메뉴 건너뛰기




Volumn 291, Issue 8, 2016, Pages 4197-4210

Functional and structural divergence in human TRPV1 channel subunits by oxidative cysteine modification

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COVALENT BONDS; ELECTROPHYSIOLOGY; MASS SPECTROMETRY; NEURONS; PROTEINS; SPECTROMETRY; SULFUR COMPOUNDS;

EID: 84964561173     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.700278     Document Type: Article
Times cited : (54)

References (58)
  • 1
    • 0347504835 scopus 로고    scopus 로고
    • TRP channels as cellular sensors
    • Clapham, D. E. (2003) TRP channels as cellular sensors. Nature 426, 517-524.
    • (2003) Nature , vol.426 , pp. 517-524
    • Clapham, D.E.1
  • 2
    • 29844451971 scopus 로고    scopus 로고
    • International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels
    • Clapham, D. E., Julius, D., Montell, C., and Schultz, G. (2005) International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels. Pharmacol. Rev. 57, 427-450.
    • (2005) Pharmacol. Rev , vol.57 , pp. 427-450
    • Clapham, D.E.1    Julius, D.2    Montell, C.3    Schultz, G.4
  • 3
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao, M., Cao, E., Julius, D., and Cheng, Y. (2013) Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107-112.
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 4
    • 84905029508 scopus 로고    scopus 로고
    • Redox regulation of transient receptor potential channels
    • Kozai, D., Ogawa, N., and Mori, Y. (2014) Redox regulation of transient receptor potential channels. Antioxid. Redox. Signal. 21, 971-986.
    • (2014) Antioxid. Redox. Signal. , vol.21 , pp. 971-986
    • Kozai, D.1    Ogawa, N.2    Mori, Y.3
  • 5
    • 33745263762 scopus 로고    scopus 로고
    • Reducing and oxidizing agents sensitize heat-activated vanilloid receptor (TRPV1) current
    • Susankova, K., Tousova, K., Vyklicky, L., Teisinger, J., and Vlachova, V. (2006) Reducing and oxidizing agents sensitize heat-activated vanilloid receptor (TRPV1) current. Mol. Pharmacol. 70, 383-394.
    • (2006) Mol. Pharmacol , vol.70 , pp. 383-394
    • Susankova, K.1    Tousova, K.2    Vyklicky, L.3    Teisinger, J.4    Vlachova, V.5
  • 6
    • 55749115431 scopus 로고    scopus 로고
    • Molecular characterization of TRPA1 channel activation by cysteine-reactive inflammatory mediators
    • Takahashi, N., Mizuno, Y., Kozai, D., Yamamoto, S., Kiyonaka, S., Shibata, T., Uchida, K., and Mori, Y. (2008) Molecular characterization of TRPA1 channel activation by cysteine-reactive inflammatory mediators. Channels 2, 287-298.
    • (2008) Channels , vol.2 , pp. 287-298
    • Takahashi, N.1    Mizuno, Y.2    Kozai, D.3    Yamamoto, S.4    Kiyonaka, S.5    Shibata, T.6    Uchida, K.7    Mori, Y.8
  • 9
    • 40449121206 scopus 로고    scopus 로고
    • Transient receptor potential A1 is a sensory receptor for multiple products of oxidative stress
    • Andersson, D. A., Gentry, C., Moss, S., and Bevan, S. (2008) Transient receptor potential A1 is a sensory receptor for multiple products of oxidative stress. J. Neurosci. 28, 2485-2494.
    • (2008) J. Neurosci , vol.28 , pp. 2485-2494
    • Andersson, D.A.1    Gentry, C.2    Moss, S.3    Bevan, S.4
  • 11
    • 84875920432 scopus 로고    scopus 로고
    • Role of TRPA1 and TRPV1 in the reactive oxygen species-dependent sensory irritation of superior laryngeal capsaicin-sensitive afferents by cigarette smoke in anesthetized rats
    • Liu, B. Y., Tsai, T. L., Ho, C. Y., Lu, S. H., Lai, C. J., and Kou, Y. R. (2013) Role of TRPA1 and TRPV1 in the reactive oxygen species-dependent sensory irritation of superior laryngeal capsaicin-sensitive afferents by cigarette smoke in anesthetized rats. Pulm. Pharmacol. Ther. 26, 364-372.
    • (2013) Pulm. Pharmacol. Ther , vol.26 , pp. 364-372
    • Liu, B.Y.1    Tsai, T.L.2    Ho, C.Y.3    Lu, S.H.4    Lai, C.J.5    Kou, Y.R.6
  • 12
    • 0037198410 scopus 로고    scopus 로고
    • Reducing agent dithiothreitol facilitates activity of the capsaicin receptor VR-1
    • Vyklický, L., Lyfenko, A., Susánková, K., Teisinger, J., and Vlachová, V. (2002) Reducing agent dithiothreitol facilitates activity of the capsaicin receptor VR-1. Neuroscience 111, 435-441.
    • (2002) Neuroscience , vol.111 , pp. 435-441
    • Vyklický, L.1    Lyfenko, A.2    Susánková, K.3    Teisinger, J.4    Vlachová, V.5
  • 15
    • 25644433563 scopus 로고    scopus 로고
    • Camphor activates and strongly desensitizes the transient receptor potential vanilloid subtype 1 channel in a vanilloid-independent mechanism
    • Xu, H., Blair, N. T., and Clapham, D. E. (2005) Camphor activates and strongly desensitizes the transient receptor potential vanilloid subtype 1 channel in a vanilloid-independent mechanism. J. Neurosci. 25, 8924-8937.
    • (2005) J. Neurosci , vol.25 , pp. 8924-8937
    • Xu, H.1    Blair, N.T.2    Clapham, D.E.3
  • 17
    • 0034700494 scopus 로고    scopus 로고
    • Induction of vanilloid receptor channel activity by protein kinase C
    • Premkumar, L. S., and Ahern, G. P. (2000) Induction of vanilloid receptor channel activity by protein kinase C. Nature 408, 985-990.
    • (2000) Nature , vol.408 , pp. 985-990
    • Premkumar, L.S.1    Ahern, G.P.2
  • 22
  • 23
    • 33748704531 scopus 로고    scopus 로고
    • TEMPOL, a membrane-permeable radical scavenger, attenuates peroxynitrite- and superoxide anion-enhanced carrageenan- induced paw edema and hyperalgesia: A key role for superoxide anion
    • Khattab, M. M. (2006) TEMPOL, a membrane-permeable radical scavenger, attenuates peroxynitrite- and superoxide anion-enhanced carrageenan- induced paw edema and hyperalgesia: a key role for superoxide anion. Eur. J. Pharmacol. 548, 167-173.
    • (2006) Eur. J. Pharmacol , vol.548 , pp. 167-173
    • Khattab, M.M.1
  • 24
    • 33846131993 scopus 로고    scopus 로고
    • Neutrophils-derived peroxynitrite contributes to acute hyperalgesia and cell influx in zymosan arthritis. Naunyn
    • Bezerra, M. M., Brain, S. D., Girão, V. C., Greenacre, S., Keeble, J., and Rocha, F. A. (2007) Neutrophils-derived peroxynitrite contributes to acute hyperalgesia and cell influx in zymosan arthritis. Naunyn. Schmiedebergs Arch. Pharmacol. 374, 265-273.
    • (2007) Schmiedebergs Arch. Pharmacol , vol.374 , pp. 265-273
    • Bezerra, M.M.1    Brain, S.D.2    Girão, V.C.3    Greenacre, S.4    Keeble, J.5    Rocha, F.A.6
  • 26
    • 73949128944 scopus 로고    scopus 로고
    • Oxidative challenges sensitize the capsaicin receptor by covalent cysteine modification
    • Chuang, H. H., and Lin, S. (2009) Oxidative challenges sensitize the capsaicin receptor by covalent cysteine modification. Proc. Natl. Acad. Sci. U.S.A. 106, 20097-20102.
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 20097-20102
    • Chuang, H.H.1    Lin, S.2
  • 27
    • 81755189017 scopus 로고    scopus 로고
    • C-terminal dimerization activates the nociceptive transduction channel transient receptor potential vanilloid 1
    • Wang, S., and Chuang, H. H. (2011) C-terminal dimerization activates the nociceptive transduction channel transient receptor potential vanilloid 1. J. Biol. Chem. 286, 40601-40607.
    • (2011) J. Biol. Chem , vol.286 , pp. 40601-40607
    • Wang, S.1    Chuang, H.H.2
  • 28
    • 58849148335 scopus 로고    scopus 로고
    • Quantifying the global cellular thiol-disulfide status
    • Hansen, R. E., Roth, D., and Winther, J. R. (2009) Quantifying the global cellular thiol-disulfide status. Proc. Natl. Acad. Sci. U.S.A. 106, 422-427.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 422-427
    • Hansen, R.E.1    Roth, D.2    Winther, J.R.3
  • 29
    • 84863178659 scopus 로고    scopus 로고
    • Identification of in vivo disulfide conformation of TRPA1 ion channel
    • Wang, L., Cvetkov, T. L., Chance, M. R., and Moiseenkova-Bell, V. Y. (2012) Identification of in vivo disulfide conformation of TRPA1 ion channel. J. Biol. Chem. 287, 6169-6176.
    • (2012) J. Biol. Chem , vol.287 , pp. 6169-6176
    • Wang, L.1    Cvetkov, T.L.2    Chance, M.R.3    Moiseenkova-Bell, V.Y.4
  • 30
    • 0027340316 scopus 로고
    • [3H]resiniferatoxin binding by the vanilloid receptor: Species-related differences, effects of temperature and sulfhydryl reagents
    • Szallasi, A., and Blumberg, P. M. (1993) [3H]resiniferatoxin binding by the vanilloid receptor: species-related differences, effects of temperature and sulfhydryl reagents. Naunyn. Schmiedebergs Arch. Pharmacol. 347, 84-91.
    • (1993) Naunyn. Schmiedebergs, Arch. Pharmacol , vol.347 , pp. 84-91
    • Szallasi, A.1    Blumberg, P.M.2
  • 31
    • 0027493969 scopus 로고
    • Vanilloid (capsaicin) receptor in the rat: Positive cooperativity of resiniferatoxin binding and its modulation by reduction and oxidation
    • Szallasi, A., Lewin, N. A., and Blumberg, P. M. (1993) Vanilloid (capsaicin) receptor in the rat: positive cooperativity of resiniferatoxin binding and its modulation by reduction and oxidation. J. Pharmacol. Exp. Ther. 266, 678-683.
    • (1993) J. Pharmacol. Exp. Ther. , vol.266 , pp. 678-683
    • Szallasi, A.1    Lewin, N.A.2    Blumberg, P.M.3
  • 33
    • 0033609964 scopus 로고    scopus 로고
    • Activation of Rac1 increases c-Jun NH2-terminal kinase activity and DNA fragmentation in a calciumdependent manner in rat myoblast cell line H9c2, Biochem
    • Nishida, M., Nagao, T., and Kurose, H. (1999) Activation of Rac1 increases c-Jun NH2-terminal kinase activity and DNA fragmentation in a calciumdependent manner in rat myoblast cell line H9c2. Biochem. Biophys. Res. Commun. 262, 350-354.
    • (1999) Biophys. Res. Commun , vol.262 , pp. 350-354
    • Nishida, M.1    Nagao, T.2    Kurose, H.3
  • 34
    • 0033600808 scopus 로고    scopus 로고
    • Molecular and functional characterization of a novel mouse transient receptor potential protein homologue TRP7. Ca2〈-permeable cation channel that is constitutively activated and enhanced by stimulation of G protein-coupled receptor
    • Okada, T., Inoue, R., Yamazaki, K., Maeda, A., Kurosaki, T., Yamakuni, T., Tanaka, I., Shimizu, S., Ikenaka, K., Imoto, K., and Mori, Y. (1999) Molecular and functional characterization of a novel mouse transient receptor potential protein homologue TRP7. Ca2〈-permeable cation channel that is constitutively activated and enhanced by stimulation of G protein-coupled receptor. J. Biol. Chem. 274, 27359-27370.
    • (1999) J. Biol. Chem , vol.274 , pp. 27359-27370
    • Okada, T.1    Inoue, R.2    Yamazaki, K.3    Maeda, A.4    Kurosaki, T.5    Yamakuni, T.6    Tanaka, I.7    Shimizu, S.8    Ikenaka, K.9    Imoto, K.10    Mori, Y.11
  • 36
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J. K., McCormack, A. L., and Yates, J. R. (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976-989.
    • (1994) J. Am. Soc. Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 40
    • 51949103798 scopus 로고    scopus 로고
    • Heat-induced MMP-1 expression is mediated by TRPV1 through PKCα signaling in HaCaT cells
    • Lee, Y. M., Li, W. H., Kim, Y. K., Kim, K. H., and Chung, J. H. (2008) Heat-induced MMP-1 expression is mediated by TRPV1 through PKCα signaling in HaCaT cells. Exp. Dermatol. 17, 864-870.
    • (2008) Exp. Dermatol , vol.17 , pp. 864-870
    • Lee, Y.M.1    Li, W.H.2    Kim, Y.K.3    Kim, K.H.4    Chung, J.H.5
  • 42
    • 79954952532 scopus 로고    scopus 로고
    • Endocannabinoids modulate human epidermal keratinocyte proliferation and survival via the sequential engagement of cannabinoid receptor-1 and transient receptor potential vanilloid-1
    • Tóth, B. I., Dobrosi, N., Dajnoki, A., Czifra, G., Oláh, A., Szöllosi, A. G., Juhász, I., Sugawara, K., Paus, R., and Bíró, T. (2011) Endocannabinoids modulate human epidermal keratinocyte proliferation and survival via the sequential engagement of cannabinoid receptor-1 and transient receptor potential vanilloid-1. J. Invest. Dermatol. 131, 1095-1104.
    • (2011) J. Invest. Dermatol , vol.131 , pp. 1095-1104
    • Tóth, B.I.1    Dobrosi, N.2    Dajnoki, A.3    Czifra, G.4    Oláh, A.5    Szöllosi, A.G.6    Juhász, I.7    Sugawara, K.8    Paus, R.9    Bíró, T.10
  • 43
    • 84902438344 scopus 로고    scopus 로고
    • Targeting the transient receptor potential vanilloid type 1 (TRPV1) assembly domain attenuates inflammation-induced hypersensitivity
    • Flynn, R., Chapman, K., Iftinca, M., Aboushousha, R., Varela, D., and Altier, C. (2014) Targeting the transient receptor potential vanilloid type 1 (TRPV1) assembly domain attenuates inflammation-induced hypersensitivity. J. Biol. Chem. 289, 16675-16687.
    • (2014) J. Biol. Chem , vol.289 , pp. 16675-16687
    • Flynn, R.1    Chapman, K.2    Iftinca, M.3    Aboushousha, R.4    Varela, D.5    Altier, C.6
  • 44
    • 78651012345 scopus 로고
    • The production, assay, and antibiotic activity of actidione, an antibiotic from Streptomyces griseus
    • Whiffen, A. J. (1948) The production, assay, and antibiotic activity of actidione, an antibiotic from Streptomyces griseus. J. Bacteriol. 56, 283-291.
    • (1948) J. Bacteriol , vol.56 , pp. 283-291
    • Whiffen, A.J.1
  • 45
    • 0342596836 scopus 로고
    • The effect of actidione and other antifungal agents on nucleic acid and protein synthesis in Saccharomyces carlsbergensis
    • Kerridge, D. (1958) The effect of actidione and other antifungal agents on nucleic acid and protein synthesis in Saccharomyces carlsbergensis. J. Gen. Microbiol. 19, 497-506.
    • (1958) J. Gen. Microbiol , vol.19 , pp. 497-506
    • Kerridge, D.1
  • 46
    • 34250190946 scopus 로고    scopus 로고
    • The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity
    • Lishko, P. V., Procko, E., Jin, X., Phelps, C. B., and Gaudet, R. (2007) The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity. Neuron 54, 905-918.
    • (2007) Neuron , vol.54 , pp. 905-918
    • Lishko, P.V.1    Procko, E.2    Jin, X.3    Phelps, C.B.4    Gaudet, R.5
  • 47
    • 0029831704 scopus 로고    scopus 로고
    • Dimerization of TWIK-1 K〈 channel subunits via a disulfide bridge
    • Lesage, F., Reyes, R., Fink, M., Duprat, F., Guillemare, E., and Lazdunski, M. (1996) Dimerization of TWIK-1 K〈 channel subunits via a disulfide bridge. EMBO J. 15, 6400-6407.
    • (1996) EMBO J , vol.15 , pp. 6400-6407
    • Lesage, F.1    Reyes, R.2    Fink, M.3    Duprat, F.4    Guillemare, E.5    Lazdunski, M.6
  • 48
    • 84939880965 scopus 로고    scopus 로고
    • Extracellular disulfide bridges stabilize TRPC5 dimerization, trafficking, and activity
    • Hong, C., Kwak, M., Myeong, J., Ha, K., Wie, J., Jeon, J. H., and So, I. (2015) Extracellular disulfide bridges stabilize TRPC5 dimerization, trafficking, and activity. Pflugers Arch. 467, 703-712.
    • (2015) Pflugers Arch , vol.467 , pp. 703-712
    • Hong, C.1    Kwak, M.2    Myeong, J.3    Ha, K.4    Wie, J.5    Jeon, J.H.6    So, I.7
  • 49
    • 0000504876 scopus 로고    scopus 로고
    • Two critical cysteine residues implicated in disulfide bond formation and proper folding of Kir2.1
    • Cho, H. C., Tsushima, R. G., Nguyen, T. T., Guy, H. R., and Backx, P. H. (2000) Two critical cysteine residues implicated in disulfide bond formation and proper folding of Kir2.1. Biochemistry 39, 4649-4657.
    • (2000) Biochemistry , vol.39 , pp. 4649-4657
    • Cho, H.C.1    Tsushima, R.G.2    Nguyen, T.T.3    Guy, H.R.4    Backx, P.H.5
  • 52
    • 0029860157 scopus 로고    scopus 로고
    • Ligand-binding characteristics and related structural features of the expressed goldfish kainate receptors: Identification of a conserved disulfide bond and three residues important for ligand binding
    • Wo, Z. G., and Oswald, R. E. (1996) Ligand-binding characteristics and related structural features of the expressed goldfish kainate receptors: identification of a conserved disulfide bond and three residues important for ligand binding. Mol. Pharmacol. 50, 770-780.
    • (1996) Mol. Pharmacol , vol.50 , pp. 770-780
    • Wo, Z.G.1    Oswald, R.E.2
  • 53
    • 0028034803 scopus 로고
    • Identification of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor
    • Sullivan, J. M., Traynelis, S. F., Chen, H. S., Escobar, W., Heinemann, S. F., and Lipton, S. A. (1994) Identification of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor. Neuron 13, 929-936.
    • (1994) Neuron , vol.13 , pp. 929-936
    • Sullivan, J.M.1    Traynelis, S.F.2    Chen, H.S.3    Escobar, W.4    Heinemann, S.F.5    Lipton, S.A.6
  • 54
    • 72949091450 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic strong inward-rectifier K〈 channel Kir2.2 at 3.1 A resolution
    • Tao, X., Avalos, J. L., Chen, J., and MacKinnon, R. (2009) Crystal structure of the eukaryotic strong inward-rectifier K〈 channel Kir2.2 at 3.1 A resolution. Science 326, 1668-1674.
    • (2009) Science , vol.326 , pp. 1668-1674
    • Tao, X.1    Avalos, J.L.2    Chen, J.3    MacKinnon, R.4
  • 55
    • 84888301385 scopus 로고    scopus 로고
    • Thiol-blocking electrophiles interfere with labeling and detection of protein sulfenic acids
    • Reisz, J. A., Bechtold, E., King, S. B., Poole, L. B., and Furdui, C. M. (2013) Thiol-blocking electrophiles interfere with labeling and detection of protein sulfenic acids. FEBS J. 280, 6150-6161.
    • (2013) FEBS J , vol.280 , pp. 6150-6161
    • Reisz, J.A.1    Bechtold, E.2    King, S.B.3    Poole, L.B.4    Furdui, C.M.5
  • 57
    • 84860179123 scopus 로고    scopus 로고
    • Redox signal-mediated sensitization of transient receptor potential melastatin 2 (TRPM2) to temperature affects macrophage functions
    • Kashio, M., Sokabe, T., Shintaku, K., Uematsu, T., Fukuta, N., Kobayashi, N., Mori, Y., and Tominaga, M. (2012) Redox signal-mediated sensitization of transient receptor potential melastatin 2 (TRPM2) to temperature affects macrophage functions. Proc. Natl. Acad. Sci. U.S.A. 109, 6745-6750.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 6745-6750
    • Kashio, M.1    Sokabe, T.2    Shintaku, K.3    Uematsu, T.4    Fukuta, N.5    Kobayashi, N.6    Mori, Y.7    Tominaga, M.8
  • 58
    • 58149200910 scopus 로고    scopus 로고
    • Transient receptor potential channels: Targeting pain at the source
    • Patapoutian, A., Tate, S., and Woolf, C. J. (2009) Transient receptor potential channels: targeting pain at the source. Nat. Rev. Drug Discov. 8, 55-68.
    • (2009) Nat. Rev. Drug Discov , vol.8 , pp. 55-68
    • Patapoutian, A.1    Tate, S.2    Woolf, C.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.