메뉴 건너뛰기




Volumn 105, Issue 9, 2008, Pages 3545-3550

Overexpression of the dual-specificity phosphatase MKP-4/DUSP-9 protects against stress-induced insulin resistance

Author keywords

Cytokines; Diabetes; Kinases; Obesity

Indexed keywords

ANISOMYCIN; GLUCOSE TRANSPORTER 1; GLUCOSE TRANSPORTER 4; INSULIN RECEPTOR SUBSTRATE 1; INTERLEUKIN 6; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; MKP 4 ENZYME; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE B; SERINE; STRESS ACTIVATED PROTEIN KINASE; TUMOR NECROSIS FACTOR ALPHA; DUAL SPECIFICITY PHOSPHATASE; DUSP9 PROTEIN, MOUSE; INSULIN; UNCLASSIFIED DRUG;

EID: 42149155999     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0712275105     Document Type: Article
Times cited : (93)

References (33)
  • 1
    • 18244370762 scopus 로고    scopus 로고
    • Inflammation, stress, and diabetes
    • Wellen KE, Hotamisligil GS (2005) Inflammation, stress, and diabetes. J Clin Invest 115:1111-1119.
    • (2005) J Clin Invest , vol.115 , pp. 1111-1119
    • Wellen, K.E.1    Hotamisligil, G.S.2
  • 2
    • 0033773334 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha-mediated insulin resistance, but not dedifferentiation, is abrogated by MEK1/2 inhibitors in 3T3-L1 adipocytes
    • Engelman JA, Berg AH, Lewis RY, Lisanti MP, Scherer PE (2000) Tumor necrosis factor alpha-mediated insulin resistance, but not dedifferentiation, is abrogated by MEK1/2 inhibitors in 3T3-L1 adipocytes. Mol Endocrinol 14:1557-1569.
    • (2000) Mol Endocrinol , vol.14 , pp. 1557-1569
    • Engelman, J.A.1    Berg, A.H.2    Lewis, R.Y.3    Lisanti, M.P.4    Scherer, P.E.5
  • 3
    • 0034708832 scopus 로고    scopus 로고
    • The c-Jun NH (2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser(307)
    • Aguirre V, Uchida T, Yenush L, Davis R, White MF (2000) The c-Jun NH (2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser(307). J Biol Chem 275:9047-9054.
    • (2000) J Biol Chem , vol.275 , pp. 9047-9054
    • Aguirre, V.1    Uchida, T.2    Yenush, L.3    Davis, R.4    White, M.F.5
  • 4
    • 0037153158 scopus 로고    scopus 로고
    • A central role for JNK in obesity and insulin resistance
    • Hirosumi J, et al. (2002) A central role for JNK in obesity and insulin resistance. Nature 420:333-336.
    • (2002) Nature , vol.420 , pp. 333-336
    • Hirosumi, J.1
  • 5
    • 0037339991 scopus 로고    scopus 로고
    • Three mitogen-activated protein kinases inhibit insulin signaling by different mechanisms in 3T3-L1 adipocytes
    • Fujishiro M, et al. (2003) Three mitogen-activated protein kinases inhibit insulin signaling by different mechanisms in 3T3-L1 adipocytes. Mol Endocrinol 17:487-497.
    • (2003) Mol Endocrinol , vol.17 , pp. 487-497
    • Fujishiro, M.1
  • 6
    • 0037059330 scopus 로고    scopus 로고
    • Phosphorylation of Ser307 in insulin receptor substrate-1 blocks interactions with the insulin receptor and inhibits insulin action
    • Aguirre V, et al. (2002) Phosphorylation of Ser307 in insulin receptor substrate-1 blocks interactions with the insulin receptor and inhibits insulin action. J Biol Chem 277:1531-1537.
    • (2002) J Biol Chem , vol.277 , pp. 1531-1537
    • Aguirre, V.1
  • 7
    • 7044230885 scopus 로고    scopus 로고
    • Possible novel therapy for diabetes with cell-permeable JNK-inhibitory peptide
    • Kaneto H, et al. (2004) Possible novel therapy for diabetes with cell-permeable JNK-inhibitory peptide. Nat Med 10:1128-1132.
    • (2004) Nat Med , vol.10 , pp. 1128-1132
    • Kaneto, H.1
  • 8
    • 0038004740 scopus 로고    scopus 로고
    • Targeting JNK for therapeutic benefit: From junk to gold?
    • Manning AM, Davis RJ (2003) Targeting JNK for therapeutic benefit: From junk to gold? Nat Rev Drug Discov 2:554-565.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 554-565
    • Manning, A.M.1    Davis, R.J.2
  • 9
    • 34248595035 scopus 로고    scopus 로고
    • Differential regulation of MAP kinase signalling by dual-specificity protein phosphatases
    • Owens DM, Keyse SM (2007) Differential regulation of MAP kinase signalling by dual-specificity protein phosphatases. Oncogene 26:3203-3213.
    • (2007) Oncogene , vol.26 , pp. 3203-3213
    • Owens, D.M.1    Keyse, S.M.2
  • 10
    • 2042538029 scopus 로고    scopus 로고
    • Structure and regulation of MAPK phosphatases
    • Farooq A, Zhou MM (2004) Structure and regulation of MAPK phosphatases. Cell Signal 16:769-779.
    • (2004) Cell Signal , vol.16 , pp. 769-779
    • Farooq, A.1    Zhou, M.M.2
  • 11
    • 0036709020 scopus 로고    scopus 로고
    • Fidelity and spatio-temporal control in MAP kinase (ERKs) signalling
    • Pouyssegur J, Volmat V, Lenormand P (2002) Fidelity and spatio-temporal control in MAP kinase (ERKs) signalling. Biochem Pharmacol 64:755-763.
    • (2002) Biochem Pharmacol , vol.64 , pp. 755-763
    • Pouyssegur, J.1    Volmat, V.2    Lenormand, P.3
  • 12
    • 0032557632 scopus 로고    scopus 로고
    • Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase
    • Camps M, et al. (1998) Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase. Science 280:1262-1265.
    • (1998) Science , vol.280 , pp. 1262-1265
    • Camps, M.1
  • 13
    • 14844327760 scopus 로고    scopus 로고
    • Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases
    • Kamata H, et al. (2005) Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 120:649-661.
    • (2005) Cell , vol.120 , pp. 649-661
    • Kamata, H.1
  • 14
    • 0042530516 scopus 로고    scopus 로고
    • Dual specificity mitogen-activated protein (MAP) kinase phosphatase-4 plays a potential role in insulin resistance
    • Xu H, et al. (2003) Dual specificity mitogen-activated protein (MAP) kinase phosphatase-4 plays a potential role in insulin resistance. J Biol Chem 278:30187-30192.
    • (2003) J Biol Chem , vol.278 , pp. 30187-30192
    • Xu, H.1
  • 15
    • 0030028222 scopus 로고    scopus 로고
    • MKP-3, a novel cytosolic protein-tyrosine phosphatase that exemplifies a new class of mitogen-activated protein kinase phosphatase
    • Muda M, et al. (1996) MKP-3, a novel cytosolic protein-tyrosine phosphatase that exemplifies a new class of mitogen-activated protein kinase phosphatase. J Biol Chem 271:4319-4326.
    • (1996) J Biol Chem , vol.271 , pp. 4319-4326
    • Muda, M.1
  • 16
    • 18944375291 scopus 로고    scopus 로고
    • The noncatalytic amino terminus of mitogen-activated protein kinase phosphatase 1 directs nuclear targeting and serum response element transcriptional regulation
    • Wu JJ, Zhang L, Bennett AM (2005) The noncatalytic amino terminus of mitogen-activated protein kinase phosphatase 1 directs nuclear targeting and serum response element transcriptional regulation. Mol Cell Biol 25:4792-4803.
    • (2005) Mol Cell Biol , vol.25 , pp. 4792-4803
    • Wu, J.J.1    Zhang, L.2    Bennett, A.M.3
  • 17
    • 0035914379 scopus 로고    scopus 로고
    • MKP-7, a novel mitogen-activated protein kinase phosphatase, functions as a shuttle protein
    • Masuda K, Shima H, Watanabe M, Kikuchi K (2001) MKP-7, a novel mitogen-activated protein kinase phosphatase, functions as a shuttle protein. J Biol Chem 276:39002-39011.
    • (2001) J Biol Chem , vol.276 , pp. 39002-39011
    • Masuda, K.1    Shima, H.2    Watanabe, M.3    Kikuchi, K.4
  • 18
    • 15144352589 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of a novel mitogen-activated protein kinase phosphatase, MKP-4
    • Muda M, et al. (1997) Molecular cloning and functional characterization of a novel mitogen-activated protein kinase phosphatase, MKP-4. J Biol Chem 272:5141-5151.
    • (1997) J Biol Chem , vol.272 , pp. 5141-5151
    • Muda, M.1
  • 19
    • 0030458404 scopus 로고    scopus 로고
    • Negative regulation of peroxisome proliferator-activated receptor-gamma gene expression contributes to the antiadipogenic effects of tumor necrosis factor-alpha
    • Zhang B, et al. (1996) Negative regulation of peroxisome proliferator-activated receptor-gamma gene expression contributes to the antiadipogenic effects of tumor necrosis factor-alpha. Mol Endocrinol 10:1457-1466.
    • (1996) Mol Endocrinol , vol.10 , pp. 1457-1466
    • Zhang, B.1
  • 20
    • 0348107406 scopus 로고    scopus 로고
    • Regulation of adipocytokines and insulin resistance
    • Fasshauer M, Paschke R (2003) Regulation of adipocytokines and insulin resistance. Diabetologia 46:1594-1603.
    • (2003) Diabetologia , vol.46 , pp. 1594-1603
    • Fasshauer, M.1    Paschke, R.2
  • 21
    • 0025837140 scopus 로고
    • Transcriptional repression of the GLUT4 and C/EBP genes in 3T3-L1 adipocytes by tumor necrosis factor-alpha
    • Stephens JM, Pekala PH (1991) Transcriptional repression of the GLUT4 and C/EBP genes in 3T3-L1 adipocytes by tumor necrosis factor-alpha. J Biol Chem 266:21839-21845.
    • (1991) J Biol Chem , vol.266 , pp. 21839-21845
    • Stephens, J.M.1    Pekala, P.H.2
  • 22
    • 0026646608 scopus 로고
    • Tumor necrosis factor alpha-induced glucose transporter (GLUT-1) mRNA stabilization in 3T3-L1 preadipocytes. Regulation by the adenosine-uridine binding factor
    • Stephens JM, Carter BZ, Pekala PH, Malter JS (1992) Tumor necrosis factor alpha-induced glucose transporter (GLUT-1) mRNA stabilization in 3T3-L1 preadipocytes. Regulation by the adenosine-uridine binding factor. J Biol Chem 267:8336-8341.
    • (1992) J Biol Chem , vol.267 , pp. 8336-8341
    • Stephens, J.M.1    Carter, B.Z.2    Pekala, P.H.3    Malter, J.S.4
  • 23
    • 0038517834 scopus 로고    scopus 로고
    • Antisense protein tyrosine phosphatase 1B reverses activation of p38 mitogen-activated protein kinase in liver of ob/ob mice
    • Gum RJ, et al. (2003) Antisense protein tyrosine phosphatase 1B reverses activation of p38 mitogen-activated protein kinase in liver of ob/ob mice. Mol Endocrinol 17:1131-1143.
    • (2003) Mol Endocrinol , vol.17 , pp. 1131-1143
    • Gum, R.J.1
  • 24
    • 0037341276 scopus 로고    scopus 로고
    • Enhanced basal activation of mitogen-activated protein kinases in adipocytes from type 2 diabetes: Potential role of p38 in the downregulation of GLUT4 expression
    • Carlson CJ, Koterski S, Sciotti RJ, Poccard GB, Rondinone CM (2003) Enhanced basal activation of mitogen-activated protein kinases in adipocytes from type 2 diabetes: potential role of p38 in the downregulation of GLUT4 expression. Diabetes 52:634-641.
    • (2003) Diabetes , vol.52 , pp. 634-641
    • Carlson, C.J.1    Koterski, S.2    Sciotti, R.J.3    Poccard, G.B.4    Rondinone, C.M.5
  • 25
    • 24344455502 scopus 로고    scopus 로고
    • The dual-specificity protein phosphatase DUSP9/MKP-4 is essential for placental function but is not required for normal embryonic development
    • Christie GR, et al. (2005) The dual-specificity protein phosphatase DUSP9/MKP-4 is essential for placental function but is not required for normal embryonic development. Mol Cell Biol 25:8323-8333.
    • (2005) Mol Cell Biol , vol.25 , pp. 8323-8333
    • Christie, G.R.1
  • 26
    • 4544222907 scopus 로고    scopus 로고
    • Role of MAPK phosphatase-1 (MKP-1) in adipocyte differentiation
    • Sakaue H, et al. (2004) Role of MAPK phosphatase-1 (MKP-1) in adipocyte differentiation. J Biol Chem 279:39951-39957.
    • (2004) J Biol Chem , vol.279 , pp. 39951-39957
    • Sakaue, H.1
  • 27
    • 19944433322 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase isoform ERK1 is specifically required for in vitro and in vivo adipogenesis
    • Bost F, et al. (2005) The extracellular signal-regulated kinase isoform ERK1 is specifically required for in vitro and in vivo adipogenesis. Diabetes 54:402-411.
    • (2005) Diabetes , vol.54 , pp. 402-411
    • Bost, F.1
  • 28
    • 23844543478 scopus 로고    scopus 로고
    • Reduction of insulin-stimulated glucose uptake in L6 myotubes by the protein kinase inhibitor SB203580 is independent of p38MAPK activity
    • Antonescu CN, et al. (2005) Reduction of insulin-stimulated glucose uptake in L6 myotubes by the protein kinase inhibitor SB203580 is independent of p38MAPK activity. Endocrinology 146:3773-3781.
    • (2005) Endocrinology , vol.146 , pp. 3773-3781
    • Antonescu, C.N.1
  • 29
    • 0347721775 scopus 로고    scopus 로고
    • A dominant-negative p38 MAPK mutant and novel selective inhibitors of p38 MAPK reduce insulin-stimulated glucose uptake in 3T3-L1 adipocytes without affecting GLUT4 translocation
    • Somwar R, et al. (2002) A dominant-negative p38 MAPK mutant and novel selective inhibitors of p38 MAPK reduce insulin-stimulated glucose uptake in 3T3-L1 adipocytes without affecting GLUT4 translocation. J Biol Chem 277:50386-50395.
    • (2002) J Biol Chem , vol.277 , pp. 50386-50395
    • Somwar, R.1
  • 30
    • 0034967147 scopus 로고    scopus 로고
    • Construction of stable coxsackievirus and adenovirus receptor-expressing 3T3-L1 cells
    • Orlicky DJ, DeGregori J, Schaack J (2001) Construction of stable coxsackievirus and adenovirus receptor-expressing 3T3-L1 cells. J Lipid Res 42:910-915.
    • (2001) J Lipid Res , vol.42 , pp. 910-915
    • Orlicky, D.J.1    DeGregori, J.2    Schaack, J.3
  • 31
    • 0033521022 scopus 로고    scopus 로고
    • Beta(3)-adrenergic stimulation differentially inhibits insulin signaling and decreases insulin induced glucose uptake in brown adipocytes
    • Klein J, et al. (1999) Beta(3)-adrenergic stimulation differentially inhibits insulin signaling and decreases insulin induced glucose uptake in brown adipocytes. J Biol Chem 274:34795-34802.
    • (1999) J Biol Chem , vol.274 , pp. 34795-34802
    • Klein, J.1
  • 32
    • 0034717062 scopus 로고    scopus 로고
    • SOCS-3 is an insulin-induced negative regulator of insulin signaling
    • Emanuelli B, et al. (2000) SOCS-3 is an insulin-induced negative regulator of insulin signaling. J Biol Chem 275:15985-15991.
    • (2000) J Biol Chem , vol.275 , pp. 15985-15991
    • Emanuelli, B.1
  • 33
    • 0030595132 scopus 로고    scopus 로고
    • Overexpression of Rad inhibits glucose uptake in cultured muscle and fat cells
    • Moyers JS, Bilan PJ, Reynet C, Kahn CR (1996) Overexpression of Rad inhibits glucose uptake in cultured muscle and fat cells. J Biol Chem 271:23111-23116.
    • (1996) J Biol Chem , vol.271 , pp. 23111-23116
    • Moyers, J.S.1    Bilan, P.J.2    Reynet, C.3    Kahn, C.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.