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Volumn 5, Issue 4, 2011, Pages

The calmodulin antagonist W-7 inhibits the epithelial Na+/H + exchanger via modulating membrane surface potential

Author keywords

Calmodulin inhibitors; Electrostatic interaction; NHE3; Surface charge; W 7

Indexed keywords

CATION; LIPOSOME; N (6 AMINOHEXYL) 5 CHLORO 1 NAPHTHALENESULFONAMIDE; SODIUM PROTON EXCHANGE PROTEIN 3;

EID: 84855760146     PISSN: 19336950     EISSN: 19336969     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (2)

References (28)
  • 2
    • 69949121187 scopus 로고    scopus 로고
    • NHERF3 (PDZK1) contributes to basal and calcium inhibition of NHE3 activity in Caco-2BBe cells
    • Zachos NC, Li X, Kovbasnjuk O, Hogema B, Sarker R, Lee LJ, et al. NHERF3 (PDZK1) contributes to basal and calcium inhibition of NHE3 activity in Caco-2BBe cells. J Biol Chem 2009; 284:23708-18.
    • (2009) J Biol Chem , vol.284 , pp. 23708-23718
    • Zachos, N.C.1    Li, X.2    Kovbasnjuk, O.3    Hogema, B.4    Sarker, R.5    Lee, L.J.6
  • 5
    • 0242594703 scopus 로고    scopus 로고
    • 2+-dependent inhibition of NHE3 requires PKC alpha which binds to E3KARP to decrease surface NHE3 containing plasma membrane complexes
    • 2+-dependent inhibition of NHE3 requires PKC alpha which binds to E3KARP to decrease surface NHE3 containing plasma membrane complexes. Am J Physiol Cell Physiol 2003; 285:1527-36.
    • (2003) Am J Physiol Cell Physiol , vol.285 , pp. 1527-1536
    • Lee-Kwon, W.1    Kim, J.H.2    Choi, J.W.3    Kawano, K.4    Cha, B.5    Dartt, D.A.6
  • 6
    • 0037189512 scopus 로고    scopus 로고
    • + exchanger 3 (NHE3) requires an NHE3-E3KARP-alpha-actinin-4 complex for oligomerization and endocytosis
    • + exchanger 3 (NHE3) requires an NHE3-E3KARP-alpha-actinin-4 complex for oligomerization and endocytosis. J Biol Chem 2002; 277:23714-24.
    • (2002) J Biol Chem , vol.277 , pp. 23714-23724
    • Kim, J.H.1    Lee-Kwon, W.2    Park, J.B.3    Ryu, S.H.4    Yun, C.H.5    Donowitz, M.6
  • 7
    • 77956243677 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II
    • 2+/calmodulin-dependent protein kinase II. J Biol Chem 2010; 285:27869-78.
    • (2010) J Biol Chem , vol.285 , pp. 27869-27878
    • He, P.1    Klein, J.2    Yun, C.C.3
  • 8
    • 57749112095 scopus 로고    scopus 로고
    • + exchanger NHE3 and activates NHE3 activity in response to calcium
    • + exchanger NHE3 and activates NHE3 activity in response to calcium. J Biol Chem 2008; 283:33544-53.
    • (2008) J Biol Chem , vol.283 , pp. 33544-33553
    • He, P.1    Zhang, H.2    Yun, C.C.3
  • 9
  • 10
    • 57649229838 scopus 로고    scopus 로고
    • Elevated intracellular calcium stimulates NHE3 activity by an IKEPP (NHERF4) dependent mechanism
    • Zachos NC, Hodson C, Kovbasnjuk O, Li X, Thelin WR, Cha B, et al. Elevated intracellular calcium stimulates NHE3 activity by an IKEPP (NHERF4) dependent mechanism. Cell Physiol Biochem 2008; 22:693-704.
    • (2008) Cell Physiol Biochem , vol.22 , pp. 693-704
    • Zachos, N.C.1    Hodson, C.2    Kovbasnjuk, O.3    Li, X.4    Thelin, W.R.5    Cha, B.6
  • 12
    • 0026014910 scopus 로고
    • + exchange by ATP depletion and calmodulin antagonism in renal epithelial cells
    • + exchange by ATP depletion and calmodulin antagonism in renal epithelial cells. Am J Physiol 1991; 261:607-16.
    • (1991) Am J Physiol , vol.261 , pp. 607-616
    • Burns, K.D.1    Homma, T.2    Harris, R.C.3
  • 13
    • 34247189583 scopus 로고    scopus 로고
    • Membrane-permeable calmodulin inhibitors (e.g. W-7/W-13) bind to membranes, changing the electrostatic surface potential: Dual effect of W-13 on epidermal growth factor receptor activation
    • DOI 10.1074/jbc.M607211200
    • Sengupta P, Ruano MJ, Tebar F, Golebiewska U, Zaitseva I, Enrich C, et al. Membrane-permeable calmodulin inhibitors (e.g., W-7/W-13) bind to membranes, changing the electrostatic surface potential: dual effect of W-13 on epidermal growth factor receptor activation. J Biol Chem 2007; 282:8474-86. (Pubitemid 47093617)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.11 , pp. 8474-8486
    • Sengupta, P.1    Ruano, M.J.2    Tebar, F.3    Golebiewska, U.4    Zaitseva, I.5    Enrich, C.6    McLaughlin, S.7    Villalobo, A.8
  • 14
    • 79951812429 scopus 로고    scopus 로고
    • Membrane surface charge dictates the structure and function of the epithelial Na+/H+ exchanger
    • Alexander RT, Jaumouille V, Yeung T, Furuya W, Peltekova I, Boucher A, et al. Membrane surface charge dictates the structure and function of the epithelial Na+/H+ exchanger. EMBO J 2011; 30:679-91.
    • (2011) EMBO J , vol.30 , pp. 679-691
    • Alexander, R.T.1    Jaumouille, V.2    Yeung, T.3    Furuya, W.4    Peltekova, I.5    Boucher, A.6
  • 16
    • 78049370026 scopus 로고    scopus 로고
    • NHE3 activity is dependent on direct phosphoinositide binding at the N terminus of its intracellular cytosolic region
    • Mohan S, Tse CM, Gabelli SB, Sarker R, Cha B, Fahie K, et al. NHE3 activity is dependent on direct phosphoinositide binding at the N terminus of its intracellular cytosolic region. J Biol Chem 2010; 285:34566-78.
    • (2010) J Biol Chem , vol.285 , pp. 34566-34578
    • Mohan, S.1    Tse, C.M.2    Gabelli, S.B.3    Sarker, R.4    Cha, B.5    Fahie, K.6
  • 19
    • 4344578072 scopus 로고    scopus 로고
    • The lateral mobility of NHE3 on the apical membrane of renal epithelial OK cells is limited by the PDZ domain proteins NHERF1/2, but is dependent on an intact actin cytoskeleton as determined by FRAP
    • DOI 10.1242/jcs.01180
    • Cha B, Kenworthy A, Murtazina R, Donowitz M. The lateral mobility of NHE3 on the apical membrane of renal epithelial OK cells is limited by the PDZ domain proteins NHERF1/2, but is dependent on an intact actin cytoskeleton as determined by FRAP. J Cell Sci 2004; 117:3353-65. (Pubitemid 39139919)
    • (2004) Journal of Cell Science , vol.117 , Issue.15 , pp. 3353-3365
    • Cha, B.1    Kenworthy, A.2    Murtazina, R.3    Donowitz, M.4
  • 20
    • 33744779069 scopus 로고    scopus 로고
    • The NHE3 juxtamembrane cytoplasmic domain directly binds ezrin: Dual role in NHE3 trafficking and mobility in the brush border
    • DOI 10.1091/mbc.E05-09-0843
    • Cha B, Tse M, Yun C, Kovbasnjuk O, Mohan S, Hubbard A, et al. The NHE3 juxtamembrane cytoplasmic domain directly binds ezrin: dual role in NHE3 trafficking and mobility in the brush border. Mol Biol Cell 2006; 17:2661-73. (Pubitemid 43825503)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.6 , pp. 2661-2673
    • Cha, B.1    Tse, M.2    Yun, C.3    Kovbasnjuk, O.4    Mohan, S.5    Hubbard, A.6    Arpin, M.7    Donowitz, M.8
  • 21
  • 22
    • 79955140408 scopus 로고    scopus 로고
    • NHERF1 and NHERF2 are necessary for multiple but usually separate aspects of basal and acute regulation of NHE3 activity
    • Sarker R, Valkhoff VE, Zachos NC, Lin R, Cha B, Chen TE, et al. NHERF1 and NHERF2 are necessary for multiple but usually separate aspects of basal and acute regulation of NHE3 activity. Am J Physiol Cell Physiol 2011; 300:771-82.
    • (2011) Am J Physiol Cell Physiol , vol.300 , pp. 771-782
    • Sarker, R.1    Valkhoff, V.E.2    Zachos, N.C.3    Lin, R.4    Cha, B.5    Chen, T.E.6
  • 23
  • 24
    • 0036346708 scopus 로고    scopus 로고
    • ERM proteins and merlin: Integrators at the cell cortex
    • Bretscher A, Edwards K, Fehon RG. ERM proteins and merlin: integrators at the cell cortex. Nat Rev Mol Cell Biol 2002; 3:586-99.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 586-599
    • Bretscher, A.1    Edwards, K.2    Fehon, R.G.3
  • 25
    • 0029121577 scopus 로고
    • Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site
    • Gary R, Bretscher A. Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site. Mol Biol Cell 1995; 6:1061-75.
    • (1995) Mol Biol Cell , vol.6 , pp. 1061-1075
    • Gary, R.1    Bretscher, A.2
  • 27
    • 0037053367 scopus 로고    scopus 로고
    • Topography of helices 5-7 in membrane-inserted diphtheria toxin T domain. Identification and insertion boundaries of two hydrophobic sequences that do not form a stable transmembrane hairpin
    • DOI 10.1074/jbc.M200442200
    • Rosconi MP, London E. Topography of helices 5-7 in membrane-inserted diphtheria toxin T domain: identification and insertion boundaries of two hydrophobic sequences that do not form a stable transmembrane hairpin. J Biol Chem 2002; 277:16517-27. (Pubitemid 34967667)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.19 , pp. 16517-16527
    • Rosconi, M.P.1    London, E.2
  • 28
    • 0018764575 scopus 로고
    • Intracellular pH measurements in Ehrlich ascites tumor cells utilizing spectroscopic probes generated in situ
    • DOI 10.1021/bi00578a012
    • Thomas JA, Buchsbaum RN, Zimniak A, Racker E. Intracellular pH measurements in Ehrlich ascites tumor cells utilizing spectroscopic probes generated in situ. Biochemistry 1979; 18:2210-8. (Pubitemid 9191034)
    • (1979) Biochemistry , vol.18 , Issue.11 , pp. 2210-2218
    • Thomas, J.A.1    Buchsbaum, R.N.2    Zimniak, A.3    Racker, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.