메뉴 건너뛰기




Volumn 39, Issue 7, 2012, Pages 7717-7726

The connection between GRKs and various signaling pathways involved in diabetic nephropathy

Author keywords

Diabetic nephropathy; G protein coupled; G protein coupled receptor kinases; Receptors

Indexed keywords

ANGIOTENSIN RECEPTOR ANTAGONIST; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; G PROTEIN COUPLED RECEPTOR; G PROTEIN COUPLED RECEPTOR KINASE; GUANINE NUCLEOTIDE BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PROSTAGLANDIN E; PROSTAGLANDIN E2; PROTEIN KINASE C; RUBOXISTAURIN; TRANSFORMING GROWTH FACTOR BETA;

EID: 84864280362     PISSN: 03014851     EISSN: 15734978     Source Type: Journal    
DOI: 10.1007/s11033-012-1608-x     Document Type: Article
Times cited : (3)

References (87)
  • 1
    • 79751477368 scopus 로고    scopus 로고
    • A glimpse of various pathogenetic mechanisms of diabetic nephropathy
    • Kanwar YS, Sun L, Xie P, Liu FY, Chen S (2011) A glimpse of various pathogenetic mechanisms of diabetic nephropathy. Annu Rev Pathol Mech 6:395-423
    • (2011) Annu Rev Pathol Mech , vol.6 , pp. 395-423
    • Kanwar, Y.S.1    Sun, L.2    Xie, P.3    Liu, F.Y.4    Chen, S.5
  • 3
    • 34047251834 scopus 로고    scopus 로고
    • Histopathology of Diabetic Nephropathy
    • DOI 10.1016/j.semnephrol.2007.01.012, PII S0270929507000149, Diabetic Nephropathy
    • Fioretto P, Mauer M (2007) Histopathology of diabetic nephropathy. Semin Nephrol 27:195-207 (Pubitemid 46550314)
    • (2007) Seminars in Nephrology , vol.27 , Issue.2 , pp. 195-207
    • Fioretto, P.1    Mauer, M.2
  • 4
    • 34250361947 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of proteinuria in diabetic nephropathy
    • Wolf G, Ziyadeh FN (2007) Cellular and molecular mechanisms of proteinuria in diabetic nephropathy. Nephron Physiol 106:26-31
    • (2007) Nephron Physiol , vol.106 , pp. 26-31
    • Wolf, G.1    Ziyadeh, F.N.2
  • 5
    • 0037407520 scopus 로고    scopus 로고
    • Extracellular matrix metabolism in diabetic nephropathy
    • DOI 10.1097/01.ASN.0000065640.77499.D7
    • Mason RM, Wahab NA (2003) Extracellular matrix metabolism in diabetic nephropathy. J Am Soc Nephrol 14:1358-1373 (Pubitemid 36519197)
    • (2003) Journal of the American Society of Nephrology , vol.14 , Issue.5 , pp. 1358-1373
    • Mason, R.M.1    Wahab, N.A.2
  • 6
    • 33947375174 scopus 로고    scopus 로고
    • Physiological roles of G protein-coupled receptor kinases and arrestins
    • DOI 10.1146/annurev.physiol.69.022405.154731
    • Premont RT, Gainetdinov RR (2007) Physiological roles of G protein-coupled receptor kinases and arrestins. Annu Rev Physiol 69:511-534 (Pubitemid 46457653)
    • (2007) Annual Review of Physiology , vol.69 , pp. 511-534
    • Premont, R.T.1    Gainetdinov, R.R.2
  • 7
    • 77952840083 scopus 로고    scopus 로고
    • The complex G protein-coupled receptor kinase 2 (GRK2) interac-tome unveils new physiopathological targets
    • Penela P, Murga C, Ribas C, Lafarga V, Mayor F Jr (2010) The complex G protein-coupled receptor kinase 2 (GRK2) interac-tome unveils new physiopathological targets. Br J Pharmacol 160:821-832
    • (2010) Br J Pharmacol , vol.160 , pp. 821-832
    • Penela, P.1    Murga, C.2    Ribas, C.3    Lafarga, V.4    Mayor, Jr.F.5
  • 10
  • 11
    • 0030029153 scopus 로고    scopus 로고
    • High affinity binding of beta-adrenergic receptor kinase to microsomal membranes. Modulation of the activity of bound kinase by heterotrimeric G protein activation
    • Murga C, Ruiz-Gomez A, Garcia-Higuera I, Kim CM, Benovic JL, Mayor F Jr (1996) High affinity binding of beta-adrenergic receptor kinase to microsomal membranes. Modulation of the activity of bound kinase by heterotrimeric G protein activation. J Biol Chem 271:985-994
    • (1996) J Biol Chem , vol.271 , pp. 985-994
    • Murga, C.1    Ruiz-Gomez, A.2    Garcia-Higuera, I.3    Kim, C.M.4    Benovic, J.L.5    Mayor, Jr.F.6
  • 12
    • 33947424008 scopus 로고    scopus 로고
    • The G protein-coupled receptor kinase (GRK) interactome: Role of grks in GPCR regulation and signaling
    • Ribas Catalina, Penela Petronila (2007) The G protein-coupled receptor kinase (GRK) interactome: role of GRKs in GPCR regulation and signaling. Biochim Biophys Acta 1768:913-922
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 913-922
    • Ribas, C.1    Petronila, P.2
  • 14
    • 0027481032 scopus 로고
    • The binding site for the βγ subunits of heterotrimeric G proteins on the β-adrenergic receptor kinase
    • Koch WJ, Inglese J, Stone WC, Lefkowitz RJ (1993) The binding site for the beta gamma subunits of heterotrimeric G proteins on the beta-adrenergic receptor kinase. J Biol Chem 268:8256-8260 (Pubitemid 23120415)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.11 , pp. 8256-8260
    • Koch, W.J.1    Inglese, J.2    Stone, W.C.3    Lefkowitz, R.J.4
  • 15
    • 0028891875 scopus 로고
    • Muta-tional analysis of the pleckstrin homology domain of the beta-adrenergic receptor kinase. Differential effects on G beta gamma and phosphatidylinositol 4, 5-Bisphosphate binding
    • Touhara K, Koch WJ, Hawes BE, Lefkowitz RJ (1995) Muta-tional analysis of the pleckstrin homology domain of the beta-adrenergic receptor kinase. Differential effects on G beta gamma and phosphatidylinositol 4, 5-bisphosphate binding. J Biol Chem 270:17000-17005
    • (1995) J Biol Chem , vol.270 , pp. 17000-17005
    • Touhara, K.1    Koch, W.J.2    Hawes, B.E.3    Lefkowitz, R.J.4
  • 17
    • 0032857194 scopus 로고    scopus 로고
    • The grk4 subfamily of G protein-coupled receptor kinases. Alternative splicing, gene organization, and sequence conservation
    • Premont RT, Macrae AD, Aparicio SA, Kendall HE, Welch JE, Lefkowitz RJ (1999) The GRK4 subfamily of G protein-coupled receptor kinases. Alternative splicing, gene organization, and sequence conservation. J Biol Chem 274:29381-29389
    • (1999) J Biol Chem , vol.274 , pp. 29381-29389
    • Premont, R.T.1    MacRae, A.D.2    Aparicio, S.A.3    Kendall, H.E.4    Welch, J.E.5    Lefkowitz, R.J.6
  • 18
    • 28344450854 scopus 로고    scopus 로고
    • The variable C-terminal extension of G-protein-coupled receptor kinase 6 constitutes an accessorial autoregulatory domain
    • DOI 10.1111/j.1742-4658.2005.04995.x
    • Vatter P, Stoesser C, Samel I, Gierschik P, Moepps B (2005) The variable C-terminal extension of G-protein-coupled receptor kinase 6 constitutes an accessorial autoregulatory domain. FEBS J 272:6039-6051 (Pubitemid 41715234)
    • (2005) FEBS Journal , vol.272 , Issue.23 , pp. 6039-6051
    • Vatter, P.1    Stoesser, C.2    Samel, I.3    Gierschik, P.4    Moepps, B.5
  • 19
    • 0032553549 scopus 로고    scopus 로고
    • Structure-function analysis of G protein-coupled receptor kinase-5: Role of the carboxyl terminus in kinase regulation
    • DOI 10.1074/jbc.273.47.31510
    • Pronin AN, Carman CV, Benovic JL (1998) Structure-function analysis of G protein-coupled receptor kinase-5. Role of the carboxyl terminus in kinase regulation. J Biol Chem 273:31510-31518 (Pubitemid 28533173)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.47 , pp. 31510-31518
    • Pronin, A.N.1    Carman, C.V.2    Benovic, J.L.3
  • 20
    • 45749127330 scopus 로고    scopus 로고
    • Methylglyoxal induces prostaglandin E2 production in rat mesangial cells
    • Uriuhara A, Miyata S, Liu BF et al (2008) Methylglyoxal induces prostaglandin E2 production in rat mesangial cells. Kobe J Med Sci 53(6):305-315
    • (2008) Kobe J Med Sci , vol.53 , Issue.6 , pp. 305-315
    • Uriuhara, A.1    Miyata, S.2    Liu, B.F.3
  • 22
    • 0028183018 scopus 로고
    • VIII. International union of pharmacology classification of prostanoid receptors: Properties, distribution, and structure of the receptors and their subtypes
    • Coleman RA, Smith WL, Narumiya S (1994) International union of pharmacology classification of prostanoid receptors: properties, distribution, and structure of the receptors and their subtypes. Pharmacol Rev 46:205-229 (Pubitemid 24185151)
    • (1994) Pharmacological Reviews , vol.46 , Issue.2 , pp. 205-229
    • Coleman, R.A.1    Smith, W.L.2    Narumiya, S.3
  • 23
    • 0027205165 scopus 로고
    • 3 subtype. Different COOH- terminal domains determine sensitivity to agonist-induced desensitization
    • Negishi M, Sugimoto Y, Irie A, Narumiya S, Ichikawa A (1993) Two isoforms of prostaglandin E receptor EP3 subtype. Different COOH-terminal domains determine sensitivity to agonist-induced desensitization. J Biol Chem 268:9517-9521 (Pubitemid 23146006)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.13 , pp. 9517-9521
    • Negishi, M.1    Sugimoto, Y.2    Irie, A.3    Narumiya, S.4    Ichikawa, A.5
  • 24
    • 0029661961 scopus 로고    scopus 로고
    • Two G(s)-coupled prostaglandin E receptor subtypes, EP2 and EP4, differ in desensitization and sensitivity to the metabolic inactivation of the agonist
    • Nishigaki N, Negishi M, Ichikawa A (1996) Two Gs-coupled prostaglandin E receptor subtypes, EP2 and EP4, differ in desensitization and sensitivity to the metabolic inactivation of the agonist. Mol Pharmacol 50:1031-1037 (Pubitemid 26347726)
    • (1996) Molecular Pharmacology , vol.50 , Issue.4 , pp. 1031-1037
    • Nishigaki, N.1    Negishi, M.2    Ichikawa, A.3
  • 25
    • 0031024509 scopus 로고    scopus 로고
    • 4 subtype is essential for agonist-induced desensitization
    • Bastepe M, Ashby B (1997) The long cytoplasmic carboxyl terminus of the prostaglandin E2 receptor EP4 subtype is essential for agonist-induced desensitization. Mol Pharmacol 51:343-349 (Pubitemid 27074157)
    • (1997) Molecular Pharmacology , vol.51 , Issue.2 , pp. 343-349
    • Bastepe, M.1    Ashby, B.2
  • 26
    • 0028920668 scopus 로고
    • Protein kinases that phosphorylate activated G protein-coupled receptors
    • Premont RT, Inglese J, Lefkowitz RJ (1995) Protein kinases that phosphorylate activated G protein-coupled receptors. FASEB J 9:175-182
    • (1995) FASEB J , vol.9 , pp. 175-182
    • Premont, R.T.1    Inglese, J.2    Lefkowitz, R.J.3
  • 27
    • 0029888504 scopus 로고    scopus 로고
    • Differential localization of prostaglandin e receptor subtypes in human kidney
    • Breyer MD, Linda D, Jacobson HR, Breyer RM (1996) Differential localization of prostaglandin E receptor subtypes in human kidney. Am J Physiol 270:F912-F918
    • (1996) Am J Physiol , vol.270
    • Breyer, M.D.1    Linda, D.2    Jacobson, H.R.3    Breyer, R.M.4
  • 32
    • 34547487924 scopus 로고    scopus 로고
    • The role of protein kinase C activation in diabetic nephropathy
    • DOI 10.1038/sj.ki.5002386, PII 5002386
    • Noh H, King GL (2007) The role of PKC activation in diabetic nephropathy. Kidney Int 106:S49-S53 (Pubitemid 47172561)
    • (2007) Kidney International , vol.72 , Issue.SUPPL. 106
    • Noh, H.1    King, G.L.2
  • 34
    • 40749139536 scopus 로고    scopus 로고
    • Inhibition of NADPH oxidase prevents advanced glycation end product-mediated damage in diabetic nephropathy through pkc-a-dependent pathway
    • Thallas-Bonke V, Thorpe SR, Coughlan MT, Fukami K, Yap FY et al (2007) Inhibition of NADPH oxidase prevents advanced glycation end product-mediated damage in diabetic nephropathy through PKC-a-dependent pathway. Diabetes 57:460-469
    • (2007) Diabetes , vol.57 , pp. 460-469
    • Thallas-Bonke, V.1    Thorpe, S.R.2    Coughlan, M.T.3    Fukami, K.4    Yap, F.Y.5
  • 35
    • 77952468064 scopus 로고    scopus 로고
    • Activation of protein kinase C iso-forms and its impact on diabetic complications
    • Geraldes P, King GL (2010) Activation of protein kinase C iso-forms and its impact on diabetic complications. Circ Res 106(8):1319-1331
    • (2010) Circ Res , vol.106 , Issue.8 , pp. 1319-1331
    • Geraldes, P.1    King, G.L.2
  • 36
    • 28644442122 scopus 로고    scopus 로고
    • The effect of ruboxistaurin on nephropathy in type 2 diabetes
    • DOI 10.2337/diacare.28.11.2686
    • Tuttle KR, Bakris GL, Toto RD, McGill JB, Hu K, Anderson PW (2005) The effect of ruboxistaurin on nephropathy in type 2 diabetes. Diabetes Care 28:2686-2690 (Pubitemid 43951160)
    • (2005) Diabetes Care , vol.28 , Issue.11 , pp. 2686-2690
    • Tuttle, K.R.1    Bakris, G.L.2    Toto, R.D.3    McGill, J.B.4    Hu, K.5    Anderson, P.W.6
  • 37
    • 0037624579 scopus 로고    scopus 로고
    • Pleckstrin homology domain of G protein-coupled receptor kinase-2 binds to PKC and affects the activity of PKC kinase
    • Yang XL, Zhang YL, Lai ZS, Xing FY, Liu YH (2003) Pleckstrin homology domain of G protein-coupled receptor kinase-2 binds to PKC and affects the activity of PKC kinase. World J Gastro-enterol 9(4):800-803
    • (2003) World J Gastro-enterol , vol.9 , Issue.4 , pp. 800-803
    • Yang, X.L.1    Zhang, Y.L.2    Lai, Z.S.3    Xing, F.Y.4    Liu, Y.H.5
  • 38
    • 4043139440 scopus 로고    scopus 로고
    • PH domain of G protein-coupled receptor kinase-2 binds to protein kinase C (PKC) and negatively regulates activity of PKC kinase
    • a1-d305
    • Ji S, Liu X, Li S, Shen L, Li F, Wang J, Han J, Yao L (2003) PH domain of G protein-coupled receptor kinase-2 binds to protein kinase C (PKC) and negatively regulates activity of PKC kinase. Front Biosci 8:a34-a39 (Pubitemid 39069941)
    • (2003) Frontiers in Bioscience , vol.8
    • Ji, S.1    Liu, X.2    Li, S.3    Shen, L.4    Li, F.5    Wang, J.6    Han, J.7    Yao, L.8
  • 39
    • 0032953024 scopus 로고    scopus 로고
    • The state and responsiveness of the renin-angiotensin-aldosterone system in patients with type 2 diabetes mellitus
    • Price D, De'Oliveira J, Fisher N et al (1999) The state and responsiveness of the renin-angiotensin-aldosterone system in patients with type 2 diabetes mellitus. Am J Hypertens 12:348
    • (1999) Am J Hypertens , vol.12 , pp. 348
    • Price, D.1    De'Oliveira, J.2    Fisher, N.3
  • 40
    • 25144432973 scopus 로고    scopus 로고
    • The G protein-coupled receptor kinase-2 is a TGFβ-inducible antagonist of TGFβ signal transduction
    • DOI 10.1038/sj.emboj.7600794, PII 7600794
    • Ho J, Cocolakis E, Dumas VM, Posner BL, Laporte SA, Lebrun JJ (2005) The G protein-coupled receptor kinase-2 is TGFb inducible antagonist of TGFb signal transduction. EMBO J 24:3247-3258 (Pubitemid 41348699)
    • (2005) EMBO Journal , vol.24 , Issue.18 , pp. 3247-3258
    • Ho, J.1    Cocolakis, E.2    Dumas, V.M.3    Posner, B.I.4    Laporte, S.A.5    Lebrun, J.-J.6
  • 41
    • 4544345529 scopus 로고    scopus 로고
    • Free radicals in cell biology
    • DOI 10.1016/S0074-7696(04)37002-6, PII S0074769604370026
    • Djordjevic VB (2004) Free radicals in cell biology. Int Rev Cytol 237:57-89 (Pubitemid 39221038)
    • (2004) International Review of Cytology , vol.237 , pp. 57-89
    • Djordjevic, V.B.1
  • 42
    • 34548027510 scopus 로고    scopus 로고
    • q/11α G protein-phospholipase C signaling involving G protein-coupled receptor kinase 2
    • DOI 10.1152/ajprenal.00108.2007
    • Banday AA, Lokhandwala MF (2007) Oxidative stress reduces renal dopamine D1 receptor-Gq/11a G protein-phospholipase C signaling involving G protein-coupled receptor kinase 2. Am J Physiol Renal Physiol 293:F306-F315 (Pubitemid 47345031)
    • (2007) American Journal of Physiology - Renal Physiology , vol.293 , Issue.1
    • Banday, A.A.1    Lokhandwala, M.F.2
  • 43
    • 0033861278 scopus 로고    scopus 로고
    • Intrarenal dopamine: A key signal in the interactive regulation of sodium metabolism
    • DOI 10.1146/annurev.physiol.62.1.621
    • Aperia AC (2000) Intrarenal dopamine: a key signal in the interactive regulation of sodium metabolism. Annu Rev Physiol 62:621-647 (Pubitemid 30618277)
    • (2000) Annual Review of Physiology , vol.62 , pp. 621-647
    • Aperia, A.C.1
  • 44
    • 0031845971 scopus 로고    scopus 로고
    • Renal dopamine receptor function in hypertension
    • Hussain T, Lokhandwala MF (1998) Renal dopamine receptor function in hypertension. Hypertension 32:187-197 (Pubitemid 28376472)
    • (1998) Hypertension , vol.32 , Issue.2 , pp. 187-197
    • Hussain, T.1    Lokhandwala, M.F.2
  • 45
    • 21344447490 scopus 로고    scopus 로고
    • Tempol reduces oxidative stress, improves insulin sensitivity, decreases renal dopamine D1 receptor hyperphosphorylation, and restores D1 receptor-G-protein coupling and function in obese Zucker rats
    • DOI 10.2337/diabetes.54.7.2219
    • Banday AA, Marwaha A, Tallam LS, Lokhandwala MF (2005) Tempol reduces oxidative stress, improves insulin sensitivity, decreases renal dopamine D1 receptor hyperphosphorylation, and restores D1 receptor-G protein coupling and function in obese Zucker rats. Diabetes 54:2219-2226 (Pubitemid 40911287)
    • (2005) Diabetes , vol.54 , Issue.7 , pp. 2219-2226
    • Banday, A.A.1    Marwaha, A.2    Tallam, L.S.3    Lokhandwala, M.F.4
  • 46
    • 0035033862 scopus 로고    scopus 로고
    • Mechanism of sodium load-induced hypertension in non-insulin dependent diabetes mellitus model rats: Defective dopaminergic system to inhibit Na-K-ATPase activity in renal epithelial cells
    • DOI 10.1291/hypres.24.127
    • Tsuchida H, Imai G, Shima Y, Satoh T, Owada S (2001) Mechanism of sodium load-induced hypertension in non-insulin dependent diabetes mellitus model rats: defective dopaminergic system to inhibit Na-K-ATPase activity in renal epithelial cells. Hypertens Res 24:127-135 (Pubitemid 32377583)
    • (2001) Hypertension Research , vol.24 , Issue.2 , pp. 127-135
    • Tsuchida, H.1    Imai, G.2    Shima, Y.3    Satoh, T.4    Owada, S.5
  • 47
    • 33644841768 scopus 로고    scopus 로고
    • 1 dopamine receptor is constitutively phosphorylated by G protein-coupled receptor kinase 4
    • DOI 10.1124/mol.105.019901
    • Rankin ML, Marinec PS, Cabrera DM, Wang Z, Jose PA, Sibley DR (2006) The D1 dopamine receptor is constitutively phos-phorylated by G protein coupled receptor kinase 4. Mol Pharmacol 69:759-769 (Pubitemid 43363850)
    • (2006) Molecular Pharmacology , vol.69 , Issue.3 , pp. 759-769
    • Rankin, M.L.1    Marinec, P.S.2    Cabrera, D.M.3    Wang, Z.4    Jose, P.A.5    Sibley, D.R.6
  • 49
    • 22344448639 scopus 로고    scopus 로고
    • s protein coupling by reducing receptor hyperphosphorylation in obese rats
    • DOI 10.1152/ajprenal.00362.2004
    • Trivedi M, Lokhandwala MF (2005) Rosiglitazone restores renal d1a receptor-gs protein coupling by reducing receptor hyper-phosphorylation in obese rats. Am J Physiol Renal Physiol 289:F298-F304 (Pubitemid 41003659)
    • (2005) American Journal of Physiology - Renal Physiology , vol.289 , Issue.2
    • Trivedi, M.1    Lokhandwala, M.F.2
  • 50
    • 28744455710 scopus 로고    scopus 로고
    • Hydrogen peroxide causes uncoupling of dopamine D1-like receptors from G proteins via a mechanism involving protein kinase C and G-protein-coupled receptor kinase 2
    • DOI 10.1016/j.freeradbiomed.2005.08.018, PII S0891584905004648
    • Asghar M, Banday AA, Fardoun RZ, Lokhandwala MF (2006) Hydrogen peroxide causes uncoupling of dopamine D1-like receptors from G proteins via a mechanism involving protein kinase C and G-protein-coupled receptor kinase 2. Free Radic Biol Med 40:13-20 (Pubitemid 41759399)
    • (2006) Free Radical Biology and Medicine , vol.40 , Issue.1 , pp. 13-20
    • Asghar, M.1    Banday, A.A.2    Fardoun, R.Z.3    Lokhandwala, M.F.4
  • 53
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-β signaling from cell membrane to the nucleus
    • DOI 10.1016/S0092-8674(03)00432-X
    • Shi Y, Massague J (2003) Mechanisms of TGF-beta signaling from cell membrane to the nucleus. Cell 113:685-700 (Pubitemid 36724933)
    • (2003) Cell , vol.113 , Issue.6 , pp. 685-700
    • Shi, Y.1    Massague, J.2
  • 54
    • 0347511753 scopus 로고    scopus 로고
    • Mediators of Diabetic Renal Disease: The Case for TGF-β as the Major Mediator
    • Ziyadeh FN (2004) Mediators of diabetic renal disease: the case for TGF-b as the major mediator. J Am Soc Nephrol 15:S55-S57 (Pubitemid 38018457)
    • (2004) Journal of the American Society of Nephrology , vol.15 , Issue.SUPPL. 1
    • Ziyadeh, F.N.1
  • 55
    • 2142646426 scopus 로고    scopus 로고
    • Tgf-b signaling and the fibrotic response
    • Leask A, Abraham DJ (2004) TGF-b signaling and the fibrotic response. FASEB J 18:816-827
    • (2004) FASEB J , vol.18 , pp. 816-827
    • Leask, A.1    Abraham, D.J.2
  • 56
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-β signaling from cell membrane to the nucleus
    • DOI 10.1016/S0092-8674(03)00432-X
    • Shi Y, Massague J (2003) Mechanisms of TGF-b signaling from cell membrane to the nucleus. Cell 113(6):685-700 (Pubitemid 36724933)
    • (2003) Cell , vol.113 , Issue.6 , pp. 685-700
    • Shi, Y.1    Massague, J.2
  • 57
    • 33750577820 scopus 로고    scopus 로고
    • Mechanisms of diabetic nephropathy: Role of hypertension
    • DOI 10.1161/01.HYP.0000240331.32352.0c, PII 0000426820061000000001
    • Guinti S, Barit D, Cooper ME (2006) Mechanisms of diabetic nephropathy: role of hypertension. Hypertension 48:519-526 (Pubitemid 44843845)
    • (2006) Hypertension , vol.48 , Issue.4 , pp. 519-526
    • Giunti, S.1    Barit, D.2    Cooper, M.E.3
  • 58
    • 0026681076 scopus 로고
    • Diabetes mellitus and hypertension
    • Epstein M, Sowers J (1992) Diabetes mellitus and hypertension. Hypertension 19:403-418
    • (1992) Hypertension , vol.19 , pp. 403-418
    • Epstein, M.1    Sowers, J.2
  • 59
    • 33748324580 scopus 로고    scopus 로고
    • Hypertension and Diabetes: Role of the Renin-Angiotensin System
    • DOI 10.1016/j.ecl.2006.06.007, PII S0889852906000478, Impaired Glucose Tolerance and Cardiovascular Disease
    • Jandeleit-Dahm K, Cooper ME (2006) Hypertension and diabetes: role of renin-angiotensin system. Endocrino Meab Clin N Am 35:469-490 (Pubitemid 44321946)
    • (2006) Endocrinology and Metabolism Clinics of North America , vol.35 , Issue.3 , pp. 469-490
    • Jandeleit-Dahm, K.1    Cooper, M.E.2
  • 60
    • 34748859681 scopus 로고    scopus 로고
    • The intrarenal renin-angiotensin system: From physiology to the pathobiology of hypertension and kidney disease
    • DOI 10.1124/pr.59.3.3
    • Kobori H, Nangaku M, Navar LG, Nishiyama A (2007) The intrarenal renin-angiotensin system: from physiology to the pathobiology of hypertension and kidney disease. Pharmacol Rev 59:251-287 (Pubitemid 47481436)
    • (2007) Pharmacological Reviews , vol.59 , Issue.3 , pp. 251-287
    • Kobori, H.1    Nangaku, M.2    Navar, L.G.3    Nishiyama, A.4
  • 63
    • 33644815729 scopus 로고    scopus 로고
    • The role of the kidneys in hypertension
    • Navar LG (2005) The role of the kidneys in hypertension. J Clin Hypertens (Greenwich) 7:542-549
    • (2005) J Clin Hypertens (Greenwich) , vol.7 , pp. 542-549
    • Navar, L.G.1
  • 64
    • 32844466545 scopus 로고    scopus 로고
    • Chronically increased intrarenal angiotensin II causes nephropathy in an animal model of type 2 diabetes
    • Sharma R, Sharma M, Reddy S, Savin VJ, Nagaria AM, Wiegmann TB (2006) Chronically increased intrarenal angiotensin II causes nephropathy in an animal model of type 2 diabetes. Front Biosci 11:968-976 (Pubitemid 43253451)
    • (2006) Frontiers in Bioscience , vol.11 , Issue.P889-1198 , pp. 968-976
    • Sharma, R.1    Sharma, M.2    Reddy, S.3    Savin, V.J.4    Nagaria, A.M.5    Wiegmann, T.B.6
  • 65
    • 0038577163 scopus 로고    scopus 로고
    • The angiotensin II type 1 receptor mediates renal interstitial content of tumor necrosis factor-α in diabetic rats
    • DOI 10.1210/en.2003-0010
    • Siragy HM, Awad A, Abadir P, Webb R (2003) The angiotensin II type 1 receptor mediates renal interstitial content of tumor necrosis factor-a in diabetic rats. Endocrinology 144:2229-2233 (Pubitemid 36629871)
    • (2003) Endocrinology , vol.144 , Issue.6 , pp. 2229-2233
    • Siragy, H.M.1    Awad, A.2    Abadir, P.3    Webb, R.4
  • 66
    • 0032835393 scopus 로고    scopus 로고
    • Role of angiotensin II in glucose-induced inhibition of mesangial matrix degradation
    • DOI 10.2337/diabetes.48.10.2066
    • Singh R, Alavi N, Singh AK, Leehey DJ (1999) Role of angio-tensin II in glucose-induced inhibition of mesangial matrix degradation. Diabetes 48:2066-2073 (Pubitemid 29458373)
    • (1999) Diabetes , vol.48 , Issue.10 , pp. 2066-2073
    • Singh, R.1    Alavi, N.2    Singh, A.K.3    Leehey, D.J.4
  • 67
    • 18744376906 scopus 로고    scopus 로고
    • A novel mechanism for angiotensin II formation in streptozotocin-diabetic rat glomeruli
    • DOI 10.1152/ajprenal.00159.2003
    • Singh R, Singh AK, Leehey DJ (2005) A novel mechanism for angiotensin II formation in streptozotocin diabetic rat glomeruli. Am J Physiol 288:F1183-F1190 (Pubitemid 40677088)
    • (2005) American Journal of Physiology - Renal Physiology , vol.288 , Issue.6
    • Singh, R.1    Singh, A.K.2    Leehey, D.J.3
  • 68
    • 0029991655 scopus 로고    scopus 로고
    • Phosphorylation of the type 1A angiotensin II receptor by G protein-coupled receptor kinases and protein kinase C
    • Oppermann M, Freedman NJ, Alexander RW, Lefkowitz RJ (1996) Phosphorylation of the type 1A angiotensin II receptor by G protein-coupled receptor kinases and protein kinase C. J Biol Chem 271:13266-13272
    • (1996) J Biol Chem , vol.271 , pp. 13266-13272
    • Oppermann, M.1    Freedman, N.J.2    Alexander, R.W.3    Lefkowitz, R.J.4
  • 69
    • 78049254400 scopus 로고    scopus 로고
    • Dopamine and G protein-coupled receptor kinase 4 in the kidney: Role in blood pressure regulation
    • Jose PA, Soares-da-Silva P, Gilbert ME, Felder RA (2010) Dopamine and G protein-coupled receptor kinase 4 in the kidney: role in blood pressure regulation. Biochim Biophys Acta 1802:1259-1267
    • (2010) Biochim Biophys Acta , vol.1802 , pp. 1259-1267
    • Jose, P.A.1    Soares-Da-Silva, P.2    Gilbert, M.E.3    Felder, R.A.4
  • 70
    • 0028685827 scopus 로고
    • Plasma endothelin levels in NIDDM patients with macroangiopathy
    • Donatelli M, Colletti I, Bucalo M et al (1994) Plasma endothelin levels in NIDDM patients with macroangiopathy. Diabetes Res 25:159-164
    • (1994) Diabetes Res , vol.25 , pp. 159-164
    • Donatelli, M.1    Colletti, I.2    Bucalo, M.3
  • 71
    • 0030757504 scopus 로고    scopus 로고
    • Phosphorylation and desensitization of human endothelin A and B receptors: Evidence for G protein-coupled receptor kinase specificity
    • DOI 10.1074/jbc.272.28.17734
    • Freedman NJ, Ament AS, Oppermann M, Stoffel RH, Exum ST, Lefkowitz RJ (1997) Phosphorylation and desensitization of human endothelin A and B receptors. Evidence for G proteincoupled receptor kinase specificity. J Biol Chem 272:17734-17743 (Pubitemid 27311212)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.28 , pp. 17734-17743
    • Freedman, N.J.1    Ament, A.S.2    Oppermann, M.3    Stoffel, R.H.4    Exum, S.T.5    Lefkowitz, R.J.6
  • 72
    • 3543038233 scopus 로고    scopus 로고
    • GRK2 is an endogenous protein inhibitor of the insulin signaling pathway for glucose transport stimulation
    • DOI 10.1038/sj.emboj.7600297
    • Usui I, Imamura T, Satoh H, Huang J, Babendure JL, Hupfeld CJ, Olefsky JM (2004) GRK2 is an endogenous protein inhibitor of the insulin signaling pathway for glucose transport stimulation. EMBO J 23:2821-2829 (Pubitemid 39013554)
    • (2004) EMBO Journal , vol.23 , Issue.14 , pp. 2821-2829
    • Usui, I.1    Imamura, T.2    Satoh, H.3    Huang, J.4    Babendure, J.L.5    Hupfeld, C.J.6    Olefsky, J.M.7
  • 73
    • 0021929962 scopus 로고
    • Thrombomodulin is found on endothelium of arteries, veins, capillaries, and lymphatics, and on syncytiotrophoblast of human placenta
    • DOI 10.1083/jcb.101.2.363
    • Maruyama I, Bell CE, Majerus PW (1985) Thrombomodulin is found on endothelium of arteries, veins, capillaries, and lymphatics, and on syncytiotrophoblast of human placenta. J Cell Biol 101:363-371 (Pubitemid 15239110)
    • (1985) Journal of Cell Biology , vol.101 , Issue.2 , pp. 363-371
    • Maruyama, I.1    Bell, C.E.2    Majerus, P.W.3
  • 75
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu T-KH, Hung DT, Wheaton VI, Coughlin SR (1991) Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell 64:1057-1068 (Pubitemid 121001193)
    • (1991) Cell , vol.64 , Issue.6 , pp. 1057-1068
    • Vu, T.-K.H.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 79
    • 14844321939 scopus 로고    scopus 로고
    • Characterization of glucagon-like peptide-1 receptor β-arrestin 2 interaction: A high-affinity receptor phenotype
    • DOI 10.1210/me.2004-0312
    • Jorgensen R, Martini L, Schwartz TW, Elling CE (2005) Characterization of glucagon-like peptide-1 receptor beta-arrestin 2 interaction: a high-affinity receptor phenotype. Mol Endocrinol 19:812-823 (Pubitemid 40349451)
    • (2005) Molecular Endocrinology , vol.19 , Issue.3 , pp. 812-823
    • Jorgensen, R.1    Martini, L.2    Schwartz, T.W.3    Elling, C.E.4
  • 80
    • 34250714898 scopus 로고    scopus 로고
    • Oxyntomodulin differentially affects glucagon-like peptide-1 receptor -beta-arrestin recruitment and signaling through gas
    • Jorgensen R, Kubale V, Vrecl M (2007) Oxyntomodulin differentially affects glucagon-like peptide-1 receptor -beta-arrestin recruitment and signaling through GaS. J Pharmacol Exp Ther 322:148-154
    • (2007) J Pharmacol Exp Ther , vol.322 , pp. 148-154
    • Jorgensen, R.1    Kubale, V.2    Vrecl, M.3
  • 82
    • 22344448639 scopus 로고    scopus 로고
    • s protein coupling by reducing receptor hyperphosphorylation in obese rats
    • DOI 10.1152/ajprenal.00362.2004
    • Trivedi M, Lokhandwala MF (2005) Rosiglitazone restores renal D1A receptor-Gs protein coupling by reducing receptor hyper-phosphorylation in obese rats. Am J Physiol Renal Physiol 289:F298-F304 (Pubitemid 41003659)
    • (2005) American Journal of Physiology - Renal Physiology , vol.289 , Issue.2
    • Trivedi, M.1    Lokhandwala, M.F.2
  • 86
    • 0032850020 scopus 로고    scopus 로고
    • P38 MAPK signalling cascades in inflammatory disease
    • DOI 10.1016/S1357-4310(99)01544-0, PII S1357431099015440
    • Herlaar E, Brown Z (1999) p38MAPK signaling cascades in inflammatory disease. Mol Med Today 5:439-447 (Pubitemid 29455026)
    • (1999) Molecular Medicine Today , vol.5 , Issue.10 , pp. 439-447
    • Herlaar, E.1    Brown, Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.