메뉴 건너뛰기




Volumn 593, Issue 15, 2015, Pages 3241-3251

New and notable ion-channels in the sarcoplasmic/endoplasmic reticulum: Do they support the process of intracellular Ca2+ release?

Author keywords

[No Author keywords available]

Indexed keywords

ANION CHANNEL; CALCIUM CHANNEL; CHLORIDE CHANNEL; INOSITOL TRISPHOSPHATE RECEPTOR; ION CHANNEL; MEMBRANE PROTEIN; MITSUGUMIN 23; PANNEXIN; POTASSIUM CHANNEL; PRESENILIN; RECEPTOR PROTEIN; RYANODINE RECEPTOR; TMEM16E PROTEIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL; TRIMERIC INTRACELLULAR CATION PROTEIN; UNCLASSIFIED DRUG;

EID: 84938200751     PISSN: 00223751     EISSN: 14697793     Source Type: Journal    
DOI: 10.1113/jphysiol.2014.281881     Document Type: Review
Times cited : (54)

References (86)
  • 1
    • 0031967058 scopus 로고    scopus 로고
    • 2+-activated anion channel in sarcoplasmic reticulum of skeletal muscle
    • 2+-activated anion channel in sarcoplasmic reticulum of skeletal muscle. Biophys J 74, 2335-2351.
    • (1998) Biophys J , vol.74 , pp. 2335-2351
    • Ahern, G.P.1    Laver, D.R.2
  • 2
    • 77955293473 scopus 로고    scopus 로고
    • Pannexin1 and pannexin2 channels show quaternary similarities to connexons and different oligomerization numbers from each other
    • Ambrosi C, Gassmann O, Pranskevich JN, Boassa D, Smock A, Wang J, Dahl G, Steinem C & Sosinsky GE (2010). Pannexin1 and pannexin2 channels show quaternary similarities to connexons and different oligomerization numbers from each other. J Biol Chem 285, 24420-24431.
    • (2010) J Biol Chem , vol.285 , pp. 24420-24431
    • Ambrosi, C.1    Gassmann, O.2    Pranskevich, J.N.3    Boassa, D.4    Smock, A.5    Wang, J.6    Dahl, G.7    Steinem, C.8    Sosinsky, G.E.9
  • 4
    • 4143127920 scopus 로고    scopus 로고
    • Pannexin membrane channels are mechanosensitive conduits for ATP
    • Bao L, Locovei S & Dahl G (2004). Pannexin membrane channels are mechanosensitive conduits for ATP. FEBS Lett 572, 65-68.
    • (2004) FEBS Lett , vol.572 , pp. 65-68
    • Bao, L.1    Locovei, S.2    Dahl, G.3
  • 5
    • 0021934497 scopus 로고
    • + channel in neutral and negatively charged bilayers
    • + channel in neutral and negatively charged bilayers. Biophys J 48, 349-353.
    • (1985) Biophys J , vol.48 , pp. 349-353
    • Bell, J.1
  • 6
    • 0021309504 scopus 로고
    • + channel of sarcoplasmic reticulum
    • + channel of sarcoplasmic reticulum. Biophys J 45, 279-287.
    • (1984) Biophys J , vol.45 , pp. 279-287
    • Bell, J.E.1    Miller, C.2
  • 7
    • 84894146350 scopus 로고    scopus 로고
    • Cardiac sarcoplasmic reticulum calcium leak: basis and roles in cardiac dysfunction
    • Bers DM (2014). Cardiac sarcoplasmic reticulum calcium leak: basis and roles in cardiac dysfunction. Annu Rev Physiol 76, 107-127.
    • (2014) Annu Rev Physiol , vol.76 , pp. 107-127
    • Bers, D.M.1
  • 12
    • 77949695459 scopus 로고    scopus 로고
    • TRP channels of intracellular membranes
    • Dong X-P, Wang X & Xu H (2010). TRP channels of intracellular membranes. J Neurochem 113, 313-328.
    • (2010) J Neurochem , vol.113 , pp. 313-328
    • Dong, X.-P.1    Wang, X.2    Xu, H.3
  • 13
    • 0035793617 scopus 로고    scopus 로고
    • The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator
    • Dulhunty A, Gage P, Curtis S, Chelvanayagam G & Board P (2001). The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator. J Biol Chem 276, 3319-3323.
    • (2001) J Biol Chem , vol.276 , pp. 3319-3323
    • Dulhunty, A.1    Gage, P.2    Curtis, S.3    Chelvanayagam, G.4    Board, P.5
  • 14
    • 0021879714 scopus 로고
    • Conductance and selectivity properties of a substate of the rabbit sarcoplasmic reticulum channel
    • Fox JA (1985). Conductance and selectivity properties of a substate of the rabbit sarcoplasmic reticulum channel. Biophys J 47, 573-576.
    • (1985) Biophys J , vol.47 , pp. 573-576
    • Fox, J.A.1
  • 16
    • 56049089848 scopus 로고    scopus 로고
    • Intracellular calcium release channels mediate their own countercurrent: the ryanodine receptor case study
    • Gillespie D & Fill M (2008). Intracellular calcium release channels mediate their own countercurrent: the ryanodine receptor case study. Biophys J 95, 3706-3714.
    • (2008) Biophys J , vol.95 , pp. 3706-3714
    • Gillespie, D.1    Fill, M.2
  • 18
    • 84938215672 scopus 로고
    • + channel of rabbit cardiac muscle SR; effect of block by a bis-quaternary ammonium compound
    • + channel of rabbit cardiac muscle SR; effect of block by a bis-quaternary ammonium compound. J Physiol 369, 183P.
    • (1985) J Physiol , vol.369 , pp. 183P
    • Gray, M.A.1    Williams, A.J.2
  • 20
    • 0024555789 scopus 로고
    • Potassium channel of cardiac sarcoplasmic reticulum is a multi-ion channel
    • Hill JA Jr, Coronado R & Strauss HC (1989). Potassium channel of cardiac sarcoplasmic reticulum is a multi-ion channel. Biophys J 55, 35-45.
    • (1989) Biophys J , vol.55 , pp. 35-45
    • Hill Jr, J.A.1    Coronado, R.2    Strauss, H.C.3
  • 25
    • 0031961854 scopus 로고    scopus 로고
    • Changes in luminal pH caused by calcium release in sarcoplasmic reticulum vesicles
    • Kamp F, Donoso P & Hidalgo C (1998). Changes in luminal pH caused by calcium release in sarcoplasmic reticulum vesicles. Biophys J 74, 290-296.
    • (1998) Biophys J , vol.74 , pp. 290-296
    • Kamp, F.1    Donoso, P.2    Hidalgo, C.3
  • 26
    • 0027323146 scopus 로고
    • 2+-calmodulin complex in cardiac sarcoplasmic reticulum
    • 2+-calmodulin complex in cardiac sarcoplasmic reticulum. Circ Res 73, 751-757.
    • (1993) Circ Res , vol.73 , pp. 751-757
    • Kawano, S.1    Hiraoka, M.2
  • 27
    • 0033593216 scopus 로고    scopus 로고
    • Anion permeability and conduction of adenine nucleotides through a chloride channel in cardiac sarcoplasmic reticulum
    • Kawano S, Kuruma A, Hirayama Y & Hiraoka M (1999). Anion permeability and conduction of adenine nucleotides through a chloride channel in cardiac sarcoplasmic reticulum. J Biol Chem 274, 2085-2092.
    • (1999) J Biol Chem , vol.274 , pp. 2085-2092
    • Kawano, S.1    Kuruma, A.2    Hirayama, Y.3    Hiraoka, M.4
  • 28
    • 0026735602 scopus 로고
    • Cardiac sarcoplasmic reticulum chloride channels regulated by protein kinase A
    • Kawano S, Nakamura F, Tanaka T & Hiraoka M (1992). Cardiac sarcoplasmic reticulum chloride channels regulated by protein kinase A. Circ Res 71, 585-589.
    • (1992) Circ Res , vol.71 , pp. 585-589
    • Kawano, S.1    Nakamura, F.2    Tanaka, T.3    Hiraoka, M.4
  • 30
    • 84858114931 scopus 로고    scopus 로고
    • Endoplasmic reticulum potassium-hydrogen exchanger and small conductance calcium-activated potassium channel activities are essential for ER calcium uptake in neurons and cardiomyocytes
    • Kuum M, Veksler V, Liiv J, Ventura-Clapier R & Kaasik A (2012). Endoplasmic reticulum potassium-hydrogen exchanger and small conductance calcium-activated potassium channel activities are essential for ER calcium uptake in neurons and cardiomyocytes. J Cell Sci 125, 625-633.
    • (2012) J Cell Sci , vol.125 , pp. 625-633
    • Kuum, M.1    Veksler, V.2    Liiv, J.3    Ventura-Clapier, R.4    Kaasik, A.5
  • 31
    • 0018960687 scopus 로고
    • +-selective channel from the sarcoplasmic reticulum membrane
    • +-selective channel from the sarcoplasmic reticulum membrane. J Gen Physiol 76, 397-424.
    • (1980) J Gen Physiol , vol.76 , pp. 397-424
    • Labarca, P.1    Coronado, R.2    Miller, C.3
  • 32
    • 0019794177 scopus 로고
    • +-selective, three-state channel from fragmented sarcoplasmic reticulum of frog leg muscle
    • +-selective, three-state channel from fragmented sarcoplasmic reticulum of frog leg muscle. J Membr Biol 61, 31-38.
    • (1981) J Membr Biol , vol.61 , pp. 31-38
    • Labarca, P.1    Miller, C.2
  • 33
    • 77952899083 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator in human muscle: Dysfunction causes abnormal metabolic recovery in exercise
    • Lamhonwah A-M, Bear CE, Huan LJ, Chiaw PK, Ackerley CA & Tein I (2010). Cystic fibrosis transmembrane conductance regulator in human muscle: Dysfunction causes abnormal metabolic recovery in exercise. Ann Neurol 67, 802-808.
    • (2010) Ann Neurol , vol.67 , pp. 802-808
    • Lamhonwah, A.-M.1    Bear, C.E.2    Huan, L.J.3    Chiaw, P.K.4    Ackerley, C.A.5    Tein, I.6
  • 34
    • 0025912604 scopus 로고
    • 2+: Two-binding-site model of blockade
    • 2+: Two-binding-site model of blockade. Biophys J 60, 198-203.
    • (1991) Biophys J , vol.60 , pp. 198-203
    • Liu, Q.Y.1    Strauss, H.C.2
  • 35
    • 0037135534 scopus 로고    scopus 로고
    • 2+ leak from the endoplasmic reticulum of pancreatic acinar cells. Second messenger-activated channels and translocons
    • 2+ leak from the endoplasmic reticulum of pancreatic acinar cells. Second messenger-activated channels and translocons. J Biol Chem 277, 26479-26485.
    • (2002) J Biol Chem , vol.277 , pp. 26479-26485
    • Lomax, R.B.1    Camello, C.2    Van Coppenolle, F.3    Petersen, O.H.4    Tepikin, A.V.5
  • 36
    • 84874830784 scopus 로고    scopus 로고
    • Characterization of functional TRPV1 channels in the sarcoplasmic reticulum of mouse skeletal muscle
    • Lotteau S, Ducreux S, Romestaing C, Legrand C & Van Coppenolle F (2013). Characterization of functional TRPV1 channels in the sarcoplasmic reticulum of mouse skeletal muscle. PLoS ONE 8, e58673.
    • (2013) PLoS ONE , vol.8 , pp. e58673
    • Lotteau, S.1    Ducreux, S.2    Romestaing, C.3    Legrand, C.4    Van Coppenolle, F.5
  • 37
    • 74549203920 scopus 로고    scopus 로고
    • Modulation of the cold-activated cation channel TRPM8 by surface charge screening
    • Mahieu F, Janssens A, Gees M, Talavera K, Nilius B & Voets T (2010). Modulation of the cold-activated cation channel TRPM8 by surface charge screening. J Physiol 588, 315-324.
    • (2010) J Physiol , vol.588 , pp. 315-324
    • Mahieu, F.1    Janssens, A.2    Gees, M.3    Talavera, K.4    Nilius, B.5    Voets, T.6
  • 39
    • 0017797606 scopus 로고
    • Voltage-gated cation conductance channel from fragmented sarcoplasmic reticulum: Steady-state electrical properties
    • Miller C (1978). Voltage-gated cation conductance channel from fragmented sarcoplasmic reticulum: Steady-state electrical properties. J Membr Biol 40, 1-23.
    • (1978) J Membr Biol , vol.40 , pp. 1-23
    • Miller, C.1
  • 41
    • 77954129392 scopus 로고    scopus 로고
    • Familial Alzheimer's disease mutations in presenilins: effects on endoplasmic reticulum calcium homeostasis and correlation with clinical phenotypes
    • Nelson O, Supnet C, Liu H & Bezprozvanny I (2010). Familial Alzheimer's disease mutations in presenilins: effects on endoplasmic reticulum calcium homeostasis and correlation with clinical phenotypes. J Alzheimers Dis 21, 781-793.
    • (2010) J Alzheimers Dis , vol.21 , pp. 781-793
    • Nelson, O.1    Supnet, C.2    Liu, H.3    Bezprozvanny, I.4
  • 42
    • 0031713099 scopus 로고    scopus 로고
    • Mitsugumin23, a novel transmembrane protein on endoplasmic reticulum and nuclear membranes
    • Nishi M, Komazaki S, Iino M, Kangawa K & Takeshima H (1998). Mitsugumin23, a novel transmembrane protein on endoplasmic reticulum and nuclear membranes. FEBS Lett 432, 191-196.
    • (1998) FEBS Lett , vol.432 , pp. 191-196
    • Nishi, M.1    Komazaki, S.2    Iino, M.3    Kangawa, K.4    Takeshima, H.5
  • 43
    • 33845656789 scopus 로고    scopus 로고
    • The human ClC-4 protein, a member of the CLC chloride channel/transporter family, is localized to the endoplasmic reticulum by its N-terminus
    • Okkenhaug H, Weylandt K-H, Carmena D, Wells DJ, Higgins CF & Sardini A (2006). The human ClC-4 protein, a member of the CLC chloride channel/transporter family, is localized to the endoplasmic reticulum by its N-terminus. FASEB J 20, 2390-2392.
    • (2006) FASEB J , vol.20 , pp. 2390-2392
    • Okkenhaug, H.1    Weylandt, K.-H.2    Carmena, D.3    Wells, D.J.4    Higgins, C.F.5    Sardini, A.6
  • 44
    • 65749114825 scopus 로고    scopus 로고
    • The role of CLCA proteins in inflammatory airway disease
    • Patel AC, Brett TJ & Holtzman MJ (2009). The role of CLCA proteins in inflammatory airway disease. Annu Rev Physiol 71, 425-449.
    • (2009) Annu Rev Physiol , vol.71 , pp. 425-449
    • Patel, A.C.1    Brett, T.J.2    Holtzman, M.J.3
  • 45
    • 84900406113 scopus 로고    scopus 로고
    • Structure and Function of TMEM16 Proteins (Anoctamins)
    • Pedemonte N & Galietta LJV (2014). Structure and Function of TMEM16 Proteins (Anoctamins). Physiol Rev 94, 419-459.
    • (2014) Physiol Rev , vol.94 , pp. 419-459
    • Pedemonte, N.1    Galietta, L.J.V.2
  • 46
    • 84904089253 scopus 로고    scopus 로고
    • Pannexin channels and their links to human disease
    • Penuela S, Harland L, Simek J & Laird DW (2014). Pannexin channels and their links to human disease. Biochem J 461, 371-381.
    • (2014) Biochem J , vol.461 , pp. 371-381
    • Penuela, S.1    Harland, L.2    Simek, J.3    Laird, D.W.4
  • 47
    • 0030060113 scopus 로고    scopus 로고
    • Conducting and voltage-dependent behaviors of potassium ion channels reconstituted from diaphragm sarcoplasmic reticulum: Comparison with the cardiac isoform
    • Picher M, Decrouy A & Rousseau E (1996). Conducting and voltage-dependent behaviors of potassium ion channels reconstituted from diaphragm sarcoplasmic reticulum: Comparison with the cardiac isoform. Biochim Biophys Acta 1279, 93-103.
    • (1996) Biochim Biophys Acta , vol.1279 , pp. 93-103
    • Picher, M.1    Decrouy, A.2    Rousseau, E.3
  • 50
    • 0026733025 scopus 로고
    • Reconstitution and regulation of cation-selective channels from cardiac sarcoplasmic reticulum
    • Rousseau E, Chabot H, Beaudry C & Muller B (1992). Reconstitution and regulation of cation-selective channels from cardiac sarcoplasmic reticulum. Mol Cell Biochem 114, 109-117.
    • (1992) Mol Cell Biochem , vol.114 , pp. 109-117
    • Rousseau, E.1    Chabot, H.2    Beaudry, C.3    Muller, B.4
  • 51
    • 0023805595 scopus 로고
    • Properties of single chloride selective channel from sarcoplasmic reticulum
    • Rousseau E, Roberson M & Meissner G (1988). Properties of single chloride selective channel from sarcoplasmic reticulum. Biophys J 16, 143-151.
    • (1988) Biophys J , vol.16 , pp. 143-151
    • Rousseau, E.1    Roberson, M.2    Meissner, G.3
  • 52
    • 84901633705 scopus 로고    scopus 로고
    • A novel deletion mutation involving TMEM38B in a patient with autosomal recessive osteogenesis imperfecta
    • Rubinato E, Morgan A, D'Eustacchio A, Pecile V, Gortani G, Gasparini P & Faletra F (2014). A novel deletion mutation involving TMEM38B in a patient with autosomal recessive osteogenesis imperfecta. Gene 545, 290-292.
    • (2014) Gene , vol.545 , pp. 290-292
    • Rubinato, E.1    Morgan, A.2    D'Eustacchio, A.3    Pecile, V.4    Gortani, G.5    Gasparini, P.6    Faletra, F.7
  • 57
    • 84868129315 scopus 로고    scopus 로고
    • Cell biology and physiology of CLC chloride channels and transporters
    • John Wiley & Sons, Inc.
    • Stauber T, Weinert S & Jentsch TJ (2012). Cell biology and physiology of CLC chloride channels and transporters. In Comprehensive Physiology. John Wiley & Sons, Inc.
    • (2012) Comprehensive Physiology
    • Stauber, T.1    Weinert, S.2    Jentsch, T.J.3
  • 58
    • 78650172970 scopus 로고    scopus 로고
    • Calcium-dependent phospholipid scrambling by TMEM16F
    • Suzuki J, Umeda M, Sims PJ & Nagata S (2010). Calcium-dependent phospholipid scrambling by TMEM16F. Nature 468, 834-838.
    • (2010) Nature , vol.468 , pp. 834-838
    • Suzuki, J.1    Umeda, M.2    Sims, P.J.3    Nagata, S.4
  • 59
    • 0023462497 scopus 로고
    • An anion channel of sarcoplasmic reticulum incorporated into planar lipid bilayers. Single channel behavior and conductance
    • Tanifuji M, Sokabe M & Kasai M (1987). An anion channel of sarcoplasmic reticulum incorporated into planar lipid bilayers. Single channel behavior and conductance. J Membr Biol 99, 103-111.
    • (1987) J Membr Biol , vol.99 , pp. 103-111
    • Tanifuji, M.1    Sokabe, M.2    Kasai, M.3
  • 61
  • 62
    • 0022502935 scopus 로고
    • + channel into liposomes suitable for patch clamp studies
    • + channel into liposomes suitable for patch clamp studies. Pflugers Arch 407, 341-347.
    • (1986) Pflugers Arch , vol.407 , pp. 341-347
    • Tomlins, B.1    Williams, A.J.2
  • 63
    • 0021227253 scopus 로고
    • The characterization of a monovalent cation selective channel of mammalian cardiac muscle sarcoplasmic reticulum
    • Tomlins B, Williams AJ & Montgomery RAP (1984). The characterization of a monovalent cation selective channel of mammalian cardiac muscle sarcoplasmic reticulum. J Membr Biol 80, 191-199.
    • (1984) J Membr Biol , vol.80 , pp. 191-199
    • Tomlins, B.1    Williams, A.J.2    Montgomery, R.A.P.3
  • 64
    • 0028844766 scopus 로고
    • Characterization of a chloride channel reconstituted from cardiac sarcoplasmic reticulum
    • Townsend C & Rosenberg RL (1995). Characterization of a chloride channel reconstituted from cardiac sarcoplasmic reticulum. J Membr Biol 147, 121-136.
    • (1995) J Membr Biol , vol.147 , pp. 121-136
    • Townsend, C.1    Rosenberg, R.L.2
  • 67
    • 0028273499 scopus 로고
    • Calcium modulation of single SR potassium channel currents in heart muscle
    • Uehara A, Yasukochi M & Imanaga I (1994). Calcium modulation of single SR potassium channel currents in heart muscle. J Mol Cell Cardiol 26, 195-202.
    • (1994) J Mol Cell Cardiol , vol.26 , pp. 195-202
    • Uehara, A.1    Yasukochi, M.2    Imanaga, I.3
  • 71
    • 29544450609 scopus 로고    scopus 로고
    • The TRPV1 receptor: target of toxicants and therapeutics
    • Veronesi B & Oortgiesen M (2006). The TRPV1 receptor: target of toxicants and therapeutics. Toxicol Sci 89, 1-3.
    • (2006) Toxicol Sci , vol.89 , pp. 1-3
    • Veronesi, B.1    Oortgiesen, M.2
  • 73
    • 0028229572 scopus 로고
    • Characterization of the potassium channel from frog skeletal muscle sarcoplasmic reticulum membrane
    • Wang J & Best PM (1994). Characterization of the potassium channel from frog skeletal muscle sarcoplasmic reticulum membrane. J Physiol 477, 279-290.
    • (1994) J Physiol , vol.477 , pp. 279-290
    • Wang, J.1    Best, P.M.2
  • 75
    • 84881412454 scopus 로고    scopus 로고
    • Analysis of a pannexin 2-pannexin 1 chimeric protein supports divergent roles for pannexin C-termini in cellular localization
    • Wicki-Stordeur LE, Boyce AKJ & Swayne LA (2013). Analysis of a pannexin 2-pannexin 1 chimeric protein supports divergent roles for pannexin C-termini in cellular localization. Cell Commun Adhes 20, 73-79.
    • (2013) Cell Commun Adhes , vol.20 , pp. 73-79
    • Wicki-Stordeur, L.E.1    Boyce, A.K.J.2    Swayne, L.A.3
  • 78
    • 84876498476 scopus 로고    scopus 로고
    • Protective role of the endoplasmic reticulum protein mitsugumin23 against ultraviolet C-induced cell death
    • Yamashita A, Taniwaki T, Kaikoi Y & Yamazaki T (2013). Protective role of the endoplasmic reticulum protein mitsugumin23 against ultraviolet C-induced cell death. FEBS Lett 587, 1299-1303.
    • (2013) FEBS Lett , vol.587 , pp. 1299-1303
    • Yamashita, A.1    Taniwaki, T.2    Kaikoi, Y.3    Yamazaki, T.4
  • 80
    • 75749130723 scopus 로고    scopus 로고
    • Facilitation of DNA damage-induced apoptosis by endoplasmic reticulum protein mitsugumin23
    • Yamazaki T, Sasaki N, Nishi M & Takeshima H (2010). Facilitation of DNA damage-induced apoptosis by endoplasmic reticulum protein mitsugumin23. Biochem Biophys Res Commun 392, 196-200.
    • (2010) Biochem Biophys Res Commun , vol.392 , pp. 196-200
    • Yamazaki, T.1    Sasaki, N.2    Nishi, M.3    Takeshima, H.4
  • 85
    • 84894437193 scopus 로고    scopus 로고
    • Trimeric intracellular cation channels and sarcoplasmic/endoplasmic reticulum calcium homeostasis
    • Zhou X, Lin P, Yamazaki D, Park KH, Komazaki S, Chen SRW, Takeshima H & Ma J (2014). Trimeric intracellular cation channels and sarcoplasmic/endoplasmic reticulum calcium homeostasis. Circ Res 114, 706-716.
    • (2014) Circ Res , vol.114 , pp. 706-716
    • Zhou, X.1    Lin, P.2    Yamazaki, D.3    Park, K.H.4    Komazaki, S.5    Chen, S.R.W.6    Takeshima, H.7    Ma, J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.