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Volumn 287, Issue 5 31-5, 2004, Pages

p38 MAP kinase-dependent regulation of endothelial cell permeability

Author keywords

Caldesmon; p38 mitogen activated protein kinase; Thrombin; Transendothelial electrical resistance

Indexed keywords

4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; ACTIN BINDING PROTEIN; ADENOVIRUS VECTOR; CALDESMON; MITOGEN ACTIVATED PROTEIN KINASE P38; MYOSIN LIGHT CHAIN KINASE; THROMBIN;

EID: 6344254520     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.00372.2003     Document Type: Article
Times cited : (103)

References (45)
  • 1
    • 0028071812 scopus 로고
    • Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity
    • Benndorf R, Hayess K, Ryazantsev S, Wieske M, Behlke J, and Lutsch G. Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity. J Biol Chem 269: 20780-20784, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 20780-20784
    • Benndorf, R.1    Hayess, K.2    Ryazantsev, S.3    Wieske, M.4    Behlke, J.5    Lutsch, G.6
  • 3
    • 0035039649 scopus 로고    scopus 로고
    • Regulation of endothelial cell barrier function by calcium/calmodulin- dependent protein kinase II
    • Borbiev T, Verin AD, Shi S, Liu F, and Garcia JG. Regulation of endothelial cell barrier function by calcium/calmodulin-dependent protein kinase II. Am J Physiol Lung Cell Mol Physiol 280: L983-L990, 2001.
    • (2001) Am J Physiol Lung Cell Mol Physiol , vol.280
    • Borbiev, T.1    Verin, A.D.2    Shi, S.3    Liu, F.4    Garcia, J.G.5
  • 4
    • 0033570095 scopus 로고    scopus 로고
    • Mammal-specific, ERK-dependent, caldesmon phosphorylation in smooth muscle. Quantitation using novel anti-phosphopeptide antibodies
    • D'Angelo G, Graceffa P, Wang CA, Wrangle J, and Adam LP. Mammal-specific, ERK-dependent, caldesmon phosphorylation in smooth muscle. Quantitation using novel anti-phosphopeptide antibodies. J Biol Chem 274: 30115-30121, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 30115-30121
    • D'Angelo, G.1    Graceffa, P.2    Wang, C.A.3    Wrangle, J.4    Adam, L.P.5
  • 5
    • 0032496421 scopus 로고    scopus 로고
    • Pervanadate inhibits mitogen-activated protein kinase kinase-1 in a p38MAPK-dependent manner
    • Daum G, Kalmes A, Levkau B, Wang Y, Davies MG, and Clowes AW. Pervanadate inhibits mitogen-activated protein kinase kinase-1 in a p38MAPK-dependent manner. FEBS Lett 427: 271-274, 1998.
    • (1998) FEBS Lett , vol.427 , pp. 271-274
    • Daum, G.1    Kalmes, A.2    Levkau, B.3    Wang, Y.4    Davies, M.G.5    Clowes, A.W.6
  • 6
    • 0031722643 scopus 로고    scopus 로고
    • A role for MAP kinase in differentiated smooth muscle contraction evoked by α-adrenoceptor stimulation
    • Dessy C, Kim I, Sougnez CL, Laporte R, and Morgan KG. A role for MAP kinase in differentiated smooth muscle contraction evoked by α-adrenoceptor stimulation. Am J Physiol Cell Physiol 275: C1081-C1086, 1998.
    • (1998) Am J Physiol Cell Physiol , vol.275
    • Dessy, C.1    Kim, I.2    Sougnez, C.L.3    Laporte, R.4    Morgan, K.G.5
  • 7
    • 0034807581 scopus 로고    scopus 로고
    • Cytoskeletal regulation of pulmonary vascular permeability
    • Dudek SM and Garcia JG. Cytoskeletal regulation of pulmonary vascular permeability. J Appl Physiol 91: 1487-1500, 2001.
    • (2001) J Appl Physiol , vol.91 , pp. 1487-1500
    • Dudek, S.M.1    Garcia, J.G.2
  • 9
    • 0032102902 scopus 로고    scopus 로고
    • Conversion of SB 203580-insensitive MAP kinase family members to drug-sensitive forms by a single amino-acid substitution
    • Eyers PA, Craxton M, Morrice N, Cohen P, and Goedert M. Conversion of SB 203580-insensitive MAP kinase family members to drug-sensitive forms by a single amino-acid substitution. Chem Biol 5: 321-328, 1998.
    • (1998) Chem Biol , vol.5 , pp. 321-328
    • Eyers, P.A.1    Craxton, M.2    Morrice, N.3    Cohen, P.4    Goedert, M.5
  • 10
    • 0029012398 scopus 로고
    • Regulation of endothelial cell gap formation and barrier dysfunction: Role of myosin light chain phosphorylation
    • Garcia JG, Davis HW, and Patterson CE. Regulation of endothelial cell gap formation and barrier dysfunction: role of myosin light chain phosphorylation. J Cell Physiol 163: 510-522, 1995.
    • (1995) J Cell Physiol , vol.163 , pp. 510-522
    • Garcia, J.G.1    Davis, H.W.2    Patterson, C.E.3
  • 11
    • 0029283128 scopus 로고
    • Regulation of endothelial cell gap formation and paracellular permeability
    • Garcia JG and Schaphorst KL. Regulation of endothelial cell gap formation and paracellular permeability. J Investig Med 43: 117-126, 1995.
    • (1995) J Investig Med , vol.43 , pp. 117-126
    • Garcia, J.G.1    Schaphorst, K.L.2
  • 13
    • 0037083375 scopus 로고    scopus 로고
    • MAPKK-independent activation of p38α mediated by TAB1-dependent autophosphorylation of p38α
    • Ge B, Gram H, Padova DI, Huang B, New L, Ulevitch RJ, Luo Y, and Han J. MAPKK-independent activation of p38α mediated by TAB1-dependent autophosphorylation of p38α. Science 295: 1291-1294, 2002.
    • (2002) Science , vol.295 , pp. 1291-1294
    • Ge, B.1    Gram, H.2    Padova, D.I.3    Huang, B.4    New, L.5    Ulevitch, R.J.6    Luo, Y.7    Han, J.8
  • 16
    • 0029119895 scopus 로고
    • Myosin light chain kinase-regulated endothelial cell contraction: The relationship between isomeric tension, actin polymerization, and myosin phosphorylation
    • Goeckeler ZM and Wysolmerski RB. Myosin light chain kinase-regulated endothelial cell contraction: the relationship between isomeric tension, actin polymerization, and myosin phosphorylation. J Cell Biol 130: 613-627, 1995.
    • (1995) J Cell Biol , vol.130 , pp. 613-627
    • Goeckeler, Z.M.1    Wysolmerski, R.B.2
  • 18
    • 0031056783 scopus 로고    scopus 로고
    • Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27
    • Guay J, Lambert H, Gingras-Breton G, Lavoie JN, Huot J, and Landry J. Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27. J Cell Sci 110: 357-368, 1997.
    • (1997) J Cell Sci , vol.110 , pp. 357-368
    • Guay, J.1    Lambert, H.2    Gingras-Breton, G.3    Lavoie, J.N.4    Huot, J.5    Landry, J.6
  • 19
    • 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 KK, Trollinger D, Rihanek M, and Manthey CL. Differential expression and activation of p38 mitogen-activated protein kinase alpha, beta, gamma, and delta in inflammatory cell lineages. J Immunol 162: 4246-4252, 1999.
    • (1999) J Immunol , vol.162 , pp. 4246-4252
    • Hale, K.K.1    Trollinger, D.2    Rihanek, M.3    Manthey, C.L.4
  • 23
    • 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, Houle F, Marceau F, and Landry J. Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/ heat shock protein 27 pathway in vascular endothelial cells. Circ Res 80: 383-392, 1997.
    • (1997) Circ Res , vol.80 , pp. 383-392
    • Huot, J.1    Houle, F.2    Marceau, F.3    Landry, J.4
  • 24
    • 0032583203 scopus 로고    scopus 로고
    • SAPK2/p38-dependent F-actin reorganization regulates early membrane blebbing during stress-induced apoptosis
    • Huot J, Houle F, Rousseau S, Deschesnes RG, Shah GM, and Landry J. SAPK2/p38-dependent F-actin reorganization regulates early membrane blebbing during stress-induced apoptosis. J Cell Biol 143: 1361-1373, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 1361-1373
    • Huot, J.1    Houle, F.2    Rousseau, S.3    Deschesnes, R.G.4    Shah, G.M.5    Landry, J.6
  • 26
    • 0033043630 scopus 로고    scopus 로고
    • Rat-1 is activated by the p38 mitogen-activated protein kinase inhibitor, SB 203580
    • Kalmes A, Deou J, Clowes AW, and Daum G. Rat-1 is activated by the p38 mitogen-activated protein kinase inhibitor, SB203580. FEBS Lett 444: 71-74, 1999.
    • (1999) FEBS Lett , vol.444 , pp. 71-74
    • Kalmes, A.1    Deou, J.2    Clowes, A.W.3    Daum, G.4
  • 27
    • 0035896223 scopus 로고    scopus 로고
    • Thrombin activates p38 mitogen-activated protein kinase in vascular smooth muscle cells
    • Kanda Y, Nishio E, Kuroki Y, Mizuno K, and Watanabe Y. Thrombin activates p38 mitogen-activated protein kinase in vascular smooth muscle cells. Life Sci 68: 1989-2000, 2001.
    • (2001) Life Sci , vol.68 , pp. 1989-2000
    • Kanda, Y.1    Nishio, E.2    Kuroki, Y.3    Mizuno, K.4    Watanabe, Y.5
  • 28
    • 0037044735 scopus 로고    scopus 로고
    • Cytoskeletal changes in hypoxic pulmonary endothelial cells are dependent on MAPK-activated protein kinase MK2
    • Kayyali US, Pennella CM, Trujillo C, Villa O, Gaestel M, and Hassoun PM. Cytoskeletal changes in hypoxic pulmonary endothelial cells are dependent on MAPK-activated protein kinase MK2. J Biol Chem 277: 42596-42602, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 42596-42602
    • Kayyali, U.S.1    Pennella, C.M.2    Trujillo, C.3    Villa, O.4    Gaestel, M.5    Hassoun, P.M.6
  • 29
    • 0033515597 scopus 로고    scopus 로고
    • HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus
    • Lambert H, Charette SJ, Bernier AF, Guimond A, and Landry J. HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus. J Biol Chem 274: 9378-9385, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 9378-9385
    • Lambert, H.1    Charette, S.J.2    Bernier, A.F.3    Guimond, A.4    Landry, J.5
  • 30
    • 0032617026 scopus 로고    scopus 로고
    • Regulation of actin dynamics by stress-activated protein kinase 2 (SAPK2)-dependent phosphorylation of heat-shock protein of 27 kDa (Hsp27)
    • Landry J and Huot J. Regulation of actin dynamics by stress-activated protein kinase 2 (SAPK2)-dependent phosphorylation of heat-shock protein of 27 kDa (Hsp27). Biochem Soc Symp 64: 79-89, 1999.
    • (1999) Biochem Soc Symp , vol.64 , pp. 79-89
    • Landry, J.1    Huot, J.2
  • 31
    • 0021889823 scopus 로고
    • Thrombin-induced alterations in lung fluid balance in awake sheep
    • Lo SK, Perlman MB, Niehaus GD, and Malik AB. Thrombin-induced alterations in lung fluid balance in awake sheep. J Appl Physiol 58: 1421-1427, 1985.
    • (1985) J Appl Physiol , vol.58 , pp. 1421-1427
    • Lo, S.K.1    Perlman, M.B.2    Niehaus, G.D.3    Malik, A.B.4
  • 32
    • 0033965158 scopus 로고    scopus 로고
    • The p38 signal transduction pathway: Activation and function
    • Ono K and Han J. The p38 signal transduction pathway: activation and function. Cell Signal 12: 1-13, 2000.
    • (2000) Cell Signal , vol.12 , pp. 1-13
    • Ono, K.1    Han, J.2
  • 34
    • 0031734967 scopus 로고    scopus 로고
    • Heat shock protein 27 kDa expression and phosphorylation regulates endothelial cell migration
    • Piotrowicz RS, Hickey E, and Levin EG. Heat shock protein 27 kDa expression and phosphorylation regulates endothelial cell migration. FASEB J 12: 1481-1490, 1998.
    • (1998) FASEB J , vol.12 , pp. 1481-1490
    • Piotrowicz, R.S.1    Hickey, E.2    Levin, E.G.3
  • 36
    • 0031772351 scopus 로고    scopus 로고
    • In vivo evaluation of hsp27 as an inhibitor of actin polymerization: hsp 27 limits actin stress fiber and focal adhesion formation after heat shock
    • Schneider GB, Hamano H, and Cooper LF. In vivo evaluation of hsp27 as an inhibitor of actin polymerization: hsp27 limits actin stress fiber and focal adhesion formation after heat shock. J Cell Physiol 177: 575-584, 1998.
    • (1998) J Cell Physiol , vol.177 , pp. 575-584
    • Schneider, G.B.1    Hamano, H.2    Cooper, L.F.3
  • 37
    • 0025900837 scopus 로고
    • Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems
    • Sobue K and Sellers JR. Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems. J Biol Chem 266: 12115-12118, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 12115-12118
    • Sobue, K.1    Sellers, J.R.2
  • 38
    • 0026781107 scopus 로고
    • Protein kinase C phosphorylates caldesmon 77 and vimentin and enhances albumin permeability across cultured bovine pulmonary artery endothelial cell monolayers
    • Stasek JE Jr, Patterson CE, and Garcia JG. Protein kinase C phosphorylates caldesmon77 and vimentin and enhances albumin permeability across cultured bovine pulmonary artery endothelial cell monolayers. J Cell Physiol 153: 62-75, 1992.
    • (1992) J Cell Physiol , vol.153 , pp. 62-75
    • Stasek Jr., J.E.1    Patterson, C.E.2    Garcia, J.G.3
  • 42
    • 0030434253 scopus 로고    scopus 로고
    • Serotonin activates the mitogen-activated protein kinase pathway in vascular smooth muscle: Use of the mitogen-activated protein kinase kinase inhibitor PD098059
    • Watts SW. Serotonin activates the mitogen-activated protein kinase pathway in vascular smooth muscle: use of the mitogen-activated protein kinase kinase inhibitor PD098059. J Pharmacol Exp Ther 279: 1541-1550, 1996.
    • (1996) J Pharmacol Exp Ther , vol.279 , pp. 1541-1550
    • Watts, S.W.1
  • 43
    • 0025186832 scopus 로고
    • Involvement of myosin light-chain kinase in endothelial cell retraction
    • Wysolmerski RB and Lagunoff D. Involvement of myosin light-chain kinase in endothelial cell retraction. Proc Natl Acad Sci USA 87: 16-20, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 16-20
    • Wysolmerski, R.B.1    Lagunoff, D.2
  • 44
    • 0025743578 scopus 로고
    • Regulation of permeabilized endothelial cell retraction by myosin phosphorylation
    • Wysolmerski RB and Lagunoff D. Regulation of permeabilized endothelial cell retraction by myosin phosphorylation. Am J Physiol Cell Physiol 261: C32-C40, 1991.
    • (1991) Am J Physiol Cell Physiol , vol.261
    • Wysolmerski, R.B.1    Lagunoff, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.