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Volumn 8, Issue 4-6, 2001, Pages 277-281

Calmodulin colocalizes with connexins and plays a direct role in gap junction channel gating

Author keywords

Calmodulin; Channel; Connexin; Fluorescent proteins; Gating; Immunofluorescence

Indexed keywords

CALMODULIN; CONNEXIN 32; FLUORESCENT DYE; GAP JUNCTION PROTEIN; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; MUTANT PROTEIN;

EID: 0035757440     PISSN: 10615385     EISSN: None     Source Type: Journal    
DOI: 10.3109/15419060109080737     Document Type: Article
Times cited : (35)

References (21)
  • 1
    • 0027930117 scopus 로고
    • Micromolar levels of intracellular calcium reduce gap junctional permeability in lens cultures
    • Crow, J. M., et al. 1994. Micromolar levels of intracellular calcium reduce gap junctional permeability in lens cultures. Invest. Ophthalmol. Vis. Sci. 35:3332-3341.
    • (1994) Invest. Ophthalmol. Vis. Sci. , vol.35 , pp. 3332-3341
    • Crow, J.M.1
  • 3
    • 0028828220 scopus 로고
    • Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins. Application to the immunogold labeling of intercellular junctional complexes
    • Fujimoto, K. 1995. Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins. Application to the immunogold labeling of intercellular junctional complexes. J. Cell Sci. 108:3443-3449.
    • (1995) J. Cell Sci. , vol.108 , pp. 3443-3449
    • Fujimoto, K.1
  • 4
    • 0002175975 scopus 로고    scopus 로고
    • Characterization and regulation of gap junction channels in cultured astrocytes
    • eds. D.C Spray and R. Dermietzel, Austin, TX: R.G. Landes Medical Pub. Co.
    • Giaume, C., and Venance, L. 1996. Characterization and regulation of gap junction channels in cultured astrocytes. In Gap Junctions in the Nervous System, eds. D.C Spray and R. Dermietzel, pp. 135-157. Austin, TX: R.G. Landes Medical Pub. Co.
    • (1996) Gap Junctions in the Nervous System , pp. 135-157
    • Giaume, C.1    Venance, L.2
  • 5
    • 0020399716 scopus 로고
    • Liver gap junctions and lens fiber junctions: Comparative analysis and calmodulin interaction
    • Hertzberg, E. L., and Gilula, N. B. 1981. Liver gap junctions and lens fiber junctions: comparative analysis and calmodulin interaction. Cold Spring Harbor Symp. Quant. Biol. 46:639-645.
    • (1981) Cold Spring Harbor Symp. Quant. Biol. , vol.46 , pp. 639-645
    • Hertzberg, E.L.1    Gilula, N.B.2
  • 6
    • 0027448843 scopus 로고
    • Gap junction gating sensitivity to physiological internal calcium regardless of pH in Novikoff hepatoma cells
    • Lazrak, A., and Peracchia, C. 1993. Gap junction gating sensitivity to physiological internal calcium regardless of pH in Novikoff hepatoma cells. Biophys. J. 65:2002-2012.
    • (1993) Biophys. J. , vol.65 , pp. 2002-2012
    • Lazrak, A.1    Peracchia, C.2
  • 7
    • 0028141842 scopus 로고
    • Ca-mediated and independent effects of arachidonic acid on gap junctions and Ca-independent effects of oleic acid and halothane
    • Lazrak, A., et al. 1994. Ca-mediated and independent effects of arachidonic acid on gap junctions and Ca-independent effects of oleic acid and halothane. Biophys. J. 67:1052-1059.
    • (1994) Biophys. J. , vol.67 , pp. 1052-1059
    • Lazrak, A.1
  • 8
    • 0033119289 scopus 로고    scopus 로고
    • It is calmodulin after all! Mediator of the calcium modulation of multiple ion channels
    • Levitan, I. B. 1999. It is calmodulin after all! Mediator of the calcium modulation of multiple ion channels. Neuron 22:645-648.
    • (1999) Neuron , vol.22 , pp. 645-648
    • Levitan, I.B.1
  • 9
    • 0021148916 scopus 로고
    • Communicating junctions and calmodulin. Inhibition of electrical uncoupling in Xenopus embryo by calmidazolium
    • Peracchia, C. 1984. Communicating junctions and calmodulin. Inhibition of electrical uncoupling in Xenopus embryo by calmidazolium. J. Membr. Biol. 81:49-58.
    • (1984) J. Membr. Biol. , vol.81 , pp. 49-58
    • Peracchia, C.1
  • 10
    • 0023127381 scopus 로고
    • Calmodulin-like proteins and communicating junctions. Electrical uncoupling of crayfish axons is inhibited by the calmodulin inhibitor W7 and is not affected by cyclic nucleotides
    • Peracchia, C. 1987. Calmodulin-like proteins and communicating junctions. Electrical uncoupling of crayfish axons is inhibited by the calmodulin inhibitor W7 and is not affected by cyclic nucleotides. Pflügers Arch. 408:379-385.
    • (1987) Pflügers Arch. , vol.408 , pp. 379-385
    • Peracchia, C.1
  • 11
    • 0025092104 scopus 로고
    • Increase in gap junction resistance with acidification in crayfish septate axons is closely related to changes in intracellular calcium but not hydrogen ion concentration
    • Peracchia, C. 1990. Increase in gap junction resistance with acidification in crayfish septate axons is closely related to changes in intracellular calcium but not hydrogen ion concentration. J. Membr. Biol. 113:75-92.
    • (1990) J. Membr. Biol. , vol.113 , pp. 75-92
    • Peracchia, C.1
  • 12
    • 0003324793 scopus 로고
    • A calmodulin inhibitor prevents gap junction crystallization and electrical uncoupling
    • Peracchia, C., et al. 1981. A calmodulin inhibitor prevents gap junction crystallization and electrical uncoupling. J. Cell Biol. 91:124a.
    • (1981) J. Cell Biol. , vol.91
    • Peracchia, C.1
  • 13
    • 0021063967 scopus 로고
    • Is calmodulin involved in the regulation of gap junction permeability?
    • Peracchia, C., et al. 1983. Is calmodulin involved in the regulation of gap junction permeability? Pflügers Arch. 399:152-154.
    • (1983) Pflügers Arch. , vol.399 , pp. 152-154
    • Peracchia, C.1
  • 14
    • 0029964362 scopus 로고    scopus 로고
    • Inhibition of calmodulin expression prevents low-pH-induced gap junction uncoupling in Xenopus oocytes
    • Peracchia, C., et al. 1996. Inhibition of calmodulin expression prevents low-pH-induced gap junction uncoupling in Xenopus oocytes. Plügers Arch. 431:379-387.
    • (1996) Plügers Arch. , vol.431 , pp. 379-387
    • Peracchia, C.1
  • 15
    • 0034714396 scopus 로고    scopus 로고
    • Calmodulin directly gates gap junction channels
    • Peracchia, C., et al. 2000a. Calmodulin directly gates gap junction channels. J. Biol. Chem. 275:26220-26224.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26220-26224
    • Peracchia, C.1
  • 16
    • 0034330496 scopus 로고    scopus 로고
    • Slow gating of gap junction channels and calmodulin
    • Peracchia, C., et al. 2000b. Slow gating of gap junction channels and calmodulin. J. Membr. Biol. 78:55-70.
    • (2000) J. Membr. Biol. , vol.78 , pp. 55-70
    • Peracchia, C.1
  • 17
    • 0030053133 scopus 로고    scopus 로고
    • Activation of myosin light chain kinase and nitric oxide synthase activities by engineered calmodulins with duplicated or exchanged EF hand pairs
    • Persechini, A., et al. 1996. Activation of myosin light chain kinase and nitric oxide synthase activities by engineered calmodulins with duplicated or exchanged EF hand pairs. Biochemistry 35:224-228.
    • (1996) Biochemistry , vol.35 , pp. 224-228
    • Persechini, A.1
  • 18
    • 0032952188 scopus 로고    scopus 로고
    • Direct immunogold labeling of connexins and aquaporin-4 in freeze-fracture replicas of liver, brain, and spinal cord: Factors limiting quantitative analysis
    • Rash, J. E., and Yasumura, T. 1999. Direct immunogold labeling of connexins and aquaporin-4 in freeze-fracture replicas of liver, brain, and spinal cord: factors limiting quantitative analysis. Cell Tissue Res. 296:307-321.
    • (1999) Cell Tissue Res. , vol.296 , pp. 307-321
    • Rash, J.E.1    Yasumura, T.2
  • 19
    • 0030773116 scopus 로고    scopus 로고
    • Connexin 32 of gap junctions contains two cytoplasmic calmodulin-binding domains
    • Török, K., et al. 1997. Connexin 32 of gap junctions contains two cytoplasmic calmodulin-binding domains. Biochem. J. 326:479-483.
    • (1997) Biochem. J. , vol.326 , pp. 479-483
    • Török, K.1
  • 20
    • 0021952348 scopus 로고
    • Interaction of calmodulin and other calcium-modulated proteins with mammalian and arthropod junctional membrane proteins
    • Van Eldick, L. J., et al. 1985. Interaction of calmodulin and other calcium-modulated proteins with mammalian and arthropod junctional membrane proteins. Biochem. Biophys. Res. Comm. 126:825-832.
    • (1985) Biochem. Biophys. Res. Comm. , vol.126 , pp. 825-832
    • Van Eldick, L.J.1
  • 21
    • 0023644895 scopus 로고
    • Topological analysis of the major protein in isolated intact rat liver gap junctions and gap junction-derived single membrane structures
    • Zimmer, D. B., et al. 1987. Topological analysis of the major protein in isolated intact rat liver gap junctions and gap junction-derived single membrane structures. J. Biol. Chem. 262:7751-7763.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7751-7763
    • Zimmer, D.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.