker, J.G.1    McGarvey, M.2
  • 21
    • 23744513067 scopus 로고    scopus 로고
    • Parenteral glutamine increases serum heat shock protein 70 in critically ill patients
    • T. R. Ziegler, L. G. Ogden, K. D. Singleton et al., "Parenteral glutamine increases serum heat shock protein 70 in critically ill patients," Intensive Care Medicine, vol. 31, no. 8, pp. 1079-1086, 2005.
    • (2005) Intensive Care Medicine , vol.31 , Issue.8 , pp. 1079-1086
    • Ziegler, T.R.1    Ogden, L.G.2    Singleton, K.D.3
  • 22
    • 4143096014 scopus 로고    scopus 로고
    • Heat shockprotein 70 in patients with chronic heart failure: Relation to disease severity and survival
    • S. Genth-Zotz, A. P. Bolger, P.R. Kalra et al., "Heat shockprotein 70 in patients with chronic heart failure: relation to disease severity and survival," International Journal of Cardiology, vol. 96, no. 3, pp. 397-401, 2004.
    • (2004) International Journal of Cardiology , vol.96 , Issue.3 , pp. 397-401
    • Genth-Zotz, S.1    Bolger, A.P.2    Kalra, P.R.3
  • 23
    • 33748427081 scopus 로고    scopus 로고
    • Exogenous heat shock protein 70 mediates sepsis manifestations and decreases the mortality rate in rats
    • G. A. Kustanova, A. N. Murashev, V. L. Karpov et al., "Exogenous heat shock protein 70 mediates sepsis manifestations and decreases the mortality rate in rats," Cell Stress & Chaperones, vol. 11, no. 3, pp. 276-286, 2006.
    • (2006) Cell Stress & Chaperones , vol.11 , Issue.3 , pp. 276-286
    • Kustanova, G.A.1    Murashev, A.N.2    Karpov, V.L.3
  • 24
    • 84859402355 scopus 로고    scopus 로고
    • Extracellular heat shock protein 72 protects schwann cells from hydrogen peroxide-induced apoptosis
    • X. Luo, L. Tao, P. Lin, X. Mo, and H. Chen, "Extracellular heat shock protein 72 protects schwann cells from hydrogen peroxide-induced apoptosis," Journal of Neuroscience Research, vol. 90, no. 6, pp. 1261-1269, 2012.
    • (2012) Journal of Neuroscience Research , vol.90 , Issue.6 , pp. 1261-1269
    • Luo, X.1    Tao, L.2    Lin, P.3    Mo, X.4    Chen, H.5
  • 25
    • 80655146272 scopus 로고    scopus 로고
    • Treatment with recombinant Hsp72 suppresses collagen-induced arthritis in mice
    • X. Luo, X. Zuo, X. Mo, Y. Zhou, and X. Xiao, "Treatment with recombinant Hsp72 suppresses collagen-induced arthritis in mice," Inflammation, vol. 34, no. 5, pp. 432-439, 2011.
    • (2011) Inflammation , vol.34 , Issue.5 , pp. 432-439
    • Luo, X.1    Zuo, X.2    Mo, X.3    Zhou, Y.4    Xiao, X.5
  • 26
    • 84930048155 scopus 로고    scopus 로고
    • Exogenous heat shock cognate protein 70 pretreatment attenuates cardiac and hepatic dysfunction with associated anti-inflammatory responses in experimental septic shock
    • J. H. Hsu, R. C. Yang, S. J. Lin et al., "Exogenous heat shock cognate protein 70 pretreatment attenuates cardiac and hepatic dysfunction with associated anti-inflammatory responses in experimental septic shock," Shock, vol. 42, no. 6, pp. 540-547, 2014.
    • (2014) Shock , vol.42 , Issue.6 , pp. 540-547
    • Hsu, J.H.1    Yang, R.C.2    Lin, S.J.3
  • 27
    • 17644391384 scopus 로고    scopus 로고
    • Pharmacokinetic and tissue distribution mechanism of mouse recombinant heat shock protein 70 in mice
    • S. Takemoto, M. Nishikawa, and Y. Takakura, "Pharmacokinetic and tissue distribution mechanism of mouse recombinant heat shock protein 70 in mice," Pharmaceutical Research, vol. 22, no. 3, pp. 419-426, 2005.
    • (2005) Pharmaceutical Research , vol.22 , Issue.3 , pp. 419-426
    • Takemoto, S.1    Nishikawa, M.2    Takakura, Y.3
  • 28
    • 1942535086 scopus 로고    scopus 로고
    • Relationships between objective assessment of ligament stability and subjective assessment of symptoms and function after anterior cruciate ligament reconstruction
    • M. S. Kocher, J. R. Steadman, K. K. Briggs, W. I. Sterett, and R. J. Hawkins, "Relationships between objective assessment of ligament stability and subjective assessment of symptoms and function after anterior cruciate ligament reconstruction," The American Journal of Sports Medicine, vol. 32, no. 3, pp. 629-634, 2004.
    • (2004) The American Journal of Sports Medicine , vol.32 , Issue.3 , pp. 629-634
    • Kocher, M.S.1    Steadman, J.R.2    Briggs, K.K.3    Sterett, W.I.4    Hawkins, R.J.5
  • 29
    • 0018964280 scopus 로고
    • Sepsis and septic shock: A review of laboratorymodels and a proposal
    • K. A. Wichterman, A. E. Baue, and I. H. Chaudry, "Sepsis and septic shock: a review of laboratorymodels and a proposal," The Journal of Surgical Research, vol. 29, no. 2, pp. 189-201, 1980.
    • (1980) The Journal of Surgical Research , vol.29 , Issue.2 , pp. 189-201
    • Wichterman, K.A.1    Baue, A.E.2    Chaudry, I.H.3
  • 30
    • 84870059173 scopus 로고    scopus 로고
    • Attenuation ofmitochondrial unfolded protein response is associated with hepatic dysfunction in septic rats
    • L.-J. Huang, H.-P. Dong, I.-C. Chuang, M.-S. Liu, and R.-C. Yang, "Attenuation ofmitochondrial unfolded protein response is associated with hepatic dysfunction in septic rats," Shock, vol. 38, no. 6, pp. 642-648, 2012.
    • (2012) Shock , vol.38 , Issue.6 , pp. 642-648
    • Huang, L.-J.1    Dong, H.-P.2    Chuang, I.-C.3    Liu, M.-S.4    Yang, R.-C.5
  • 31
    • 38449110130 scopus 로고    scopus 로고
    • Hsp72 induces inflammation and regulates cytokine production in airway epithelium through a TLR4- and NF-kappaB-dependent mechanism
    • M. A. Chase, D. S. Wheeler, K. M. Lierl, V. S. Hughes, H. R. Wong, and K. Page, "Hsp72 induces inflammation and regulates cytokine production in airway epithelium through a TLR4- and NF-kappaB-dependent mechanism," The Journal of Immunology, vol. 179, no. 9, pp. 6318-6324, 2007.
    • (2007) The Journal of Immunology , vol.179 , Issue.9 , pp. 6318-6324
    • Chase, M.A.1    Wheeler, D.S.2    Lierl, K.M.3    Hughes, V.S.4    Wong, H.R.5    Page, K.6
  • 32
    • 45849115860 scopus 로고    scopus 로고
    • Liver perfusion in sepsis, septic shock, and multiorgan failure
    • H. Spapen, "Liver perfusion in sepsis, septic shock, and multiorgan failure," Anatomical Record, vol. 291, no. 6, pp. 714-720, 2008.
    • (2008) Anatomical Record , vol.291 , Issue.6 , pp. 714-720
    • Spapen, H.1
  • 33
    • 84920156684 scopus 로고    scopus 로고
    • Baicalein protects against polymicrobial sepsis-induced liver injury via inhibition of inflammation and apoptosis in mice
    • A. Liu, W. Wang, H. Fang et al., "Baicalein protects against polymicrobial sepsis-induced liver injury via inhibition of inflammation and apoptosis in mice," European Journal of Pharmacology, vol. 748, pp. 45-53, 2015.
    • (2015) European Journal of Pharmacology , vol.748 , pp. 45-53
    • Liu, A.1    Wang, W.2    Fang, H.3
  • 34
    • 77953189905 scopus 로고    scopus 로고
    • Exogenous mammalian extracellular HSP70 reduces endotoxin manifestations at the cellular and organismlevels
    • E. Rozhkova, M. Yurinskaya, O. Zatsepina et al., "Exogenous mammalian extracellular HSP70 reduces endotoxin manifestations at the cellular and organismlevels," Annals of the New York Academy of Sciences, vol. 1197, pp. 94-107, 2010.
    • (2010) Annals of the New York Academy of Sciences , vol.1197 , pp. 94-107
    • Rozhkova, E.1    Yurinskaya, M.2    Zatsepina, O.3
  • 35
    • 84858987433 scopus 로고    scopus 로고
    • Recombinant human Hsp70 protects against lipoteichoic acid-induced inflammation manifestations at the cellular and organismal levels
    • M. Vinokurov, V. Ostrov, M. Yurinskaya et al., "Recombinant human Hsp70 protects against lipoteichoic acid-induced inflammation manifestations at the cellular and organismal levels," Cell Stress & Chaperones, vol. 17, no. 1, pp. 89-101, 2012.
    • (2012) Cell Stress & Chaperones , vol.17 , Issue.1 , pp. 89-101
    • Vinokurov, M.1    Ostrov, V.2    Yurinskaya, M.3
  • 36
    • 84874290585 scopus 로고    scopus 로고
    • Sepsis-associated liver injury: Incidence, classification and the clinical significance
    • H. Kobashi, J. Toshimori, and K. Yamamoto, "Sepsis-associated liver injury: incidence, classification and the clinical significance," Hepatology Research, vol. 43, no. 3, pp. 255-266, 2013.
    • (2013) Hepatology Research , vol.43 , Issue.3 , pp. 255-266
    • Kobashi, H.1    Toshimori, J.2    Yamamoto, K.3
  • 37
  • 39
    • 0033120115 scopus 로고    scopus 로고
    • Overexpression of Bcl-2 in transgenic mice decreases apoptosis and improves survival in sepsis
    • R. S. Hotchkiss, P. E. Swanson, C. M. Knudson et al., "Overexpression of Bcl-2 in transgenic mice decreases apoptosis and improves survival in sepsis," Journal of Immunology, vol. 162, no. 7, pp. 4148-4156, 1999.
    • (1999) Journal of Immunology , vol.162 , Issue.7 , pp. 4148-4156
    • Hotchkiss, R.S.1    Swanson, P.E.2    Knudson, C.M.3
  • 40
    • 0031918223 scopus 로고    scopus 로고
    • BCL-2 family: Regulators of cell death
    • D. T. Chao and S. J. Korsmeyer, "BCL-2 family: regulators of cell death," Annual Review of Immunology, vol. 16, pp. 395-419, 1998.
    • (1998) Annual Review of Immunology , vol.16 , pp. 395-419
    • Chao, D.T.1    Korsmeyer, S.J.2
  • 41
    • 33745954330 scopus 로고    scopus 로고
    • BCL2 family in DNA damage and cell cycle control
    • S. Zinkel, A. Gross, and E. Yang, "BCL2 family in DNA damage and cell cycle control," Cell Death and Differentiation, vol. 13, no. 8, pp. 1351-1359, 2006.
    • (2006) Cell Death and Differentiation , vol.13 , Issue.8 , pp. 1351-1359
    • Zinkel, S.1    Gross, A.2    Yang, E.3
  • 42
    • 84961289481 scopus 로고    scopus 로고
    • Tubeimoside-1 induces glioma apoptosis through regulation of Bax/Bcl-2 and the ROS/Cytochrome C/Caspase-3 pathway
    • G. Jia, Q. Wang, R. Wang, and et al, "Tubeimoside-1 induces glioma apoptosis through regulation of Bax/Bcl-2 and the ROS/Cytochrome C/Caspase-3 pathway," Onco Targets and Therapy, vol. 8, pp. 303-2011, 2015.
    • (2015) Onco Targets and Therapy , vol.8 , pp. 303-2011
    • Jia, G.1    Wang, Q.2    Wang, R.3
  • 43
    • 1542344934 scopus 로고    scopus 로고
    • Bax-induced cytochrome c release frommitochondria depends on α-helices- 5 and -6
    • G. Heimlich, A. D. McKinnon, K. Bernardo et al., "Bax-induced cytochrome c release frommitochondria depends on α-helices- 5 and -6," The Biochemical Journal, vol. 378, no. 1, pp. 247-255, 2004.
    • (2004) The Biochemical Journal , vol.378 , Issue.1 , pp. 247-255
    • Heimlich, G.1    McKinnon, A.D.2    Bernardo, K.3
  • 45
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • M. O. Hengartner, "The biochemistry of apoptosis," Nature, vol. 407, no. 6805, pp. 770-776, 2000.
    • (2000) Nature , vol.407 , Issue.6805 , pp. 770-776
    • Hengartner, M.O.1
  • 46
    • 2442561553 scopus 로고    scopus 로고
    • Apoptosis as a novel target for cancer chemoprevention
    • S.-Y. Sun, N. Hail Jr., and R. Lotan, "Apoptosis as a novel target for cancer chemoprevention," Journal of the National Cancer Institute, vol. 96, no. 9, pp. 662-672, 2004.
    • (2004) Journal of the National Cancer Institute , vol.96 , Issue.9 , pp. 662-672
    • Sun, S.-Y.1    Hail, N.2    Lotan, R.3
  • 47
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • Y. Shi, "Mechanisms of caspase activation and inhibition during apoptosis," Molecular Cell, vol. 9, no. 3, pp. 459-470, 2002.
    • (2002) Molecular Cell , vol.9 , Issue.3 , pp. 459-470
    • Shi, Y.1


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