메뉴 건너뛰기




Volumn 81, Issue 2, 2011, Pages 189-197

HMGB1 induces human lung endothelial cell cytoskeletal rearrangement and barrier disruption

Author keywords

Acute lung injury; Endothelium; HMGB1; Hsp27; MAP kinase; RAGE

Indexed keywords

ACTIN; ADVANCED GLYCATION END PRODUCT RECEPTOR; CADHERIN; HEAT SHOCK PROTEIN 27; HIGH MOBILITY GROUP B1 PROTEIN; HIGH MOBILITY GROUP B1 PROTEIN RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; RECEPTOR PROTEIN; SMALL INTERFERING RNA; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 4; UNCLASSIFIED DRUG;

EID: 79651474104     PISSN: 00262862     EISSN: 10959319     Source Type: Journal    
DOI: 10.1016/j.mvr.2010.11.010     Document Type: Article
Times cited : (174)

References (47)
  • 1
    • 0034698830 scopus 로고    scopus 로고
    • High mobility group 1 protein (HMG-1) stimulates proinflammatory cytokine synthesis in human monocytes
    • Andersson U., et al. High mobility group 1 protein (HMG-1) stimulates proinflammatory cytokine synthesis in human monocytes. J. Exp. Med. 2000, 192:565-570.
    • (2000) J. Exp. Med. , vol.192 , pp. 565-570
    • Andersson, U.1
  • 2
    • 0025177039 scopus 로고
    • Tumor necrosis factor induces the rapid phosphorylation of the mammalian heat shock protein hsp28
    • Arrigo A.P. Tumor necrosis factor induces the rapid phosphorylation of the mammalian heat shock protein hsp28. Mol. Cell. Biol. 1990, 10:1276-1280.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1276-1280
    • Arrigo, A.P.1
  • 3
    • 27744453362 scopus 로고    scopus 로고
    • Understanding RAGE, the receptor for advanced glycation end products
    • Bierhaus A., et al. Understanding RAGE, the receptor for advanced glycation end products. J. Mol. Med. 2005, 83:876-886.
    • (2005) J. Mol. Med. , vol.83 , pp. 876-886
    • Bierhaus, A.1
  • 4
    • 59849120325 scopus 로고    scopus 로고
    • Endothelial permeability is controlled by spatially defined cytoskeletal mechanics: atomic force microscopy force mapping of pulmonary endothelial monolayer
    • Birukova A.A., et al. Endothelial permeability is controlled by spatially defined cytoskeletal mechanics: atomic force microscopy force mapping of pulmonary endothelial monolayer. Nanomedicine 2009, 5:30-41.
    • (2009) Nanomedicine , vol.5 , pp. 30-41
    • Birukova, A.A.1
  • 5
    • 20844463626 scopus 로고    scopus 로고
    • MAP kinases in lung endothelial permeability induced by microtubule disassembly
    • Birukova A.A., et al. MAP kinases in lung endothelial permeability induced by microtubule disassembly. Am. J. Physiol. Lung Cell. Mol. Physiol. 2005, 289:L75-L84.
    • (2005) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.289
    • Birukova, A.A.1
  • 6
    • 0347989369 scopus 로고    scopus 로고
    • Role of Rho GTPases in thrombin-induced lung vascular endothelial cells barrier dysfunction
    • Birukova A.A., et al. Role of Rho GTPases in thrombin-induced lung vascular endothelial cells barrier dysfunction. Microvasc. Res. 2004, 67:64-77.
    • (2004) Microvasc. Res. , vol.67 , pp. 64-77
    • Birukova, A.A.1
  • 7
    • 0034807581 scopus 로고    scopus 로고
    • Cytoskeletal regulation of pulmonary vascular permeability
    • Dudek S.M., Garcia J.G. Cytoskeletal regulation of pulmonary vascular permeability. J. Appl. Physiol. 2001, 91:1487-1500.
    • (2001) J. Appl. Physiol. , vol.91 , pp. 1487-1500
    • Dudek, S.M.1    Garcia, J.G.2
  • 8
    • 0037769813 scopus 로고    scopus 로고
    • Inflammation-promoting activity of HMGB1 on human microvascular endothelial cells
    • Fiuza C., et al. Inflammation-promoting activity of HMGB1 on human microvascular endothelial cells. Blood 2003, 101:2652-2660.
    • (2003) Blood , vol.101 , pp. 2652-2660
    • Fiuza, C.1
  • 9
    • 33244471768 scopus 로고    scopus 로고
    • MAPKAP kinases-MKs-two's company, three's a crowd
    • Gaestel M. MAPKAP kinases-MKs-two's company, three's a crowd. Nat. Rev. Mol. Cell Biol. 2006, 7:120-130.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 120-130
    • Gaestel, M.1
  • 10
    • 0034799675 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate promotes endothelial cell barrier integrity by Edg-dependent cytoskeletal rearrangement
    • Garcia J.G., et al. Sphingosine 1-phosphate promotes endothelial cell barrier integrity by Edg-dependent cytoskeletal rearrangement. J. Clin. Invest. 2001, 108:689-701.
    • (2001) J. Clin. Invest. , vol.108 , pp. 689-701
    • Garcia, J.G.1
  • 11
    • 0036314504 scopus 로고    scopus 로고
    • Critical involvement of p38 MAP kinase in pertussis toxin-induced cytoskeletal reorganization and lung permeability
    • Garcia J.G., et al. Critical involvement of p38 MAP kinase in pertussis toxin-induced cytoskeletal reorganization and lung permeability. FASEB J. 2002, 16:1064-1076.
    • (2002) FASEB J. , vol.16 , pp. 1064-1076
    • Garcia, J.G.1
  • 12
    • 33845697912 scopus 로고    scopus 로고
    • Advanced glycation end products induce actin rearrangement and subsequent hyperpermeability of endothelial cells
    • Guo X.H., et al. Advanced glycation end products induce actin rearrangement and subsequent hyperpermeability of endothelial cells. APMIS 2006, 114:874-883.
    • (2006) APMIS , vol.114 , pp. 874-883
    • Guo, X.H.1
  • 13
    • 0033120590 scopus 로고    scopus 로고
    • Differential expression and activation of p38 mitogen-activated protein kinase alpha, beta, gamma, and delta in inflammatory cell lineages
    • Hale K.K., et al. Differential expression and activation of p38 mitogen-activated protein kinase alpha, beta, gamma, and delta in inflammatory cell lineages. J. Immunol. 1999, 162:4246-4252.
    • (1999) J. Immunol. , vol.162 , pp. 4246-4252
    • Hale, K.K.1
  • 14
    • 1842661193 scopus 로고    scopus 로고
    • Endothelial barrier dysfunction caused by LPS correlates with phosphorylation of HSP27 in vivo
    • Hirano S., et al. Endothelial barrier dysfunction caused by LPS correlates with phosphorylation of HSP27 in vivo. Cell Biol. Toxicol. 2004, 20:1-14.
    • (2004) Cell Biol. Toxicol. , vol.20 , pp. 1-14
    • Hirano, S.1
  • 15
    • 0031057892 scopus 로고    scopus 로고
    • Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells
    • Huot J., et al. Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells. Circ. Res. 1997, 80:383-392.
    • (1997) Circ. Res. , vol.80 , pp. 383-392
    • Huot, J.1
  • 16
    • 0026377764 scopus 로고
    • Tumor necrosis factor levels in serum and bronchoalveolar lavage fluid of patients with the adult respiratory distress syndrome
    • Hyers T.M., et al. Tumor necrosis factor levels in serum and bronchoalveolar lavage fluid of patients with the adult respiratory distress syndrome. Am. Rev. Respir. Dis. 1991, 144:268-271.
    • (1991) Am. Rev. Respir. Dis. , vol.144 , pp. 268-271
    • Hyers, T.M.1
  • 17
    • 20244373188 scopus 로고    scopus 로고
    • HMGB1 contributes to the development of acute lung injury after hemorrhage
    • Kim J.Y., et al. HMGB1 contributes to the development of acute lung injury after hemorrhage. Am. J. Physiol. Lung Cell. Mol. Physiol. 2005, 288:L958-L965.
    • (2005) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.288
    • Kim, J.Y.1
  • 18
    • 48149096398 scopus 로고    scopus 로고
    • HMGB1: endogenous danger signaling
    • Klune J.R., et al. HMGB1: endogenous danger signaling. Mol. Med. 2008, 14:476-484.
    • (2008) Mol. Med. , vol.14 , pp. 476-484
    • Klune, J.R.1
  • 19
    • 19944431800 scopus 로고    scopus 로고
    • RAGE is the major receptor for the proinflammatory activity of HMGB1 in rodent macrophages
    • Kokkola R., et al. RAGE is the major receptor for the proinflammatory activity of HMGB1 in rodent macrophages. Scand. J. Immunol. 2005, 61:1-9.
    • (2005) Scand. J. Immunol. , vol.61 , pp. 1-9
    • Kokkola, R.1
  • 20
    • 70350474677 scopus 로고    scopus 로고
    • Heat shock protein 27 phosphorylation: kinases, phosphatases, functions and pathology
    • Kostenko S., Moens U. Heat shock protein 27 phosphorylation: kinases, phosphatases, functions and pathology. Cell. Mol. Life Sci. 2009, 66:3289-3307.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 3289-3307
    • Kostenko, S.1    Moens, U.2
  • 21
    • 0033145354 scopus 로고    scopus 로고
    • MAPKAP kinase 2 is essential for LPS-induced TNF-alpha biosynthesis
    • Kotlyarov A., et al. MAPKAP kinase 2 is essential for LPS-induced TNF-alpha biosynthesis. Nat. Cell Biol. 1999, 1:94-97.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 94-97
    • Kotlyarov, A.1
  • 22
    • 0032617026 scopus 로고    scopus 로고
    • Regulation of actin dynamics by stress-activated protein kinase 2 (SAPK2)-dependent phosphorylation of heat-shock protein of 27kDa (Hsp27)
    • Landry J., Huot J. Regulation of actin dynamics by stress-activated protein kinase 2 (SAPK2)-dependent phosphorylation of heat-shock protein of 27kDa (Hsp27). Biochem. Soc. Symp. 1999, 64:79-89.
    • (1999) Biochem. Soc. Symp. , vol.64 , pp. 79-89
    • Landry, J.1    Huot, J.2
  • 23
    • 0028924759 scopus 로고
    • Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27
    • Lavoie J.N., et al. Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. Mol. Cell. Biol. 1995, 15:505-516.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 505-516
    • Lavoie, J.N.1
  • 24
    • 2942756123 scopus 로고    scopus 로고
    • Receptor for advanced glycation end products (RAGE) regulates sepsis but not the adaptive immune response
    • Liliensiek B., et al. Receptor for advanced glycation end products (RAGE) regulates sepsis but not the adaptive immune response. J. Clin. Invest. 2004, 113:1641-1650.
    • (2004) J. Clin. Invest. , vol.113 , pp. 1641-1650
    • Liliensiek, B.1
  • 25
    • 0026348949 scopus 로고
    • The 29-kDa proteins phosphorylated in thrombin-activated human platelets are forms of the estrogen receptor-related 27-kDa heat shock protein
    • Mendelsohn M.E., et al. The 29-kDa proteins phosphorylated in thrombin-activated human platelets are forms of the estrogen receptor-related 27-kDa heat shock protein. Proc. Natl Acad. Sci. USA 1991, 88:11212-11216.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 11212-11216
    • Mendelsohn, M.E.1
  • 26
    • 0024437786 scopus 로고
    • Tumour necrosis factor in bronchopulmonary secretions of patients with adult respiratory distress syndrome
    • Millar A.B., et al. Tumour necrosis factor in bronchopulmonary secretions of patients with adult respiratory distress syndrome. Lancet 1989, 2:712-714.
    • (1989) Lancet , vol.2 , pp. 712-714
    • Millar, A.B.1
  • 27
    • 29644441337 scopus 로고    scopus 로고
    • Cutting edge: extracellular high mobility group box-1 protein is a proangiogenic cytokine
    • Mitola S., et al. Cutting edge: extracellular high mobility group box-1 protein is a proangiogenic cytokine. J. Immunol. 2006, 176:12-15.
    • (2006) J. Immunol. , vol.176 , pp. 12-15
    • Mitola, S.1
  • 28
    • 0036556697 scopus 로고    scopus 로고
    • Actin cytoskeleton and small heat shock proteins: how do they interact?
    • Mounier N., Arrigo A.P. Actin cytoskeleton and small heat shock proteins: how do they interact?. Cell Stress Chaperones 2002, 7:167-176.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 167-176
    • Mounier, N.1    Arrigo, A.P.2
  • 29
    • 0035503906 scopus 로고    scopus 로고
    • Albumin-derived advanced glycation end-products trigger the disruption of the vascular endothelial cadherin complex in cultured human and murine endothelial cells
    • Otero K., et al. Albumin-derived advanced glycation end-products trigger the disruption of the vascular endothelial cadherin complex in cultured human and murine endothelial cells. Biochem. J. 2001, 359:567-574.
    • (2001) Biochem. J. , vol.359 , pp. 567-574
    • Otero, K.1
  • 30
    • 0842266582 scopus 로고    scopus 로고
    • Extracellular HMGB1, a signal of tissue damage, induces mesoangioblast migration and proliferation
    • Palumbo R., et al. Extracellular HMGB1, a signal of tissue damage, induces mesoangioblast migration and proliferation. J. Cell Biol. 2004, 164:441-449.
    • (2004) J. Cell Biol. , vol.164 , pp. 441-449
    • Palumbo, R.1
  • 31
    • 0037376222 scopus 로고    scopus 로고
    • Activation of gene expression in human neutrophils by high mobility group box 1 protein
    • Park J.S., et al. Activation of gene expression in human neutrophils by high mobility group box 1 protein. Am. J. Physiol. Cell Physiol. 2003, 284:C870-C879.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.284
    • Park, J.S.1
  • 32
    • 33645461206 scopus 로고    scopus 로고
    • High mobility group box 1 protein interacts with multiple Toll-like receptors
    • Park J.S., et al. High mobility group box 1 protein interacts with multiple Toll-like receptors. Am. J. Physiol. Cell Physiol. 2006, 290:C917-C924.
    • (2006) Am. J. Physiol. Cell Physiol. , vol.290
    • Park, J.S.1
  • 33
    • 1542380035 scopus 로고    scopus 로고
    • Involvement of toll-like receptors 2 and 4 in cellular activation by high mobility group box 1 protein
    • Park J.S., et al. Involvement of toll-like receptors 2 and 4 in cellular activation by high mobility group box 1 protein. J. Biol. Chem. 2004, 279:7370-7377.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7370-7377
    • Park, J.S.1
  • 34
    • 0024468408 scopus 로고
    • Phallacidin prevents thrombin-induced increases in endothelial permeability to albumin
    • Phillips P.G., et al. Phallacidin prevents thrombin-induced increases in endothelial permeability to albumin. Am. J. Physiol. 1989, 257:C562-C567.
    • (1989) Am. J. Physiol. , vol.257
    • Phillips, P.G.1
  • 35
    • 3042730951 scopus 로고    scopus 로고
    • Control of actin dynamics by p38 MAP kinase-Hsp27 distribution in the lamellipodium of smooth muscle cells
    • Pichon S., et al. Control of actin dynamics by p38 MAP kinase-Hsp27 distribution in the lamellipodium of smooth muscle cells. J. Cell Sci. 2004, 117:2569-2577.
    • (2004) J. Cell Sci. , vol.117 , pp. 2569-2577
    • Pichon, S.1
  • 36
    • 33749437076 scopus 로고    scopus 로고
    • The role of RAGE in the pathogenesis of intestinal barrier dysfunction after hemorrhagic shock
    • Raman K.G., et al. The role of RAGE in the pathogenesis of intestinal barrier dysfunction after hemorrhagic shock. Am. J. Physiol. Gastrointest. Liver Physiol. 2006, 291:G556-G565.
    • (2006) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.291
    • Raman, K.G.1
  • 37
    • 0036724929 scopus 로고    scopus 로고
    • HMGB1 B box increases the permeability of Caco-2 enterocytic monolayers and impairs intestinal barrier function in mice
    • Sappington P.L., et al. HMGB1 B box increases the permeability of Caco-2 enterocytic monolayers and impairs intestinal barrier function in mice. Gastroenterology 2002, 123:790-802.
    • (2002) Gastroenterology , vol.123 , pp. 790-802
    • Sappington, P.L.1
  • 38
    • 0037636489 scopus 로고    scopus 로고
    • Role of sphingosine-1 phosphate in the enhancement of endothelial barrier integrity by platelet-released products
    • Schaphorst K.L., et al. Role of sphingosine-1 phosphate in the enhancement of endothelial barrier integrity by platelet-released products. Am. J. Physiol. Lung Cell. Mol. Physiol. 2003, 285:L258-L267.
    • (2003) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.285
    • Schaphorst, K.L.1
  • 39
    • 17144400438 scopus 로고    scopus 로고
    • Angiogenetic signaling through hypoxia: HMGB1: an angiogenetic switch molecule
    • Schlueter C., et al. Angiogenetic signaling through hypoxia: HMGB1: an angiogenetic switch molecule. Am. J. Pathol. 2005, 166:1259-1263.
    • (2005) Am. J. Pathol. , vol.166 , pp. 1259-1263
    • Schlueter, C.1
  • 40
    • 20144380566 scopus 로고    scopus 로고
    • Persistent elevation of high mobility group box-1 protein (HMGB1) in patients with severe sepsis and septic shock
    • Sunden-Cullberg J., et al. Persistent elevation of high mobility group box-1 protein (HMGB1) in patients with severe sepsis and septic shock. Crit. Care Med. 2005, 33:564-573.
    • (2005) Crit. Care Med. , vol.33 , pp. 564-573
    • Sunden-Cullberg, J.1
  • 41
    • 0026787392 scopus 로고
    • High bronchoalveolar levels of tumor necrosis factor and its inhibitors, interleukin-1, interferon, and elastase, in patients with adult respiratory distress syndrome after trauma, shock, or sepsis
    • Suter P.M., et al. High bronchoalveolar levels of tumor necrosis factor and its inhibitors, interleukin-1, interferon, and elastase, in patients with adult respiratory distress syndrome after trauma, shock, or sepsis. Am. Rev. Respir. Dis. 1992, 145:1016-1022.
    • (1992) Am. Rev. Respir. Dis. , vol.145 , pp. 1016-1022
    • Suter, P.M.1
  • 42
    • 0141750710 scopus 로고    scopus 로고
    • High mobility group 1 B-box mediates activation of human endothelium
    • Treutiger C.J., et al. High mobility group 1 B-box mediates activation of human endothelium. J. Intern. Med. 2003, 254:375-385.
    • (2003) J. Intern. Med. , vol.254 , pp. 375-385
    • Treutiger, C.J.1
  • 43
    • 10644244296 scopus 로고    scopus 로고
    • Contributions of high mobility group box protein in experimental and clinical acute lung injury
    • Ueno H., et al. Contributions of high mobility group box protein in experimental and clinical acute lung injury. Am. J. Respir. Crit. Care Med. 2004, 170:1310-1316.
    • (2004) Am. J. Respir. Crit. Care Med. , vol.170 , pp. 1310-1316
    • Ueno, H.1
  • 44
    • 0033538467 scopus 로고    scopus 로고
    • HMG-1 as a late mediator of endotoxin lethality in mice
    • Wang H., et al. HMG-1 as a late mediator of endotoxin lethality in mice. Science 1999, 285:248-251.
    • (1999) Science , vol.285 , pp. 248-251
    • Wang, H.1
  • 45
    • 33747649790 scopus 로고    scopus 로고
    • Pathophysiology of acute lung injury and the acute respiratory distress syndrome
    • Ware L.B. Pathophysiology of acute lung injury and the acute respiratory distress syndrome. Semin. Respir. Crit. Care Med. 2006, 27:337-349.
    • (2006) Semin. Respir. Crit. Care Med. , vol.27 , pp. 337-349
    • Ware, L.B.1
  • 46
    • 0030061699 scopus 로고    scopus 로고
    • Receptor-mediated endothelial cell dysfunction in diabetic vasculopathy. Soluble receptor for advanced glycation end products blocks hyperpermeability in diabetic rats
    • Wautier J.L., et al. Receptor-mediated endothelial cell dysfunction in diabetic vasculopathy. Soluble receptor for advanced glycation end products blocks hyperpermeability in diabetic rats. J. Clin. Invest. 1996, 97:238-243.
    • (1996) J. Clin. Invest. , vol.97 , pp. 238-243
    • Wautier, J.L.1
  • 47
    • 33746731651 scopus 로고    scopus 로고
    • HMGB1 signals through toll-like receptor (TLR) 4 and TLR2
    • Yu M., et al. HMGB1 signals through toll-like receptor (TLR) 4 and TLR2. Shock 2006, 26:174-179.
    • (2006) Shock , vol.26 , pp. 174-179
    • Yu, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.