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Volumn 153, Issue 12, 2012, Pages 5821-5833

TNF-α up-regulates protein level and cell surface expression of the leptin receptor by stimulating its export via a PKC-dependent mechanism

Author keywords

[No Author keywords available]

Indexed keywords

4 O METHYLPHORBOL 13 ACETATE 12 MYRISTATE; BREFELDIN A; CADHERIN; LEPTIN RECEPTOR; PROTEIN KINASE C; STAT3 PROTEIN; TRANSFERRIN RECEPTOR; TUMOR NECROSIS FACTOR ALPHA;

EID: 84870172217     PISSN: 00137227     EISSN: 19457170     Source Type: Journal    
DOI: 10.1210/en.2012-1510     Document Type: Article
Times cited : (44)

References (59)
  • 2
    • 58149480226 scopus 로고    scopus 로고
    • Molecular physiology of weight regulation in mice and humans
    • Lond
    • Leibel RL 2008 Molecular physiology of weight regulation in mice and humans. Int J Obes (Lond) 32:S98-S108
    • (2008) Int J Obes , vol.32
    • Leibel, R.L.1
  • 4
    • 0032572722 scopus 로고    scopus 로고
    • Leptin modulates the T-cell immune response and reverses starvation-induced immunosuppression
    • Lord GM, Matarese G, Howard JK, Baker RJ, Bloom SR, Lechler RI 1998 Leptin modulates the T-cell immune response and reverses starvation-induced immunosuppression. Nature 394:897-901
    • (1998) Nature , vol.394 , pp. 897-901
    • Lord, G.M.1    Matarese, G.2    Howard, J.K.3    Baker, R.J.4    Bloom, S.R.5    Lechler, R.I.6
  • 8
    • 0033521601 scopus 로고    scopus 로고
    • Leptin is an endogenous protective protein against the toxicity exerted by tumor necrosis factor
    • Takahashi N, Waelput W, Guisez Y 1999 Leptin is an endogenous protective protein against the toxicity exerted by tumor necrosis factor. J Exp Med 189:207-212
    • (1999) J Exp Med , vol.189 , pp. 207-212
    • Takahashi, N.1    Waelput, W.2    Guisez, Y.3
  • 13
    • 0030685790 scopus 로고    scopus 로고
    • Fine structure of the murine leptin receptor gene: Splice site suppression is required to form two alternatively spliced transcripts
    • Chua Jr SC, Koutras IK, Han L, Liu SM, Kay J, Young SJ, Chung WK, Leibel RL 1997 Fine structure of the murine leptin receptor gene: splice site suppression is required to form two alternatively spliced transcripts. Genomics 45:264-270
    • (1997) Genomics , vol.45 , pp. 264-270
    • Chua Jr., S.C.1    Koutras, I.K.2    Han, L.3    Liu, S.M.4    Kay, J.5    Young, S.J.6    Chung, W.K.7    Leibel, R.L.8
  • 18
    • 0035794211 scopus 로고    scopus 로고
    • Modulation of circulating leptin levels by its soluble receptor
    • Huang L, Wang Z, Li C 2001 Modulation of circulating leptin levels by its soluble receptor. J Biol Chem 276:6343-6349
    • (2001) J Biol Chem , vol.276 , pp. 6343-6349
    • Huang, L.1    Wang, Z.2    Li, C.3
  • 19
    • 2542450776 scopus 로고    scopus 로고
    • Modulation of direct leptin signaling by soluble leptin receptor
    • Yang G, Ge H, Boucher A, Yu X, Li C 2004 Modulation of direct leptin signaling by soluble leptin receptor. Mol Endocrinol 18:1354-1362
    • (2004) Mol Endocrinol , vol.18 , pp. 1354-1362
    • Yang, G.1    Ge, H.2    Boucher, A.3    Yu, X.4    Li, C.5
  • 21
  • 23
    • 0037195916 scopus 로고    scopus 로고
    • Generation of soluble leptin receptor by ectodomain shedding of membrane-spanning receptors in vitro and in vivo
    • Ge H, Huang L, Pourbahrami T, Li C 2002 Generation of soluble leptin receptor by ectodomain shedding of membrane-spanning receptors in vitro and in vivo. J Biol Chem 277:45898-45903
    • (2002) J Biol Chem , vol.277 , pp. 45898-45903
    • Ge, H.1    Huang, L.2    Pourbahrami, T.3    Li, C.4
  • 24
    • 3142546889 scopus 로고    scopus 로고
    • Low levels of expression of leptin receptor at the cell surface result from constitutive endocytosis and intracellular retention in the biosynthetic pathway
    • Belouzard S, Delcroix D, Rouillé Y 2004 Low levels of expression of leptin receptor at the cell surface result from constitutive endocytosis and intracellular retention in the biosynthetic pathway. J Biol Chem 279:28499-28508
    • (2004) J Biol Chem , vol.279 , pp. 28499-28508
    • Belouzard, S.1    Delcroix, D.2    Rouillé, Y.3
  • 25
    • 0033597897 scopus 로고    scopus 로고
    • Subcellular localization and internalization of the four human leptin receptor isoforms
    • Barr VA, Lane K, Taylor SI 1999 Subcellular localization and internalization of the four human leptin receptor isoforms. J Biol Chem 274:21416-21424
    • (1999) J Biol Chem , vol.274 , pp. 21416-21424
    • Barr, V.A.1    Lane, K.2    Taylor, S.I.3
  • 27
    • 0031821377 scopus 로고    scopus 로고
    • Leptin receptor immunoreactivity is associated with the Golgi apparatus of hypothalamic neurons and glial cells
    • Diano S, Kalra SP, Horvath TL 1998 Leptin receptor immunoreactivity is associated with the Golgi apparatus of hypothalamic neurons and glial cells. J Neuroendocrinol 10:647-650
    • (1998) J Neuroendocrinol , vol.10 , pp. 647-650
    • Diano, S.1    Kalra, S.P.2    Horvath, T.L.3
  • 28
    • 0034639235 scopus 로고    scopus 로고
    • Expression and intracellular localization of leptin receptor long isoform-GFP chimera
    • Lundin A, Rondahl H, Walum E, Wilcke M 2000 Expression and intracellular localization of leptin receptor long isoform-GFP chimera. Biochim Biophys Acta 1499:130-138
    • (2000) Biochim Biophys Acta , vol.1499 , pp. 130-138
    • Lundin, A.1    Rondahl, H.2    Walum, E.3    Wilcke, M.4
  • 29
    • 0033008075 scopus 로고    scopus 로고
    • Functional properties of leptin receptor isoforms: Internalization and degradation of leptin and ligand-induced receptor downregulation
    • Uotani S, Bjørbaek C, Tornøe J, Flier JS 1999 Functional properties of leptin receptor isoforms: internalization and degradation of leptin and ligand-induced receptor downregulation. Diabetes 48:279-286
    • (1999) Diabetes , vol.48 , pp. 279-286
    • Uotani, S.1    Bjørbaek, C.2    Tornøe, J.3    Flier, J.S.4
  • 30
    • 0034510317 scopus 로고    scopus 로고
    • Characterization of leptin intracellular trafficking
    • Wilcke M, Walum E 2000 Characterization of leptin intracellular trafficking. Eur J Histochem 44:325-334
    • (2000) Eur J Histochem , vol.44 , pp. 325-334
    • Wilcke, M.1    Walum, E.2
  • 32
    • 42649124339 scopus 로고    scopus 로고
    • TNF: A master switch for inflammation to cancer
    • Sethi G, Sung B, Aggarwal BB 2008 TNF: a master switch for inflammation to cancer. Front Biosci 13:5094-5107
    • (2008) Front Biosci , vol.13 , pp. 5094-5107
    • Sethi, G.1    Sung, B.2    Aggarwal, B.B.3
  • 33
    • 0033867178 scopus 로고    scopus 로고
    • Potential role of TNF-α in the pathogenesis of insulin resistance and type 2 diabetes
    • Moller DE 2000 Potential role of TNF-α in the pathogenesis of insulin resistance and type 2 diabetes. Trends Endocrinol Metab 11:212-217
    • (2000) Trends Endocrinol Metab , vol.11 , pp. 212-217
    • Moller, D.E.1
  • 36
    • 0035925888 scopus 로고    scopus 로고
    • Regulation of free and bound leptin and soluble leptin receptors during inflammation in mice
    • Voegeling S, Fantuzzi G 2001 Regulation of free and bound leptin and soluble leptin receptors during inflammation in mice. Cytokine 14:97-103
    • (2001) Cytokine , vol.14 , pp. 97-103
    • Voegeling, S.1    Fantuzzi, G.2
  • 38
    • 0023243675 scopus 로고
    • Functional expression of the human transferrin receptor cDNA in Chinese hamster ovary cells deficient in endogenous transferrin receptor
    • McGraw TE, Greenfield L, Maxfield FR 1987 Functional expression of the human transferrin receptor cDNA in Chinese hamster ovary cells deficient in endogenous transferrin receptor. J Cell Biol 105:207-214
    • (1987) J Cell Biol , vol.105 , pp. 207-214
    • McGraw, T.E.1    Greenfield, L.2    Maxfield, F.R.3
  • 39
    • 27544491928 scopus 로고    scopus 로고
    • Purification of adenovirus and adeno-associated virus: Comparison of novel membrane-based technology to conventional techniques
    • Duffy AM, O'Doherty AM, O'Brien T, Strappe PM 2005 Purification of adenovirus and adeno-associated virus: comparison of novel membrane-based technology to conventional techniques. Gene Ther 12 Suppl 1:S62-S72
    • (2005) Gene Ther , vol.12 , Issue.SUPPL. 1
    • Duffy, A.M.1    O'Doherty, A.M.2    O'Brien, T.3    Strappe, P.M.4
  • 40
    • 34447549109 scopus 로고    scopus 로고
    • Method to enhance transfection efficiency of cell lines and placental fibroblasts
    • Zhang M, Guller S, Huang Y 2007 Method to enhance transfection efficiency of cell lines and placental fibroblasts. Placenta 28:779-782
    • (2007) Placenta , vol.28 , pp. 779-782
    • Zhang, M.1    Guller, S.2    Huang, Y.3
  • 41
    • 34547126211 scopus 로고    scopus 로고
    • Disruption of peripheral leptin signaling in mice results in hyperleptinemia without associated metabolic abnormalities
    • Guo K, McMinn JE, Ludwig T, Yu YH, Yang G, Chen L, Loh D, Li C, Chua S Jr, Zhang Y 2007 Disruption of peripheral leptin signaling in mice results in hyperleptinemia without associated metabolic abnormalities. Endocrinology 148:3987-3997
    • (2007) Endocrinology , vol.148 , pp. 3987-3997
    • Guo, K.1    McMinn, J.E.2    Ludwig, T.3    Yu, Y.H.4    Yang, G.5    Chen, L.6    Loh, D.7    Li, C.8    Chua Jr., S.9    Zhang, Y.10
  • 42
    • 0032582687 scopus 로고    scopus 로고
    • Human leptin receptor. Determination of disulfide structure and N-glycosylation sites of the extracellular domain
    • Haniu M, Arakawa T, Bures EJ, Young Y, Hui JO, Rohde MF, Welcher AA, Horan T 1998 Human leptin receptor. Determination of disulfide structure and N-glycosylation sites of the extracellular domain. J Biol Chem 273:28691-28699
    • (1998) J Biol Chem , vol.273 , pp. 28691-28699
    • Haniu, M.1    Arakawa, T.2    Bures, E.J.3    Young, Y.4    Hui, J.O.5    Rohde, M.F.6    Welcher, A.A.7    Horan, T.8
  • 44
    • 15444377041 scopus 로고    scopus 로고
    • Induction of leptin receptor expression in the liver by leptin and food deprivation
    • Cohen P, Yang G, Yu X, Soukas AA, Wolfish CS, Friedman JM, Li C 2005 Induction of leptin receptor expression in the liver by leptin and food deprivation. J Biol Chem 280:10034-10039
    • (2005) J Biol Chem , vol.280 , pp. 10034-10039
    • Cohen, P.1    Yang, G.2    Yu, X.3    Soukas, A.A.4    Wolfish, C.S.5    Friedman, J.M.6    Li, C.7
  • 45
    • 0030467446 scopus 로고    scopus 로고
    • The OB protein (leptin) pathway: A link between adipose tissue mass and central neural networks
    • Campfield LA, Smith FJ, Burn P 1996 The OB protein (leptin) pathway: a link between adipose tissue mass and central neural networks. Horm Metab Res 28:619-632
    • (1996) Horm Metab Res , vol.28 , pp. 619-632
    • Campfield, L.A.1    Smith, F.J.2    Burn, P.3
  • 47
    • 0036789186 scopus 로고    scopus 로고
    • Tumor necrosis factor-α stimulates lipolysis in differentiated human adipocytes through activation of extracellular signal-related kinase and elevation of intracellular cAMP
    • Zhang HH, Halbleib M, Ahmad F, Manganiello VC, Greenberg AS 2002 Tumor necrosis factor-α stimulates lipolysis in differentiated human adipocytes through activation of extracellular signal-related kinase and elevation of intracellular cAMP. Diabetes 51:2929-2935
    • (2002) Diabetes , vol.51 , pp. 2929-2935
    • Zhang, H.H.1    Halbleib, M.2    Ahmad, F.3    Manganiello, V.C.4    Greenberg, A.S.5
  • 48
    • 52949108413 scopus 로고    scopus 로고
    • Regulation of neutral sphingomyelinase-2 (nSMase2) by tumor necrosis factor-α involves protein kinase C-delta in lung epithelial cells
    • Clarke CJ, Guthrie JM, Hannun YA 2008 Regulation of neutral sphingomyelinase-2 (nSMase2) by tumor necrosis factor-α involves protein kinase C-delta in lung epithelial cells. Mol Pharmacol 74:1022-1032
    • (2008) Mol Pharmacol , vol.74 , pp. 1022-1032
    • Clarke, C.J.1    Guthrie, J.M.2    Hannun, Y.A.3
  • 49
    • 4544223633 scopus 로고    scopus 로고
    • Serum concentrations of nitric oxide, tumor necrosis factor (TNF)-α and TNF soluble receptors in women with overweight and obesity
    • Olszanecka-Glinianowicz M, Zahorska-Markiewicz B, Janowska J, Zurakowski A 2004 Serum concentrations of nitric oxide, tumor necrosis factor (TNF)-α and TNF soluble receptors in women with overweight and obesity. Metabolism 53:1268-1273
    • (2004) Metabolism , vol.53 , pp. 1268-1273
    • Olszanecka-Glinianowicz, M.1    Zahorska-Markiewicz, B.2    Janowska, J.3    Zurakowski, A.4
  • 50
    • 0032749917 scopus 로고    scopus 로고
    • Elevated serum TNF-α level as a link between endothelial dysfunction and insulin resistance in normotensive obese patients
    • Winkler G, Lakatos P, Salamon F, Nagy Z, Speer G, Kovács M, Harmos G, Dworak O, Cseh K 1999 Elevated serum TNF-α level as a link between endothelial dysfunction and insulin resistance in normotensive obese patients. Diabet Med 16:207-211
    • (1999) Diabet Med , vol.16 , pp. 207-211
    • Winkler, G.1    Lakatos, P.2    Salamon, F.3    Nagy, Z.4    Speer, G.5    Kovács, M.6    Harmos, G.7    Dworak, O.8    Cseh, K.9
  • 54
    • 0024451836 scopus 로고
    • Tumor necrosis factor and interleukin-1 serum levels during severe sepsis in humans
    • Damas P, Reuter A, Gysen P, Demonty J, Lamy M, Franchimont P 1989 Tumor necrosis factor and interleukin-1 serum levels during severe sepsis in humans. Crit Care Med 17:975-978
    • (1989) Crit Care Med , vol.17 , pp. 975-978
    • Damas, P.1    Reuter, A.2    Gysen, P.3    Demonty, J.4    Lamy, M.5    Franchimont, P.6
  • 55
    • 0025266645 scopus 로고
    • Prognostic values of tumor necrosis factor/cachectin, interleukin-1, interferon-α, and interferon-γ in the serum of patients with septic shock
    • Swiss-Dutch J5 Immunoglobulin Study Group
    • Calandra T, Baumgartner JD, Grau GE, Wu MM, Lambert PH, Schellekens J, Verhoef J, Glauser MP 1990 Prognostic values of tumor necrosis factor/cachectin, interleukin-1, interferon-α, and interferon-γ in the serum of patients with septic shock. Swiss-Dutch J5 Immunoglobulin Study Group. J Infect Dis 161:982-987
    • (1990) J Infect Dis , vol.161 , pp. 982-987
    • Calandra, T.1    Baumgartner, J.D.2    Grau, G.E.3    Wu, M.M.4    Lambert, P.H.5    Schellekens, J.6    Verhoef, J.7    Glauser, M.P.8
  • 57
  • 58
    • 20044375180 scopus 로고    scopus 로고
    • Tumor necrosis factor α (TNF-α) coordinately regulates the expression of specific matrix metalloproteinases (MMPS) and angiogenic factors during fracture healing
    • Lehmann W, Edgar CM, Wang K, Cho TJ, Barnes GL, Kakar S, Graves DT, Rueger JM, Gerstenfeld LC, Einhorn TA 2005 Tumor necrosis factor α (TNF-α) coordinately regulates the expression of specific matrix metalloproteinases (MMPS) and angiogenic factors during fracture healing. Bone 36:300-310
    • (2005) Bone , vol.36 , pp. 300-310
    • Lehmann, W.1    Edgar, C.M.2    Wang, K.3    Cho, T.J.4    Barnes, G.L.5    Kakar, S.6    Graves, D.T.7    Rueger, J.M.8    Gerstenfeld, L.C.9    Einhorn, T.A.10
  • 59
    • 3042849113 scopus 로고    scopus 로고
    • Tumour necrosis factor-α stimulates expression of TNF-α converting enzyme in endothelial cells
    • Bzowska M, Jura N, Lassak A, Black RA, Bereta J 2004 Tumour necrosis factor-α stimulates expression of TNF-α converting enzyme in endothelial cells. Eur J Biochem 271:2808-2820
    • (2004) Eur J Biochem , vol.271 , pp. 2808-2820
    • Bzowska, M.1    Jura, N.2    Lassak, A.3    Black, R.A.4    Bereta, J.5


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