메뉴 건너뛰기




Volumn 292, Issue 4, 2007, Pages

Effect of hydrogen peroxide on ROMK channels in the cortical collecting duct

Author keywords

ERK; K secretion; P38; Protein tyrosine kinase; Superoxide anion

Indexed keywords

CONCANAVALIN A; HYDROGEN PEROXIDE; MEMBRANE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; POTASSIUM CHANNEL; POTASSIUM CHANNEL ROMK; PROTEIN TYROSINE KINASE; SMALL CONDUCTANCE POTASSIUM CHANNEL; UNCLASSIFIED DRUG;

EID: 34147132406     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.00389.2006     Document Type: Article
Times cited : (7)

References (36)
  • 2
    • 0026072063 scopus 로고
    • Luminal vasopressin modulates transport in the rabbit cortical collecting duct
    • Ando Y, Tabei K, Asano Y. Luminal vasopressin modulates transport in the rabbit cortical collecting duct. J Clin Invest 88: 952-959, 1991.
    • (1991) J Clin Invest , vol.88 , pp. 952-959
    • Ando, Y.1    Tabei, K.2    Asano, Y.3
  • 3
    • 33749241885 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase (MAPK) inhibits ROMK-like small conductance K channels in the CCD of K-restricted rats
    • Babilonia E, Li D, Wang ZJ, Sun P, Lin DH, Wang WH. Mitogen-activated protein kinase (MAPK) inhibits ROMK-like small conductance K channels in the CCD of K-restricted rats. J Am Soc Nephrol 17: 2687-2696, 2006.
    • (2006) J Am Soc Nephrol , vol.17 , pp. 2687-2696
    • Babilonia, E.1    Li, D.2    Wang, Z.J.3    Sun, P.4    Lin, D.H.5    Wang, W.H.6
  • 4
    • 15444377564 scopus 로고    scopus 로고
    • Superoxide anions are involved in mediating the effect of low K intake on c-Src expression and renal K secretion in the cortical collecting duct
    • Babilonia E, Wei Y, Sterling H, Kaminski P, Wolin MS, Wang WH. Superoxide anions are involved in mediating the effect of low K intake on c-Src expression and renal K secretion in the cortical collecting duct. J Biol Chem 280: 10790-10796, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 10790-10796
    • Babilonia, E.1    Wei, Y.2    Sterling, H.3    Kaminski, P.4    Wolin, M.S.5    Wang, W.H.6
  • 6
    • 0030053619 scopus 로고    scopus 로고
    • Endogenous reactive oxygen intermediates activate tyrosine kinase in human neutrophils
    • Brumell JH, Burkhardt AL, Bolen JB, Grinstein S. Endogenous reactive oxygen intermediates activate tyrosine kinase in human neutrophils. J Biol Chem 271: 1455-1461, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 1455-1461
    • Brumell, J.H.1    Burkhardt, A.L.2    Bolen, J.B.3    Grinstein, S.4
  • 7
    • 0037073677 scopus 로고    scopus 로고
    • NAD(P)H oxidase-derived hydrogen peroxide mediates endothelial nitric oxide production in response to angiotensin II
    • Cai H, Li Z, Dikalov S, Holland SM, Hwang J, Jo H, Dudley SC Jr, Harrison DG. NAD(P)H oxidase-derived hydrogen peroxide mediates endothelial nitric oxide production in response to angiotensin II. J Biol Chem 277: 48311-48317, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 48311-48317
    • Cai, H.1    Li, Z.2    Dikalov, S.3    Holland, S.M.4    Hwang, J.5    Jo, H.6    Dudley Jr, S.C.7    Harrison, D.G.8
  • 9
    • 0035844273 scopus 로고    scopus 로고
    • c-Jun N-terminal kinase activation by hydrogen peroxide in endothelial cells involves Src-dependent epidermal growth factor receptor transactivation
    • Chen K, Vita JA, Berk BC, Keany JF Jr. c-Jun N-terminal kinase activation by hydrogen peroxide in endothelial cells involves Src-dependent epidermal growth factor receptor transactivation. J Biol Chem 276: 16045-16050, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 16045-16050
    • Chen, K.1    Vita, J.A.2    Berk, B.C.3    Keany Jr, J.F.4
  • 10
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu JM, Tanner KG. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37: 5633-5642, 1998.
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 11
    • 0021752103 scopus 로고
    • Differential acute effects of aldosterone, dexamethasone, and hyperkalemia on distal tubular potassium secretion in the rat kidney
    • Field MJ, Stanton BA, Giebisch GH. Differential acute effects of aldosterone, dexamethasone, and hyperkalemia on distal tubular potassium secretion in the rat kidney. J Clin Invest 74: 1792-1802, 1984.
    • (1984) J Clin Invest , vol.74 , pp. 1792-1802
    • Field, M.J.1    Stanton, B.A.2    Giebisch, G.H.3
  • 12
    • 0031831767 scopus 로고    scopus 로고
    • Renal potassium transport: Mechanisms and regulation
    • Giebisch G. Renal potassium transport: mechanisms and regulation. Am J Physiol Renal Physiol 274: F817-F833, 1998.
    • (1998) Am J Physiol Renal Physiol , vol.274
    • Giebisch, G.1
  • 13
    • 0029970059 scopus 로고    scopus 로고
    • Potassium transport: From clearance to channels and pumps
    • Giebisch G, Wang WH. Potassium transport: from clearance to channels and pumps. Kidney Int 49: 1624-1631, 1996.
    • (1996) Kidney Int , vol.49 , pp. 1624-1631
    • Giebisch, G.1    Wang, W.H.2
  • 15
    • 0023442337 scopus 로고
    • Role of insulin receptor phosphorylation in the insulinomimetic effects of hydrogen peroxide
    • Hayes GR, Lockwood DH. Role of insulin receptor phosphorylation in the insulinomimetic effects of hydrogen peroxide. Proc Natl Acad Sci USA 84: 8115-8119, 1987.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8115-8119
    • Hayes, G.R.1    Lockwood, D.H.2
  • 16
    • 0032546013 scopus 로고    scopus 로고
    • Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gβπ
    • Huang CL, Feng S, Hilgemann DW. Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gβπ. Nature 391: 803-806, 1998.
    • (1998) Nature , vol.391 , pp. 803-806
    • Huang, C.L.1    Feng, S.2    Hilgemann, D.W.3
  • 18
    • 0031875264 scopus 로고    scopus 로고
    • Reaction of nitric oxide with superoxide inhibits basolateral K channels in the rat CCD
    • Lu M, Wang WH. Reaction of nitric oxide with superoxide inhibits basolateral K channels in the rat CCD. Am J Physiol Cell Physiol 275: C309-C316, 1998.
    • (1998) Am J Physiol Cell Physiol , vol.275
    • Lu, M.1    Wang, W.H.2
  • 19
    • 0031438076 scopus 로고    scopus 로고
    • G proteincoupled receptors mediate two functionally distinct pathways of tyrosine phosphorylation in rat 1a fibroblasts
    • Luttrell LM, Daaka Y, Della Rocca GJ, Lefkowitz RJ. G proteincoupled receptors mediate two functionally distinct pathways of tyrosine phosphorylation in rat 1a fibroblasts. J Biol Chem 272: 31648-31656, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 31648-31656
    • Luttrell, L.M.1    Daaka, Y.2    Della Rocca, G.J.3    Lefkowitz, R.J.4
  • 20
    • 0035966052 scopus 로고    scopus 로고
    • Hydrogen peroxide generated during cellular insulin stimulation is integral to activation of the distal insulin signaling cascade in 3T3-L1 adipocytes
    • Mahadev K, Wu X, Zilbering A, Zhu L, Lawrence JTR, Goldstein BJ. Hydrogen peroxide generated during cellular insulin stimulation is integral to activation of the distal insulin signaling cascade in 3T3-L1 adipocytes. J Biol Chem 276: 48662-48669, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 48662-48669
    • Mahadev, K.1    Wu, X.2    Zilbering, A.3    Zhu, L.4    Lawrence, J.T.R.5    Goldstein, B.J.6
  • 21
    • 0035877633 scopus 로고    scopus 로고
    • Insulin-stimulated hydrogen peroxide reversibly inhibits protein tyrosine phosphatase 1B in vivo and enhances the early insulin action cascade
    • Mahadev K, Zilbering A, Zhu L, Goldstein BJ. Insulin-stimulated hydrogen peroxide reversibly inhibits protein tyrosine phosphatase 1B in vivo and enhances the early insulin action cascade. J Biol Chem 276: 21938-21942, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 21938-21942
    • Mahadev, K.1    Zilbering, A.2    Zhu, L.3    Goldstein, B.J.4
  • 24
    • 0023740461 scopus 로고
    • An acute increase of peritubular K stimulates K transport through cell pathways of CCT
    • Muto S, Giebisch G, Sansom S. An acute increase of peritubular K stimulates K transport through cell pathways of CCT. Am J Physiol Renal Fluid Electrolyte Physiol 255: F108-F114, 1988.
    • (1988) Am J Physiol Renal Fluid Electrolyte Physiol , vol.255
    • Muto, S.1    Giebisch, G.2    Sansom, S.3
  • 25
    • 0027522231 scopus 로고
    • Redox regulation of a Src family protein tyrosine kinase p56Lck in T cells
    • Nakamura H, Hori T, Sato N, Sugie K, Kawakami T, Yodoi J. Redox regulation of a Src family protein tyrosine kinase p56Lck in T cells. Oncogene 8: 3133-3139, 1993.
    • (1993) Oncogene , vol.8 , pp. 3133-3139
    • Nakamura, H.1    Hori, T.2    Sato, N.3    Sugie, K.4    Kawakami, T.5    Yodoi, J.6
  • 26
    • 0033385968 scopus 로고    scopus 로고
    • Potassium secretion and the regulation of distal nephron K channels
    • Palmer LG. Potassium secretion and the regulation of distal nephron K channels. Am J Physiol Renal Physiol 277: F821-F825, 1999.
    • (1999) Am J Physiol Renal Physiol , vol.277
    • Palmer, L.G.1
  • 27
    • 0028053842 scopus 로고
    • Regulation of apical K and Na channels and Na/K pumps in rat cortical collecting tubule by dietary K
    • Palmer LG, Antonian L, Frindt G. Regulation of apical K and Na channels and Na/K pumps in rat cortical collecting tubule by dietary K. J Gen Physiol 104: 693-710, 1994.
    • (1994) J Gen Physiol , vol.104 , pp. 693-710
    • Palmer, L.G.1    Antonian, L.2    Frindt, G.3
  • 29
    • 0030898417 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways
    • Robinson MJ, Cobb MH. Mitogen-activated protein kinase pathways. Curr Opin Cell Biol 9: 180-186, 1997.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 180-186
    • Robinson, M.J.1    Cobb, M.H.2
  • 30
    • 0032867462 scopus 로고    scopus 로고
    • Phosphrylation of the insulin receptor kinase by phosphocreatine in combination with hydrogen peroxide the structure basis of redox priming
    • Schmid E, Hotz-Wagenblatt A, Hack V, Droege W. Phosphrylation of the insulin receptor kinase by phosphocreatine in combination with hydrogen peroxide the structure basis of redox priming. FASEB J 13: 1491-1500, 1999.
    • (1999) FASEB J , vol.13 , pp. 1491-1500
    • Schmid, E.1    Hotz-Wagenblatt, A.2    Hack, V.3    Droege, W.4
  • 31
    • 0036048666 scopus 로고    scopus 로고
    • Molecular analysis of mitogenactivated protein kinase signaling pathways induced by reactive oxygen intermediates
    • Schmitz ML, Bacher S, Droge W. Molecular analysis of mitogenactivated protein kinase signaling pathways induced by reactive oxygen intermediates. Methods Enzymol 352: 53-61, 2002.
    • (2002) Methods Enzymol , vol.352 , pp. 53-61
    • Schmitz, M.L.1    Bacher, S.2    Droge, W.3
  • 32
    • 0037040273 scopus 로고    scopus 로고
    • Inhibition of protein-tyrosine phosphatase stimulates the dynamin-dependent endocytosis of ROMK1
    • Sterling H, Lin DH, Gu RM, Dong K, Hebert SC, Wang WH. Inhibition of protein-tyrosine phosphatase stimulates the dynamin-dependent endocytosis of ROMK1. J Biol Chem 277: 4317-4323, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 4317-4323
    • Sterling, H.1    Lin, D.H.2    Gu, R.M.3    Dong, K.4    Hebert, S.C.5    Wang, W.H.6
  • 33
    • 0034607872 scopus 로고    scopus 로고
    • Nerve growth factor-induced neuronal differentiation requires generation of Rac1-regulated reactive oxygen species
    • Suzukawa K, Miura K, Mitsushita J, Resau J, Hirose K, Crystal R, Kamata T. Nerve growth factor-induced neuronal differentiation requires generation of Rac1-regulated reactive oxygen species. J Biol Chem 275: 13175-13178, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 13175-13178
    • Suzukawa, K.1    Miura, K.2    Mitsushita, J.3    Resau, J.4    Hirose, K.5    Crystal, R.6    Kamata, T.7
  • 34
    • 2342475910 scopus 로고    scopus 로고
    • Regulation of renal K transport by dietary K intake
    • Wang W. Regulation of renal K transport by dietary K intake. Annu Rev Med 66: 547-569, 2004.
    • (2004) Annu Rev Med , vol.66 , pp. 547-569
    • Wang, W.1
  • 36
    • 0034880303 scopus 로고    scopus 로고
    • Effect of dietary K intake on the apical small-conductance K channel in the CCD: Role of protein tyrosine kinase
    • Wei Y, Bloom P, Lin DH, Gu RM, Wang WH. Effect of dietary K intake on the apical small-conductance K channel in the CCD: role of protein tyrosine kinase. Am J Physiol Renal Physiol 281: F206-F212, 2001.
    • (2001) Am J Physiol Renal Physiol , vol.281
    • Wei, Y.1    Bloom, P.2    Lin, D.H.3    Gu, R.M.4    Wang, W.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.