메뉴 건너뛰기




Volumn 56, Issue 5, 2014, Pages 311-322

Endoplasmic reticulum stress in insulin resistance and diabetes

Author keywords

Ca2+ leak; Diabetes; Endoplasmic reticulum; Endothelial cells; ER stress; Insulin resistance; SERCA pump

Indexed keywords

CALCIUM CHANNEL; CALCIUM ION; CYSTEINE; CYTOKINE; FATTY ACID DERIVATIVE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SATURATED FATTY ACID; TYROSINE; CALCIUM;

EID: 84912114039     PISSN: 01434160     EISSN: 15321991     Source Type: Journal    
DOI: 10.1016/j.ceca.2014.08.006     Document Type: Review
Times cited : (56)

References (183)
  • 1
    • 64649104158 scopus 로고    scopus 로고
    • Banting lecture from the triumvirate to the ominous octet: a new paradigm for the treatment of type 2 diabetes mellitus
    • Defronzo R.A. Banting lecture from the triumvirate to the ominous octet: a new paradigm for the treatment of type 2 diabetes mellitus. Diabetes 2009, 58:773-795.
    • (2009) Diabetes , vol.58 , pp. 773-795
    • Defronzo, R.A.1
  • 2
    • 84860483727 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum in hepatic lipid homeostasis and stress signaling
    • Fu S., Watkins S.M., Hotamisligil G.S. The role of endoplasmic reticulum in hepatic lipid homeostasis and stress signaling. Cell Metab. 2012, 15:623-634.
    • (2012) Cell Metab. , vol.15 , pp. 623-634
    • Fu, S.1    Watkins, S.M.2    Hotamisligil, G.S.3
  • 3
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • Hotamisligil G.S. Endoplasmic reticulum stress and the inflammatory basis of metabolic disease. Cell 2010, 140:900-917.
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.S.1
  • 7
    • 79961104191 scopus 로고    scopus 로고
    • D4cpv-calsequestrin: a sensitive ratiometric biosensor accurately targeted to the calcium store of skeletal muscle
    • Sztretye M., Yi J., Figueroa L., Zhou J., Royer L., Ríos E. D4cpv-calsequestrin: a sensitive ratiometric biosensor accurately targeted to the calcium store of skeletal muscle. J. Gen. Physiol. 2011, 138:211-229.
    • (2011) J. Gen. Physiol. , vol.138 , pp. 211-229
    • Sztretye, M.1    Yi, J.2    Figueroa, L.3    Zhou, J.4    Royer, L.5    Ríos, E.6
  • 9
    • 0032888705 scopus 로고    scopus 로고
    • Correlated measurements of free and total intracellular calcium concentration in central nervous system neurons
    • Pozzo-Miller L.D., Pivovarova N.B., Connor J.A., Reese T.S., Andrews S.B. Correlated measurements of free and total intracellular calcium concentration in central nervous system neurons. Microsc. Res. Tech. 1999, 46:370-379.
    • (1999) Microsc. Res. Tech. , vol.46 , pp. 370-379
    • Pozzo-Miller, L.D.1    Pivovarova, N.B.2    Connor, J.A.3    Reese, T.S.4    Andrews, S.B.5
  • 10
    • 0031863269 scopus 로고    scopus 로고
    • 2+ pump inhibitors on release channels of intracellular stores
    • 2+ pump inhibitors on release channels of intracellular stores. J. Pharmacol. Exp. Ther. 1998, 285:739-745.
    • (1998) J. Pharmacol. Exp. Ther. , vol.285 , pp. 739-745
    • Dettbarn, C.1    Palade, P.2
  • 11
    • 0021332449 scopus 로고
    • Target size of calcium pump protein from skeletal muscle sarcoplasmic reticulum
    • Hymel L., Maurer A., Berenski C., Jung C.Y., Fleischer S. Target size of calcium pump protein from skeletal muscle sarcoplasmic reticulum. J. Biol. Chem. 1984, 259:4890-4895.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4890-4895
    • Hymel, L.1    Maurer, A.2    Berenski, C.3    Jung, C.Y.4    Fleischer, S.5
  • 12
    • 0030721991 scopus 로고    scopus 로고
    • 2+ pump in endothelium: implications to coronary artery function
    • 2+ pump in endothelium: implications to coronary artery function. Am. J. Physiol. 1997, 273:C1250-C1258.
    • (1997) Am. J. Physiol. , vol.273 , pp. C1250-C1258
    • Grover, A.K.1    Samson, S.E.2
  • 14
    • 84860740016 scopus 로고    scopus 로고
    • Diabetes alters intracellular calcium transients in cardiac endothelial cells
    • Sheikh A.Q., Hurley J.R., Huang W., Taghian T., Kogan A., Cho H., et al. Diabetes alters intracellular calcium transients in cardiac endothelial cells. PLOS ONE 2012, 7:e36840.
    • (2012) PLOS ONE , vol.7 , pp. e36840
    • Sheikh, A.Q.1    Hurley, J.R.2    Huang, W.3    Taghian, T.4    Kogan, A.5    Cho, H.6
  • 16
    • 59849120392 scopus 로고    scopus 로고
    • Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum
    • Michalak M., Groenendyk J., Szabo E., Gold L.I., Opas M. Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem. J 2009, 417:651-666.
    • (2009) Biochem. J , vol.417 , pp. 651-666
    • Michalak, M.1    Groenendyk, J.2    Szabo, E.3    Gold, L.I.4    Opas, M.5
  • 17
    • 78650673284 scopus 로고    scopus 로고
    • Massive alterations of sarcoplasmic reticulum free calcium in skeletal muscle fibers lacking calsequestrin revealed by a genetically encoded probe
    • Canato M., Scorzeto M., Giacomello M., Protasi F., Reggiani C., Stienen G.J.M. Massive alterations of sarcoplasmic reticulum free calcium in skeletal muscle fibers lacking calsequestrin revealed by a genetically encoded probe. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:22326-22331.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 22326-22331
    • Canato, M.1    Scorzeto, M.2    Giacomello, M.3    Protasi, F.4    Reggiani, C.5    Stienen, G.J.M.6
  • 18
    • 0030982434 scopus 로고    scopus 로고
    • High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system. Electron energy loss imaging analysis of quick frozen-freeze dried PC12 cells
    • Pezzati R., Bossi M., Podini P., Meldolesi J., Grohovaz F. High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system. Electron energy loss imaging analysis of quick frozen-freeze dried PC12 cells. Mol. Biol. Cell 1997, 8:1501-1512.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1501-1512
    • Pezzati, R.1    Bossi, M.2    Podini, P.3    Meldolesi, J.4    Grohovaz, F.5
  • 19
    • 0034329460 scopus 로고    scopus 로고
    • The endoplasmic reticulum as one continuous Ca(2+) pool: visualization of rapid Ca(2+) movements and equilibration
    • Park M.K., Petersen O.H., Tepikin A.V. The endoplasmic reticulum as one continuous Ca(2+) pool: visualization of rapid Ca(2+) movements and equilibration. EMBO J. 2000, 19:5729-5739.
    • (2000) EMBO J. , vol.19 , pp. 5729-5739
    • Park, M.K.1    Petersen, O.H.2    Tepikin, A.V.3
  • 20
    • 0037195869 scopus 로고    scopus 로고
    • Calreticulin differentially modulates calcium uptake and release in the endoplasmic reticulum and mitochondria
    • Arnaudeau S., Frieden M., Nakamura K., Castelbou C., Michalak M., Demaurex N. Calreticulin differentially modulates calcium uptake and release in the endoplasmic reticulum and mitochondria. J. Biol. Chem. 2002, 277:46696-46705.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46696-46705
    • Arnaudeau, S.1    Frieden, M.2    Nakamura, K.3    Castelbou, C.4    Michalak, M.5    Demaurex, N.6
  • 21
    • 84954358020 scopus 로고    scopus 로고
    • Calreticulin regulates insulin receptor expression and its downstream PI3 kinase/Akt signalling pathway
    • Jalali S., Aghasi M., Yeganeh B., Mesaeli N. Calreticulin regulates insulin receptor expression and its downstream PI3 kinase/Akt signalling pathway. Biochim. Biophys. Acta 2008, 1783:2344-2351.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 2344-2351
    • Jalali, S.1    Aghasi, M.2    Yeganeh, B.3    Mesaeli, N.4
  • 22
    • 84862777270 scopus 로고    scopus 로고
    • Structural and functional conservation of key domains in InsP3 and ryanodine receptors
    • Seo M.-D., Velamakanni S., Ishiyama N., Stathopulos P.B., Rossi A.M., Khan S.A., et al. Structural and functional conservation of key domains in InsP3 and ryanodine receptors. Nature 2012, 483:108-112.
    • (2012) Nature , vol.483 , pp. 108-112
    • Seo, M.-D.1    Velamakanni, S.2    Ishiyama, N.3    Stathopulos, P.B.4    Rossi, A.M.5    Khan, S.A.6
  • 25
    • 0028925223 scopus 로고
    • The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues
    • Giannini G., Conti A., Mammarella S., Scrobogna M., Sorrentino V. The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues. J. Cell Biol. 1995, 128:893-904.
    • (1995) J. Cell Biol. , vol.128 , pp. 893-904
    • Giannini, G.1    Conti, A.2    Mammarella, S.3    Scrobogna, M.4    Sorrentino, V.5
  • 26
    • 4043099050 scopus 로고    scopus 로고
    • Localization of ryanodine receptor 3 in the sinus endothelial cells of the rat spleen
    • Uehara K., Onoue H., Jeyakumar L.H., Fleischer S., Uehara A. Localization of ryanodine receptor 3 in the sinus endothelial cells of the rat spleen. Cell Tissue Res. 2004, 317:137-145.
    • (2004) Cell Tissue Res. , vol.317 , pp. 137-145
    • Uehara, K.1    Onoue, H.2    Jeyakumar, L.H.3    Fleischer, S.4    Uehara, A.5
  • 27
    • 0035005391 scopus 로고    scopus 로고
    • Expression of ryanodine receptor type 3 and TRP channels in endothelial cells: comparison of in situ and cultured human endothelial cells
    • Köhler R., Brakemeier S., Kühn M., Degenhardt C., Buhr H., Pries A., et al. Expression of ryanodine receptor type 3 and TRP channels in endothelial cells: comparison of in situ and cultured human endothelial cells. Cardiovasc. Res. 2001, 51:160-168.
    • (2001) Cardiovasc. Res. , vol.51 , pp. 160-168
    • Köhler, R.1    Brakemeier, S.2    Kühn, M.3    Degenhardt, C.4    Buhr, H.5    Pries, A.6
  • 31
    • 79956196405 scopus 로고    scopus 로고
    • Protein kinase CbetaII-mediated phosphorylation of endothelial nitric oxide synthase threonine 495 mediates the endothelial dysfunction induced by FK506 (tacrolimus)
    • Chiasson V.L., Quinn M.A., Young K.J., Mitchell B.M. Protein kinase CbetaII-mediated phosphorylation of endothelial nitric oxide synthase threonine 495 mediates the endothelial dysfunction induced by FK506 (tacrolimus). J. Pharmacol. Exp. Ther. 2011, 337:718-723.
    • (2011) J. Pharmacol. Exp. Ther. , vol.337 , pp. 718-723
    • Chiasson, V.L.1    Quinn, M.A.2    Young, K.J.3    Mitchell, B.M.4
  • 32
    • 78549238600 scopus 로고    scopus 로고
    • Acidic NAADP-sensitive calcium stores in the endothelium: agonist-specific recruitment and role in regulating blood pressure
    • Brailoiu G.C., Gurzu B., Gao X., Parkesh R., Aley P.K., Trifa D.I., et al. Acidic NAADP-sensitive calcium stores in the endothelium: agonist-specific recruitment and role in regulating blood pressure. J. Biol. Chem. 2010, 285:37133-37137.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37133-37137
    • Brailoiu, G.C.1    Gurzu, B.2    Gao, X.3    Parkesh, R.4    Aley, P.K.5    Trifa, D.I.6
  • 33
    • 4544220704 scopus 로고    scopus 로고
    • Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity
    • Um S.H., Frigerio F., Watanabe M., Picard F., Joaquin M., Sticker M., et al. Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity. Nature 2004, 431:200-205.
    • (2004) Nature , vol.431 , pp. 200-205
    • Um, S.H.1    Frigerio, F.2    Watanabe, M.3    Picard, F.4    Joaquin, M.5    Sticker, M.6
  • 34
    • 69249218908 scopus 로고    scopus 로고
    • Variable luminal sarcoplasmic reticulum Ca(2+) buffer capacity in smooth muscle cells
    • Dagnino-Acosta A., Guerrero-Hernández A. Variable luminal sarcoplasmic reticulum Ca(2+) buffer capacity in smooth muscle cells. Cell Calcium 2009, 46:188-196.
    • (2009) Cell Calcium , vol.46 , pp. 188-196
    • Dagnino-Acosta, A.1    Guerrero-Hernández, A.2
  • 37
    • 84880167897 scopus 로고    scopus 로고
    • Regulators of calcium homeostasis identified by inference of kinetic model parameters from live single cells perturbed by siRNA
    • Bandara S., Malmersjö S., Meyer T. Regulators of calcium homeostasis identified by inference of kinetic model parameters from live single cells perturbed by siRNA. Sci. Signal. 2013, 6:ra56.
    • (2013) Sci. Signal. , vol.6 , pp. ra56
    • Bandara, S.1    Malmersjö, S.2    Meyer, T.3
  • 38
    • 17644363740 scopus 로고    scopus 로고
    • 2+ signaling in HEK-293 and skeletal muscle cells expressing recombinant ryanodine receptors harboring malignant hyperthermia and central core disease mutations
    • 2+ signaling in HEK-293 and skeletal muscle cells expressing recombinant ryanodine receptors harboring malignant hyperthermia and central core disease mutations. J. Biol. Chem. 2005, 280:15380-15389.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15380-15389
    • Brini, M.1    Manni, S.2    Pierobon, N.3    Du, G.G.4    Sharma, P.5    MacLennan, D.H.6
  • 39
    • 11844284861 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum
    • Oakes S.A., Scorrano L., Opferman J.T., Bassik M.C., Nishino M., Pozzan T., et al. Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:105-110.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 105-110
    • Oakes, S.A.1    Scorrano, L.2    Opferman, J.T.3    Bassik, M.C.4    Nishino, M.5    Pozzan, T.6
  • 42
    • 79955999336 scopus 로고    scopus 로고
    • InsP3 receptors and Orai channels in pancreatic acinar cells: co-localization and its consequences
    • Lur G., Sherwood M.W., Ebisui E., Haynes L., Feske S., Sutton R., et al. InsP3 receptors and Orai channels in pancreatic acinar cells: co-localization and its consequences. Biochem. J 2011, 436:231-239.
    • (2011) Biochem. J , vol.436 , pp. 231-239
    • Lur, G.1    Sherwood, M.W.2    Ebisui, E.3    Haynes, L.4    Feske, S.5    Sutton, R.6
  • 46
    • 0036319111 scopus 로고    scopus 로고
    • The ryanodine receptor calcium channel of b cells: molecular regulation and physiological significance
    • Islam M.S. The ryanodine receptor calcium channel of b cells: molecular regulation and physiological significance. Diabetes 2002, 51:1299-1309.
    • (2002) Diabetes , vol.51 , pp. 1299-1309
    • Islam, M.S.1
  • 47
    • 84874905830 scopus 로고    scopus 로고
    • Effects of CaMKII-mediated phosphorylation of ryanodine receptor type 2 on islet calcium handling, insulin secretion, and glucose tolerance
    • Dixit S.S., Wang T., Manzano E.J.Q., Yoo S., Lee J., Chiang D.Y., et al. Effects of CaMKII-mediated phosphorylation of ryanodine receptor type 2 on islet calcium handling, insulin secretion, and glucose tolerance. PLOS ONE 2013, 8:e58655.
    • (2013) PLOS ONE , vol.8 , pp. e58655
    • Dixit, S.S.1    Wang, T.2    Manzano, E.J.Q.3    Yoo, S.4    Lee, J.5    Chiang, D.Y.6
  • 49
    • 34250791617 scopus 로고    scopus 로고
    • Removal of FKBP12/12.6 from endothelial ryanodine receptors leads to an intracellular calcium leak and endothelial dysfunction
    • Long C., Cook L.G., Wu G.-Y., Mitchell B.M. Removal of FKBP12/12.6 from endothelial ryanodine receptors leads to an intracellular calcium leak and endothelial dysfunction. Arterioscler. Thromb. Vasc. Biol. 2007, 27:1580-1586.
    • (2007) Arterioscler. Thromb. Vasc. Biol. , vol.27 , pp. 1580-1586
    • Long, C.1    Cook, L.G.2    Wu, G.-Y.3    Mitchell, B.M.4
  • 50
    • 77955562391 scopus 로고    scopus 로고
    • Ryanodine receptor channelopathies
    • Betzenhauser M.J., Marks A.R. Ryanodine receptor channelopathies. Pflugers Arch. 2010, 460:467-480.
    • (2010) Pflugers Arch. , vol.460 , pp. 467-480
    • Betzenhauser, M.J.1    Marks, A.R.2
  • 52
    • 0037135534 scopus 로고    scopus 로고
    • Basal and physiological Ca(2+) leak from the endoplasmic reticulum of pancreatic acinar cells. Second messenger-activated channels and translocons
    • Lomax R.B., Camello C., Van Coppenolle F., Petersen O.H., Tepikin A.V. Basal and physiological Ca(2+) leak from the endoplasmic reticulum of pancreatic acinar cells. Second messenger-activated channels and translocons. J. Biol. Chem. 2002, 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
  • 54
    • 33847136350 scopus 로고    scopus 로고
    • Intracellular Ca(2+) release via the ER translocon activates store-operated calcium entry
    • Ong H.L., Liu X., Sharma A., Hegde R.S., Ambudkar I.S. Intracellular Ca(2+) release via the ER translocon activates store-operated calcium entry. Pflugers Arch. 2007, 453:797-808.
    • (2007) Pflugers Arch. , vol.453 , pp. 797-808
    • Ong, H.L.1    Liu, X.2    Sharma, A.3    Hegde, R.S.4    Ambudkar, I.S.5
  • 57
    • 84889594608 scopus 로고    scopus 로고
    • TRPV1 structures in distinct conformations reveal activation mechanisms
    • Cao E., Liao M., Cheng Y., Julius D. TRPV1 structures in distinct conformations reveal activation mechanisms. Nature 2013, 504:113-118.
    • (2013) Nature , vol.504 , pp. 113-118
    • Cao, E.1    Liao, M.2    Cheng, Y.3    Julius, D.4
  • 59
    • 0038414614 scopus 로고    scopus 로고
    • Discrimination of intracellular calcium store subcompartments using TRPV1 (transient receptor potential channel, vanilloid subfamily member 1) release channel activity
    • Turner H., Fleig A., Stokes A., Kinet J., Penner R. Discrimination of intracellular calcium store subcompartments using TRPV1 (transient receptor potential channel, vanilloid subfamily member 1) release channel activity. Biochem. J 2003, 371:341-350.
    • (2003) Biochem. J , vol.371 , pp. 341-350
    • Turner, H.1    Fleig, A.2    Stokes, A.3    Kinet, J.4    Penner, R.5
  • 60
    • 84857784321 scopus 로고    scopus 로고
    • TRPV1 activation improves exercise endurance and energy metabolism through PGC-1α upregulation in mice
    • Luo Z., Ma L., Zhao Z., He H., Yang D., Feng X., et al. TRPV1 activation improves exercise endurance and energy metabolism through PGC-1α upregulation in mice. Cell Res. 2012, 22:551-564.
    • (2012) Cell Res. , vol.22 , pp. 551-564
    • Luo, Z.1    Ma, L.2    Zhao, Z.3    He, H.4    Yang, D.5    Feng, X.6
  • 62
    • 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. Characterization of functional TRPV1 channels in the sarcoplasmic reticulum of mouse skeletal muscle. PLOS ONE 2013, 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
  • 63
    • 84872055469 scopus 로고    scopus 로고
    • Activation of calcium signaling through Trpv1 by nNOS and peroxynitrite as a key trigger of skeletal muscle hypertrophy
    • Ito N., Ruegg U.T., Kudo A., Miyagoe-Suzuki Y., Takeda S. Activation of calcium signaling through Trpv1 by nNOS and peroxynitrite as a key trigger of skeletal muscle hypertrophy. Nat. Med. 2013, 19:101-106.
    • (2013) Nat. Med. , vol.19 , pp. 101-106
    • Ito, N.1    Ruegg, U.T.2    Kudo, A.3    Miyagoe-Suzuki, Y.4    Takeda, S.5
  • 66
  • 70
    • 84860774401 scopus 로고    scopus 로고
    • TMBIM3/GRINA is a novel unfolded protein response (UPR) target gene that controls apoptosis through the modulation of ER calcium homeostasis
    • Rojas-Rivera D., Armisén R., Colombo A., Martínez G., Eguiguren A.L., Díaz A., et al. TMBIM3/GRINA is a novel unfolded protein response (UPR) target gene that controls apoptosis through the modulation of ER calcium homeostasis. Cell Death Differ. 2012, 19:1013-1026.
    • (2012) Cell Death Differ. , vol.19 , pp. 1013-1026
    • Rojas-Rivera, D.1    Armisén, R.2    Colombo, A.3    Martínez, G.4    Eguiguren, A.L.5    Díaz, A.6
  • 73
    • 58149333308 scopus 로고    scopus 로고
    • Stim1 and Orai1 mediate CRAC currents and store-operated calcium entry important for endothelial cell proliferation
    • Abdullaev I.F., Bisaillon J.M., Potier M., Gonzalez J.C., Motiani R.K., Trebak M. Stim1 and Orai1 mediate CRAC currents and store-operated calcium entry important for endothelial cell proliferation. Circ. Res. 2008, 103:1289-1299.
    • (2008) Circ. Res. , vol.103 , pp. 1289-1299
    • Abdullaev, I.F.1    Bisaillon, J.M.2    Potier, M.3    Gonzalez, J.C.4    Motiani, R.K.5    Trebak, M.6
  • 74
    • 0026594980 scopus 로고
    • Depletion of intracellular calcium stores activates a calcium current in mast cells
    • Hoth M., Penner R. Depletion of intracellular calcium stores activates a calcium current in mast cells. Nature 1992, 355:353-356.
    • (1992) Nature , vol.355 , pp. 353-356
    • Hoth, M.1    Penner, R.2
  • 75
    • 0022575011 scopus 로고
    • A model for receptor-regulated calcium entry
    • Putney J. A model for receptor-regulated calcium entry. Cell Calcium 1986, 7:1-12.
    • (1986) Cell Calcium , vol.7 , pp. 1-12
    • Putney, J.1
  • 76
    • 84865657973 scopus 로고    scopus 로고
    • Phospholipase C signaling and calcium in flux
    • Putney J.W., Tomita T. Phospholipase C signaling and calcium in flux. Adv. Enzyme Regul. 2012, 52:152-164.
    • (2012) Adv. Enzyme Regul. , vol.52 , pp. 152-164
    • Putney, J.W.1    Tomita, T.2
  • 77
    • 79952040276 scopus 로고    scopus 로고
    • 2+ entry both by store-dependent, STIM1/Orai1-mediated, and store-independent, TRPC3/PLC/PKC-mediated pathways in human endothelial cells
    • 2+ entry both by store-dependent, STIM1/Orai1-mediated, and store-independent, TRPC3/PLC/PKC-mediated pathways in human endothelial cells. Cell Calcium 2011, 49:115-127.
    • (2011) Cell Calcium , vol.49 , pp. 115-127
    • Antigny, F.1    Jousset, H.2    König, S.3    Frieden, M.4
  • 78
    • 70349116421 scopus 로고    scopus 로고
    • 2+ entry in the immune system and beyond
    • 2+ entry in the immune system and beyond. Immunol. Rev. 2009, 231:189-209.
    • (2009) Immunol. Rev. , vol.231 , pp. 189-209
    • Feske, S.1
  • 82
    • 33748569838 scopus 로고    scopus 로고
    • 2+ store depletion causes STIM1 to accumulate in ER regions closely associated with the plasma membrane
    • 2+ store depletion causes STIM1 to accumulate in ER regions closely associated with the plasma membrane. J. Cell Biol. 2006, 174:803-813.
    • (2006) J. Cell Biol. , vol.174 , pp. 803-813
    • Wu, M.M.1    Buchanan, J.2    Luik, R.M.3    Lewis, R.S.4
  • 85
    • 61349137530 scopus 로고    scopus 로고
    • STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1
    • Park C.Y., Hoover P.J., Mullins F.M., Bachhawat P., Covington E.D., Raunser S., et al. STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1. Cell 2009, 136:876-890.
    • (2009) Cell , vol.136 , pp. 876-890
    • Park, C.Y.1    Hoover, P.J.2    Mullins, F.M.3    Bachhawat, P.4    Covington, E.D.5    Raunser, S.6
  • 86
    • 84866089398 scopus 로고    scopus 로고
    • Store-independent pathways for cytosolic STIM1 clustering in the regulation of store-operated Ca(2+) influx
    • Zeng B., Chen G.-L., Xu S.-Z. Store-independent pathways for cytosolic STIM1 clustering in the regulation of store-operated Ca(2+) influx. Biochem. Pharmacol. 2012, 84:1024-1035.
    • (2012) Biochem. Pharmacol. , vol.84 , pp. 1024-1035
    • Zeng, B.1    Chen, G.-L.2    Xu, S.-Z.3
  • 87
    • 84893842589 scopus 로고    scopus 로고
    • Distinct Orai-coupling domains in STIM1 and STIM2 define the Orai-activating site
    • Wang X., Wang Y., Zhou Y., Hendron E., Mancarella S., Andrake M.D., et al. Distinct Orai-coupling domains in STIM1 and STIM2 define the Orai-activating site. Nat. Commun. 2014, 5:3183.
    • (2014) Nat. Commun. , vol.5 , pp. 3183
    • Wang, X.1    Wang, Y.2    Zhou, Y.3    Hendron, E.4    Mancarella, S.5    Andrake, M.D.6
  • 89
    • 33646576875 scopus 로고    scopus 로고
    • A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function
    • Feske S., Gwack Y., Prakriya M., Srikanth S., Puppel S.-H., Tanasa B., et al. A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function. Nature 2006, 441:179-185.
    • (2006) Nature , vol.441 , pp. 179-185
    • Feske, S.1    Gwack, Y.2    Prakriya, M.3    Srikanth, S.4    Puppel, S.-H.5    Tanasa, B.6
  • 90
    • 80052304048 scopus 로고    scopus 로고
    • Remodelling of the endoplasmic reticulum during store-operated calcium entry
    • Shen W., Frieden M., Demaurex N. Remodelling of the endoplasmic reticulum during store-operated calcium entry. Biol. Cell. 2011, 103:365-380.
    • (2011) Biol. Cell. , vol.103 , pp. 365-380
    • Shen, W.1    Frieden, M.2    Demaurex, N.3
  • 92
    • 78650324846 scopus 로고    scopus 로고
    • Resting state Orai1 diffuses as homotetramer in the plasma membrane of live mammalian cells
    • Madl J., Weghuber J., Fritsch R., Derler I., Fahrner M., Frischauf I., et al. Resting state Orai1 diffuses as homotetramer in the plasma membrane of live mammalian cells. J. Biol. Chem. 2010, 285:41135-41142.
    • (2010) J. Biol. Chem. , vol.285 , pp. 41135-41142
    • Madl, J.1    Weghuber, J.2    Fritsch, R.3    Derler, I.4    Fahrner, M.5    Frischauf, I.6
  • 93
    • 84870655957 scopus 로고    scopus 로고
    • Crystal structure of the calcium release-activated calcium channel Orai
    • Hou X., Pedi L., Diver M.M., Long S.B. Crystal structure of the calcium release-activated calcium channel Orai. Science 2012, 338:1308-1313.
    • (2012) Science , vol.338 , pp. 1308-1313
    • Hou, X.1    Pedi, L.2    Diver, M.M.3    Long, S.B.4
  • 95
    • 33748655172 scopus 로고    scopus 로고
    • Molecular identification of the CRAC channel by altered ion selectivity in a mutant of Orai
    • Yeromin A.V., Zhang S.L., Jiang W., Yu Y., Safrina O., Cahalan M.D. Molecular identification of the CRAC channel by altered ion selectivity in a mutant of Orai. Nature 2006, 443:226-229.
    • (2006) Nature , vol.443 , pp. 226-229
    • Yeromin, A.V.1    Zhang, S.L.2    Jiang, W.3    Yu, Y.4    Safrina, O.5    Cahalan, M.D.6
  • 97
    • 77957733927 scopus 로고    scopus 로고
    • The N-terminal domain of Orai3 determines selectivity for activation of the store-independent ARC channel by arachidonic acid
    • Thompson J., Mignen O., Shuttleworth T.J. The N-terminal domain of Orai3 determines selectivity for activation of the store-independent ARC channel by arachidonic acid. Channels (Austin) 2010, 4:398-410.
    • (2010) Channels (Austin) , vol.4 , pp. 398-410
    • Thompson, J.1    Mignen, O.2    Shuttleworth, T.J.3
  • 100
    • 33748548406 scopus 로고    scopus 로고
    • 2+ entry: local activation of CRAC channels by STIM1 at ER-plasma membrane junctions
    • 2+ entry: local activation of CRAC channels by STIM1 at ER-plasma membrane junctions. J. Cell Biol. 2006, 174:815-825.
    • (2006) J. Cell Biol. , vol.174 , pp. 815-825
    • Luik, R.M.1    Wu, M.M.2    Buchanan, J.3    Lewis, R.S.4
  • 101
    • 33750056991 scopus 로고    scopus 로고
    • Aggregation of STIM1 underneath the plasma membrane induces clustering of Orai1
    • Xu P., Lu J., Li Z., Yu X., Chen L., Xu T. Aggregation of STIM1 underneath the plasma membrane induces clustering of Orai1. Biochem. Biophys. Res. Commun. 2006, 350:969-976.
    • (2006) Biochem. Biophys. Res. Commun. , vol.350 , pp. 969-976
    • Xu, P.1    Lu, J.2    Li, Z.3    Yu, X.4    Chen, L.5    Xu, T.6
  • 102
    • 56649094581 scopus 로고    scopus 로고
    • STIM1-Orai1 interactions and Orai1 conformational changes revealed by live-cell FRET microscopy
    • Navarro-Borelly L., Somasundaram A., Yamashita M., Ren D., Miller R.J., Prakriya M. STIM1-Orai1 interactions and Orai1 conformational changes revealed by live-cell FRET microscopy. J. Physiol. 2008, 586:5383-5401.
    • (2008) J. Physiol. , vol.586 , pp. 5383-5401
    • Navarro-Borelly, L.1    Somasundaram, A.2    Yamashita, M.3    Ren, D.4    Miller, R.J.5    Prakriya, M.6
  • 103
    • 77950377028 scopus 로고    scopus 로고
    • Molecular basis of calcium signaling in lymphocytes: STIM and ORAI
    • Hogan P.G., Lewis R.S., Rao A. Molecular basis of calcium signaling in lymphocytes: STIM and ORAI. Annu. Rev. Immunol. 2010, 28:491-533.
    • (2010) Annu. Rev. Immunol. , vol.28 , pp. 491-533
    • Hogan, P.G.1    Lewis, R.S.2    Rao, A.3
  • 105
    • 84865591543 scopus 로고    scopus 로고
    • Regulation of lymphocyte function by ORAI and STIM proteins in infection and autoimmunity
    • Shaw P.J., Feske S. Regulation of lymphocyte function by ORAI and STIM proteins in infection and autoimmunity. J. Physiol. 2012, 590:4157-4167.
    • (2012) J. Physiol. , vol.590 , pp. 4157-4167
    • Shaw, P.J.1    Feske, S.2
  • 107
    • 84856236418 scopus 로고    scopus 로고
    • Regulation of store-operated calcium entry during cell division
    • Smyth J.T., Putney J.W. Regulation of store-operated calcium entry during cell division. Biochem. Soc. Trans. 2012, 40:119-123.
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 119-123
    • Smyth, J.T.1    Putney, J.W.2
  • 108
    • 84858315403 scopus 로고    scopus 로고
    • Endothelial dysfunction in diabetes mellitus: possible involvement of endoplasmic reticulum stress?
    • Basha B., Samuel S.M., Triggle C.R., Ding H. Endothelial dysfunction in diabetes mellitus: possible involvement of endoplasmic reticulum stress?. Exp. Diabetes Res. 2012, 481840.
    • (2012) Exp. Diabetes Res. , pp. 481840
    • Basha, B.1    Samuel, S.M.2    Triggle, C.R.3    Ding, H.4
  • 109
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D., Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 2007, 8:519-529.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 110
    • 33846548110 scopus 로고    scopus 로고
    • ER stress and diseases
    • Yoshida H. ER stress and diseases. FEBS J. 2007, 274:630-658.
    • (2007) FEBS J. , vol.274 , pp. 630-658
    • Yoshida, H.1
  • 112
    • 58949085858 scopus 로고    scopus 로고
    • Protective effect of paraoxonase-2 against endoplasmic reticulum stress-induced apoptosis is lost upon disturbance of calcium homoeostasis
    • Horke S., Witte I., Wilgenbus P., Altenhöfer S., Krüger M., Li H., et al. Protective effect of paraoxonase-2 against endoplasmic reticulum stress-induced apoptosis is lost upon disturbance of calcium homoeostasis. Biochem. J 2008, 416:395-405.
    • (2008) Biochem. J , vol.416 , pp. 395-405
    • Horke, S.1    Witte, I.2    Wilgenbus, P.3    Altenhöfer, S.4    Krüger, M.5    Li, H.6
  • 113
    • 57749177096 scopus 로고    scopus 로고
    • Endothelial dysfunction and diabetes: roles of hyperglycemia, impaired insulin signaling and obesity
    • Bakker W., Eringa E.C., Sipkema P., van Hinsbergh V.W.M. Endothelial dysfunction and diabetes: roles of hyperglycemia, impaired insulin signaling and obesity. Cell Tissue Res. 2009, 335:165-189.
    • (2009) Cell Tissue Res. , vol.335 , pp. 165-189
    • Bakker, W.1    Eringa, E.C.2    Sipkema, P.3    van Hinsbergh, V.W.M.4
  • 114
    • 34249276389 scopus 로고    scopus 로고
    • High-density lipoprotein modulates oxidized phospholipid signaling in human endothelial cells from proinflammatory to anti-inflammatory
    • Gharavi N.M., Gargalovic P.S., Chang I., Araujo J.A., Clark M.J., Szeto W.L., et al. High-density lipoprotein modulates oxidized phospholipid signaling in human endothelial cells from proinflammatory to anti-inflammatory. Arterioscler. Thromb. Vasc. Biol. 2007, 27:1346-1353.
    • (2007) Arterioscler. Thromb. Vasc. Biol. , vol.27 , pp. 1346-1353
    • Gharavi, N.M.1    Gargalovic, P.S.2    Chang, I.3    Araujo, J.A.4    Clark, M.J.5    Szeto, W.L.6
  • 115
    • 74449092406 scopus 로고    scopus 로고
    • Effects of antioxidants on glucose-induced oxidative stress and endoplasmic reticulum stress in endothelial cells
    • Sheikh-Ali M., Sultan S., Alamir A.-R., Haas M.J., Mooradian A.D. Effects of antioxidants on glucose-induced oxidative stress and endoplasmic reticulum stress in endothelial cells. Diabetes Res. Clin. Pract. 2010, 87:161-166.
    • (2010) Diabetes Res. Clin. Pract. , vol.87 , pp. 161-166
    • Sheikh-Ali, M.1    Sultan, S.2    Alamir, A.-R.3    Haas, M.J.4    Mooradian, A.D.5
  • 116
    • 77953223063 scopus 로고    scopus 로고
    • The endothelial cell receptor GRP78 is required for mucormycosis pathogenesis in diabetic mice
    • Liu M., Spellberg B., Phan Q.T., Fu Y., Fu Y., Lee A.S., et al. The endothelial cell receptor GRP78 is required for mucormycosis pathogenesis in diabetic mice. J. Clin. Invest. 2010, 120:1914-1924.
    • (2010) J. Clin. Invest. , vol.120 , pp. 1914-1924
    • Liu, M.1    Spellberg, B.2    Phan, Q.T.3    Fu, Y.4    Fu, Y.5    Lee, A.S.6
  • 117
    • 84866135183 scopus 로고    scopus 로고
    • Activating transcription factor 4 mediates hyperglycaemia-induced endothelial inflammation and retinal vascular leakage through activation of STAT3 in a mouse model of type 1 diabetes
    • Chen Y., Wang J.J., Li J., Hosoya K.I., Ratan R., Townes T., et al. Activating transcription factor 4 mediates hyperglycaemia-induced endothelial inflammation and retinal vascular leakage through activation of STAT3 in a mouse model of type 1 diabetes. Diabetologia 2012, 55:2533-2545.
    • (2012) Diabetologia , vol.55 , pp. 2533-2545
    • Chen, Y.1    Wang, J.J.2    Li, J.3    Hosoya, K.I.4    Ratan, R.5    Townes, T.6
  • 118
    • 57749210168 scopus 로고    scopus 로고
    • Salvianolic acid B protects human endothelial cells from oxidative stress damage: a possible protective role of glucose-regulated protein 78 induction
    • Wu H.-L., Li Y.-H., Lin Y.-H., Wang R., Li Y.-B., Tie L., et al. Salvianolic acid B protects human endothelial cells from oxidative stress damage: a possible protective role of glucose-regulated protein 78 induction. Cardiovasc. Res. 2009, 81:148-158.
    • (2009) Cardiovasc. Res. , vol.81 , pp. 148-158
    • Wu, H.-L.1    Li, Y.-H.2    Lin, Y.-H.3    Wang, R.4    Li, Y.-B.5    Tie, L.6
  • 119
    • 79960247207 scopus 로고    scopus 로고
    • Calcium homoeostasis modulator 1 (CALHM1) reduces the calcium content of the endoplasmic reticulum (ER) and triggers ER stress
    • Gallego-Sandín S., Alonso M.T., García-Sancho J. Calcium homoeostasis modulator 1 (CALHM1) reduces the calcium content of the endoplasmic reticulum (ER) and triggers ER stress. Biochem. J 2011, 437:469-475.
    • (2011) Biochem. J , vol.437 , pp. 469-475
    • Gallego-Sandín, S.1    Alonso, M.T.2    García-Sancho, J.3
  • 120
    • 68749095178 scopus 로고    scopus 로고
    • Amiloride derivatives induce apoptosis by depleting ER Ca(2+) stores in vascular endothelial cells
    • Park K.S., Poburko D., Wollheim C.B., Demaurex N. Amiloride derivatives induce apoptosis by depleting ER Ca(2+) stores in vascular endothelial cells. Br. J. Pharmacol. 2009, 156:1296-1304.
    • (2009) Br. J. Pharmacol. , vol.156 , pp. 1296-1304
    • Park, K.S.1    Poburko, D.2    Wollheim, C.B.3    Demaurex, N.4
  • 122
    • 35848970993 scopus 로고    scopus 로고
    • Oxidation and inactivation of SERCA by selective reaction of cysteine residues with amino acid peroxides
    • Dremina E.S., Sharov V.S., Davies M.J., Schöneich C. Oxidation and inactivation of SERCA by selective reaction of cysteine residues with amino acid peroxides. Chem. Res. Toxicol. 2007, 20:1462-1469.
    • (2007) Chem. Res. Toxicol. , vol.20 , pp. 1462-1469
    • Dremina, E.S.1    Sharov, V.S.2    Davies, M.J.3    Schöneich, C.4
  • 123
    • 33749522859 scopus 로고    scopus 로고
    • Mass spectrometry of protein modifications by reactive oxygen and nitrogen species
    • Schöneich C., Sharov V.S. Mass spectrometry of protein modifications by reactive oxygen and nitrogen species. Free Radic. Biol. Med. 2006, 41:1507-1520.
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 1507-1520
    • Schöneich, C.1    Sharov, V.S.2
  • 124
    • 77949666180 scopus 로고    scopus 로고
    • Targeting the redox regulation of SERCA in vascular physiology and disease
    • Tong X., Evangelista A., Cohen R.A. Targeting the redox regulation of SERCA in vascular physiology and disease. Curr. Opin. Pharmacol. 2010, 10:133-138.
    • (2010) Curr. Opin. Pharmacol. , vol.10 , pp. 133-138
    • Tong, X.1    Evangelista, A.2    Cohen, R.A.3
  • 125
    • 9144266981 scopus 로고    scopus 로고
    • S-glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide
    • Adachi T., Weisbrod R.M., Pimentel D.R., Ying J., Sharov V.S., Schöneich C., et al. S-glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide. Nat. Med. 2004, 10:1200-1207.
    • (2004) Nat. Med. , vol.10 , pp. 1200-1207
    • Adachi, T.1    Weisbrod, R.M.2    Pimentel, D.R.3    Ying, J.4    Sharov, V.S.5    Schöneich, C.6
  • 126
    • 34247212953 scopus 로고    scopus 로고
    • Cysteine-674 of the sarco/endoplasmic reticulum calcium ATPase is required for the inhibition of cell migration by nitric oxide
    • Ying J., Tong X., Pimentel D.R., Weisbrod R.M., Trucillo M.P., Adachi T., et al. Cysteine-674 of the sarco/endoplasmic reticulum calcium ATPase is required for the inhibition of cell migration by nitric oxide. Arterioscler. Thromb. Vasc. Biol. 2007, 27:783-790.
    • (2007) Arterioscler. Thromb. Vasc. Biol. , vol.27 , pp. 783-790
    • Ying, J.1    Tong, X.2    Pimentel, D.R.3    Weisbrod, R.M.4    Trucillo, M.P.5    Adachi, T.6
  • 127
    • 77957331055 scopus 로고    scopus 로고
    • Modulation of vascular sarco/endoplasmic reticulum calcium ATPase in cardiovascular pathophysiology
    • Adachi T. Modulation of vascular sarco/endoplasmic reticulum calcium ATPase in cardiovascular pathophysiology. Adv. Pharmacol. 2010, 59:165-195.
    • (2010) Adv. Pharmacol. , vol.59 , pp. 165-195
    • Adachi, T.1
  • 128
    • 54949115096 scopus 로고    scopus 로고
    • Cysteine-674 oxidation and degradation of sarcoplasmic reticulum Ca(2+) ATPase in diabetic pig aorta
    • Ying J., Sharov V., Xu S., Jiang B., Gerrity R., Schöneich C., et al. Cysteine-674 oxidation and degradation of sarcoplasmic reticulum Ca(2+) ATPase in diabetic pig aorta. Free Radic. Biol. Med. 2008, 45:756-762.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 756-762
    • Ying, J.1    Sharov, V.2    Xu, S.3    Jiang, B.4    Gerrity, R.5    Schöneich, C.6
  • 129
    • 78650615554 scopus 로고    scopus 로고
    • 2+-ATPase 2b is a major regulator of endoplasmic reticulum stress and glucose homeostasis in obesity
    • 2+-ATPase 2b is a major regulator of endoplasmic reticulum stress and glucose homeostasis in obesity. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:19320-19325.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 19320-19325
    • Park, S.W.1    Zhou, Y.2    Lee, J.3    Lee, J.4    Ozcan, U.5
  • 130
    • 84899591166 scopus 로고    scopus 로고
    • Hepatic extracellular signal-regulated kinase 2 suppresses endoplasmic reticulum stress and protects from oxidative stress and endothelial dysfunction
    • Kujiraoka T., Satoh Y., Ayaori M., Shiraishi Y., Arai-Nakaya Y., Hakuno D., et al. Hepatic extracellular signal-regulated kinase 2 suppresses endoplasmic reticulum stress and protects from oxidative stress and endothelial dysfunction. J. Am. Heart Assoc. 2013, 2:e000361.
    • (2013) J. Am. Heart Assoc. , vol.2 , pp. e000361
    • Kujiraoka, T.1    Satoh, Y.2    Ayaori, M.3    Shiraishi, Y.4    Arai-Nakaya, Y.5    Hakuno, D.6
  • 131
    • 84875982580 scopus 로고    scopus 로고
    • Protein tyrosine nitration and thiol oxidation by peroxynitrite-strategies to prevent these oxidative modifications
    • Daiber A., Daub S., Bachschmid M., Schildknecht S., Oelze M., Steven S., et al. Protein tyrosine nitration and thiol oxidation by peroxynitrite-strategies to prevent these oxidative modifications. Int. J. Mol. Sci. 2013, 14:7542-7570.
    • (2013) Int. J. Mol. Sci. , vol.14 , pp. 7542-7570
    • Daiber, A.1    Daub, S.2    Bachschmid, M.3    Schildknecht, S.4    Oelze, M.5    Steven, S.6
  • 132
    • 0034925593 scopus 로고    scopus 로고
    • Tyrosine nitration: localisation, quantification, consequences for protein function and signal transduction
    • Greenacre S.A., Ischiropoulos H. Tyrosine nitration: localisation, quantification, consequences for protein function and signal transduction. Free Radic. Res. 2001, 34:541-581.
    • (2001) Free Radic. Res. , vol.34 , pp. 541-581
    • Greenacre, S.A.1    Ischiropoulos, H.2
  • 133
    • 62149135339 scopus 로고    scopus 로고
    • Nitrotyrosine-modified SERCA2: a cellular sensor of reactive nitrogen species
    • Bigelow D.J. Nitrotyrosine-modified SERCA2: a cellular sensor of reactive nitrogen species. Pflugers Arch. 2009, 457:701-710.
    • (2009) Pflugers Arch. , vol.457 , pp. 701-710
    • Bigelow, D.J.1
  • 134
    • 25444450030 scopus 로고    scopus 로고
    • 3-Nitrotyrosine modification of SERCA2a in the aging heart: a distinct signature of the cellular redox environment
    • Knyushko T.V., Sharov V.S., Williams T.D., Schöneich C., Bigelow D.J. 3-Nitrotyrosine modification of SERCA2a in the aging heart: a distinct signature of the cellular redox environment. Biochemistry 2005, 44:13071-13081.
    • (2005) Biochemistry , vol.44 , pp. 13071-13081
    • Knyushko, T.V.1    Sharov, V.S.2    Williams, T.D.3    Schöneich, C.4    Bigelow, D.J.5
  • 135
    • 33744937888 scopus 로고    scopus 로고
    • Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging
    • 02118
    • Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., et al. Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging. Am. J. Physiol. Heart Circ. Physiol. 2006, 02118:2220-2227.
    • (2006) Am. J. Physiol. Heart Circ. Physiol. , pp. 2220-2227
    • Xu, S.1    Ying, J.2    Jiang, B.3    Guo, W.4    Adachi, T.5    Sharov, V.6
  • 138
    • 12944326874 scopus 로고    scopus 로고
    • Chronic exposure to high glucose impairs bradykinin-stimulated nitric oxide production by interfering with the phospholipase-C-implicated signalling pathway in endothelial cells: evidence for the involvement of protein kinase C
    • Tang Y., Li G.D. Chronic exposure to high glucose impairs bradykinin-stimulated nitric oxide production by interfering with the phospholipase-C-implicated signalling pathway in endothelial cells: evidence for the involvement of protein kinase C. Diabetologia 2004, 47:2093-2104.
    • (2004) Diabetologia , vol.47 , pp. 2093-2104
    • Tang, Y.1    Li, G.D.2
  • 139
    • 84878524199 scopus 로고    scopus 로고
    • Role of impaired endothelial cell Ca(2+) signaling in uteroplacental vascular dysfunction during diabetic rat pregnancy
    • Gokina N.I., Bonev A.D., Gokin A.P., Goloman G. Role of impaired endothelial cell Ca(2+) signaling in uteroplacental vascular dysfunction during diabetic rat pregnancy. Am. J. Physiol. Heart Circ. Physiol. 2013, 304:H935-H945.
    • (2013) Am. J. Physiol. Heart Circ. Physiol. , vol.304 , pp. H935-H945
    • Gokina, N.I.1    Bonev, A.D.2    Gokin, A.P.3    Goloman, G.4
  • 140
    • 33646426382 scopus 로고    scopus 로고
    • 2+ signaling contributes to pregnancy-enhanced vasodilation of rat uteroplacental arteries
    • 2+ signaling contributes to pregnancy-enhanced vasodilation of rat uteroplacental arteries. Am. J. Physiol. Heart Circ. Physiol. 2006, 290:2124-2135.
    • (2006) Am. J. Physiol. Heart Circ. Physiol. , vol.290 , pp. 2124-2135
    • Gokina, N.I.1    Goecks, T.2
  • 141
    • 85047691537 scopus 로고    scopus 로고
    • Inhibition of GAPDH activity by poly (ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells
    • Du X., Matsumura T., Edelstein D., Rossetti L., Zsengellér Z., Szabó C., et al. Inhibition of GAPDH activity by poly (ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells. J. Clin. Invest. 2003, 112:1049-1057.
    • (2003) J. Clin. Invest. , vol.112 , pp. 1049-1057
    • Du, X.1    Matsumura, T.2    Edelstein, D.3    Rossetti, L.4    Zsengellér, Z.5    Szabó, C.6
  • 143
    • 84861062943 scopus 로고    scopus 로고
    • Biochemistry, physiology, and pathophysiology of NADPH oxidases in the cardiovascular system
    • Lassègue B., San Martín A., Griendling K.K. Biochemistry, physiology, and pathophysiology of NADPH oxidases in the cardiovascular system. Circ. Res. 2012, 110:1364-1390.
    • (2012) Circ. Res. , vol.110 , pp. 1364-1390
    • Lassègue, B.1    San Martín, A.2    Griendling, K.K.3
  • 144
    • 84904321037 scopus 로고    scopus 로고
    • Mitochondria, endothelial cell function, and vascular diseases
    • Tang X., Luo Y.-X., Chen H.-Z., Liu D.-P. Mitochondria, endothelial cell function, and vascular diseases. Front. Physiol. 2014, 5:175.
    • (2014) Front. Physiol. , vol.5 , pp. 175
    • Tang, X.1    Luo, Y.-X.2    Chen, H.-Z.3    Liu, D.-P.4
  • 145
    • 25444525139 scopus 로고    scopus 로고
    • Selective role for superoxide in InsP3 receptor-mediated mitochondrial dysfunction and endothelial apoptosis
    • Madesh M., Hawkins B.J., Milovanova T., Bhanumathy C.D., Joseph S.K., Ramachandrarao S.P., et al. Selective role for superoxide in InsP3 receptor-mediated mitochondrial dysfunction and endothelial apoptosis. J. Cell Biol. 2005, 170:1079-1090.
    • (2005) J. Cell Biol. , vol.170 , pp. 1079-1090
    • Madesh, M.1    Hawkins, B.J.2    Milovanova, T.3    Bhanumathy, C.D.4    Joseph, S.K.5    Ramachandrarao, S.P.6
  • 146
    • 83655172387 scopus 로고    scopus 로고
    • The link between metabolic abnormalities and endothelial dysfunction in type 2 diabetes: an update
    • Zhang H., Dellsperger K.C., Zhang C. The link between metabolic abnormalities and endothelial dysfunction in type 2 diabetes: an update. Basic Res. Cardiol. 2012, 107:237.
    • (2012) Basic Res. Cardiol. , vol.107 , pp. 237
    • Zhang, H.1    Dellsperger, K.C.2    Zhang, C.3
  • 147
    • 39149126992 scopus 로고    scopus 로고
    • High glucose oxidizes SERCA cysteine-674 and prevents inhibition by nitric oxide of smooth muscle cell migration
    • Tong X., Ying J., Pimentel D.R., Trucillo M., Adachi T., Cohen R.A. High glucose oxidizes SERCA cysteine-674 and prevents inhibition by nitric oxide of smooth muscle cell migration. J. Mol. Cell. Cardiol. 2008, 44:361-369.
    • (2008) J. Mol. Cell. Cardiol. , vol.44 , pp. 361-369
    • Tong, X.1    Ying, J.2    Pimentel, D.R.3    Trucillo, M.4    Adachi, T.5    Cohen, R.A.6
  • 148
    • 0030721991 scopus 로고    scopus 로고
    • 2+ pump in endothelium: implications to coronary artery function
    • 2+ pump in endothelium: implications to coronary artery function. Am. Physiol. Soc. 1997, 1250-1258.
    • (1997) Am. Physiol. Soc. , pp. 1250-1258
    • Grover, A.K.1    Samson, S.E.2
  • 150
    • 33644749330 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase reduces hyperglycemia-induced mitochondrial reactive oxygen species production and promotes mitochondrial biogenesis in human umbilical vein endothelial cells
    • Kukidome D., Nishikawa T., Sonoda K., Imoto K., Fujisawa K., Yano M., et al. Activation of AMP-activated protein kinase reduces hyperglycemia-induced mitochondrial reactive oxygen species production and promotes mitochondrial biogenesis in human umbilical vein endothelial cells. Diabetes 2006, 55:120-127.
    • (2006) Diabetes , vol.55 , pp. 120-127
    • Kukidome, D.1    Nishikawa, T.2    Sonoda, K.3    Imoto, K.4    Fujisawa, K.5    Yano, M.6
  • 151
    • 84872241559 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species enhance AMP-activated protein kinase activation in the endothelium of patients with coronary artery disease and diabetes
    • Mackenzie R.M., Salt I.P., Miller W.H., Logan A., Ibrahim H.A., Degasperi A., et al. Mitochondrial reactive oxygen species enhance AMP-activated protein kinase activation in the endothelium of patients with coronary artery disease and diabetes. Clin. Sci. (Lond). 2013, 124:403-411.
    • (2013) Clin. Sci. (Lond). , vol.124 , pp. 403-411
    • Mackenzie, R.M.1    Salt, I.P.2    Miller, W.H.3    Logan, A.4    Ibrahim, H.A.5    Degasperi, A.6
  • 152
    • 84861609778 scopus 로고    scopus 로고
    • Hyperglycemia and oxidative stress in cultured endothelial cells - a comparison of primary endothelial cells with an immortalized endothelial cell line
    • Karbach S., Jansen T., Horke S., Heeren T., Scholz A., Coldewey M., et al. Hyperglycemia and oxidative stress in cultured endothelial cells - a comparison of primary endothelial cells with an immortalized endothelial cell line. J. Diabetes Complications 2012, 26:155-162.
    • (2012) J. Diabetes Complications , vol.26 , pp. 155-162
    • Karbach, S.1    Jansen, T.2    Horke, S.3    Heeren, T.4    Scholz, A.5    Coldewey, M.6
  • 153
    • 4444236143 scopus 로고    scopus 로고
    • Peroxynitrite and vascular endothelial dysfunction in diabetes mellitus
    • Zou M.-H., Cohen R., Ullrich V. Peroxynitrite and vascular endothelial dysfunction in diabetes mellitus. Endothelium 2004, 11:89-97.
    • (2004) Endothelium , vol.11 , pp. 89-97
    • Zou, M.-H.1    Cohen, R.2    Ullrich, V.3
  • 154
    • 34547691067 scopus 로고    scopus 로고
    • Role of vascular reactive oxygen species in development of vascular abnormalities in diabetes
    • Son S.M. Role of vascular reactive oxygen species in development of vascular abnormalities in diabetes. Diabetes Res. Clin. Pract. 2007, 77(Suppl 1):S65-S70.
    • (2007) Diabetes Res. Clin. Pract. , vol.77 , pp. S65-S70
    • Son, S.M.1
  • 155
    • 41749108854 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in disease pathogenesis
    • Lin J., Walter P., Yen B. Endoplasmic reticulum stress in disease pathogenesis. Annu. Rev. Pathol. 2013, 3:399-425.
    • (2013) Annu. Rev. Pathol. , vol.3 , pp. 399-425
    • Lin, J.1    Walter, P.2    Yen, B.3
  • 156
    • 57049117856 scopus 로고    scopus 로고
    • Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities
    • Kim I., Xu W., Reed J.C. Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities. Nat. Rev. Drug Discov. 2008, 7:1013-1030.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 1013-1030
    • Kim, I.1    Xu, W.2    Reed, J.C.3
  • 157
    • 39149104320 scopus 로고    scopus 로고
    • The role for endoplasmic reticulum stress in diabetes mellitus
    • Eizirik D.L., Cardozo A.K., Cnop M. The role for endoplasmic reticulum stress in diabetes mellitus. Endocr. Rev. 2008, 29:42-61.
    • (2008) Endocr. Rev. , vol.29 , pp. 42-61
    • Eizirik, D.L.1    Cardozo, A.K.2    Cnop, M.3
  • 159
    • 45449087963 scopus 로고    scopus 로고
    • Apoptosis induced by endoplasmic reticulum stress involved in diabetic kidney disease
    • Liu G., Sun Y., Li Z., Song T., Wang H., Zhang Y., et al. Apoptosis induced by endoplasmic reticulum stress involved in diabetic kidney disease. Biochem. Biophys. Res. Commun. 2008, 370:651-656.
    • (2008) Biochem. Biophys. Res. Commun. , vol.370 , pp. 651-656
    • Liu, G.1    Sun, Y.2    Li, Z.3    Song, T.4    Wang, H.5    Zhang, Y.6
  • 160
    • 67349269219 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is implicated in retinal inflammation and diabetic retinopathy
    • Li J., Wang J.J., Yu Q., Wang M., Zhang S.X. Endoplasmic reticulum stress is implicated in retinal inflammation and diabetic retinopathy. FEBS Lett. 2009, 583:1521-1527.
    • (2009) FEBS Lett. , vol.583 , pp. 1521-1527
    • Li, J.1    Wang, J.J.2    Yu, Q.3    Wang, M.4    Zhang, S.X.5
  • 161
    • 84874438608 scopus 로고    scopus 로고
    • Role of endoplasmic reticulum stress in diabetic neuropathy
    • Cameron N.E. Role of endoplasmic reticulum stress in diabetic neuropathy. Diabetes 2013, 62:696-697.
    • (2013) Diabetes , vol.62 , pp. 696-697
    • Cameron, N.E.1
  • 162
    • 33748069813 scopus 로고    scopus 로고
    • Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes
    • Ozcan U., Yilmaz E., Ozcan L., Furuhashi M., Vaillancourt E., Smith R.O., et al. Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes. Science 2006, 313:1137-1140.
    • (2006) Science , vol.313 , pp. 1137-1140
    • Ozcan, U.1    Yilmaz, E.2    Ozcan, L.3    Furuhashi, M.4    Vaillancourt, E.5    Smith, R.O.6
  • 164
    • 33644790277 scopus 로고    scopus 로고
    • Peroxynitrite causes endoplasmic reticulum stress and apoptosis in human vascular endothelium: implications in atherogenesis
    • Dickhout J.G., Hossain G.S., Pozza L.M., Zhou J., Lhoták S., Austin R.C. Peroxynitrite causes endoplasmic reticulum stress and apoptosis in human vascular endothelium: implications in atherogenesis. Arterioscler. Thromb. Vasc. Biol. 2005, 25:2623-2629.
    • (2005) Arterioscler. Thromb. Vasc. Biol. , vol.25 , pp. 2623-2629
    • Dickhout, J.G.1    Hossain, G.S.2    Pozza, L.M.3    Zhou, J.4    Lhoták, S.5    Austin, R.C.6
  • 165
    • 77958003056 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum stress in the progression of atherosclerosis
    • Tabas I. The role of endoplasmic reticulum stress in the progression of atherosclerosis. Circ. Res. 2010, 107:839-850.
    • (2010) Circ. Res. , vol.107 , pp. 839-850
    • Tabas, I.1
  • 166
    • 84895801260 scopus 로고    scopus 로고
    • Vascular effects of advanced glycation endproducts: clinical effects and molecular mechanisms
    • Stirban A., Gawlowski T., Roden M. Vascular effects of advanced glycation endproducts: clinical effects and molecular mechanisms. Mol. Metab. 2014, 3:94-108.
    • (2014) Mol. Metab. , vol.3 , pp. 94-108
    • Stirban, A.1    Gawlowski, T.2    Roden, M.3
  • 167
    • 0035116150 scopus 로고    scopus 로고
    • Diabetes and endothelial dysfunction: a clinical perspective
    • Calles-Escandon J., Cipolla M. Diabetes and endothelial dysfunction: a clinical perspective. Endocr. Rev. 2001, 22:36-52.
    • (2001) Endocr. Rev. , vol.22 , pp. 36-52
    • Calles-Escandon, J.1    Cipolla, M.2
  • 168
    • 84872158502 scopus 로고    scopus 로고
    • Vascular complications of diabetes: mechanisms of injury and protective factors
    • Rask-Madsen C., King G.L. Vascular complications of diabetes: mechanisms of injury and protective factors. Cell Metab. 2013, 17:20-33.
    • (2013) Cell Metab. , vol.17 , pp. 20-33
    • Rask-Madsen, C.1    King, G.L.2
  • 169
    • 33749532327 scopus 로고    scopus 로고
    • Albumin induces endoplasmic reticulum stress and apoptosis in renal proximal tubular cells
    • Ohse T., Inagi R., Tanaka T., Ota T., Miyata T., Kojima I., et al. Albumin induces endoplasmic reticulum stress and apoptosis in renal proximal tubular cells. Kidney Int. 2006, 70:1447-1455.
    • (2006) Kidney Int. , vol.70 , pp. 1447-1455
    • Ohse, T.1    Inagi, R.2    Tanaka, T.3    Ota, T.4    Miyata, T.5    Kojima, I.6
  • 170
    • 79954996508 scopus 로고    scopus 로고
    • Attenuation of diabetic nephropathy in diabetes rats induced by streptozotocin by regulating the endoplasmic reticulum stress inflammatory response
    • Qi W., Mu J., Luo Z.-F., Zeng W., Guo Y.-H., Pang Q., et al. Attenuation of diabetic nephropathy in diabetes rats induced by streptozotocin by regulating the endoplasmic reticulum stress inflammatory response. Metabolism. 2011, 60:594-603.
    • (2011) Metabolism. , vol.60 , pp. 594-603
    • Qi, W.1    Mu, J.2    Luo, Z.-F.3    Zeng, W.4    Guo, Y.-H.5    Pang, Q.6
  • 171
    • 79960242803 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum stress in the early stage of diabetic retinopathy
    • Li B., Wang H.S., Li G.G., Zhao M.J., Zhao M.H. The role of endoplasmic reticulum stress in the early stage of diabetic retinopathy. Acta Diabetol. 2011, 48:103-111.
    • (2011) Acta Diabetol. , vol.48 , pp. 103-111
    • Li, B.1    Wang, H.S.2    Li, G.G.3    Zhao, M.J.4    Zhao, M.H.5
  • 172
    • 84897417301 scopus 로고    scopus 로고
    • Glucocorticoids: structure, signaling and molecular mechanisms in the treatment of diabetic retinopathy and diabetic macular edema
    • Zhang X., Wang N., Schachat aP., Bao S., Gillies M.C. Glucocorticoids: structure, signaling and molecular mechanisms in the treatment of diabetic retinopathy and diabetic macular edema. Curr. Mol. Med. 2014, 14:376-384.
    • (2014) Curr. Mol. Med. , vol.14 , pp. 376-384
    • Zhang, X.1    Wang, N.2    Schachat, A.3    Bao, S.4    Gillies, M.C.5
  • 173
    • 84875475183 scopus 로고    scopus 로고
    • Mild endoplasmic reticulum stress promotes retinal neovascularization via induction of BiP/GRP78
    • Nakamura S., Takizawa H., Shimazawa M., Hashimoto Y., Sugitani S., Tsuruma K., et al. Mild endoplasmic reticulum stress promotes retinal neovascularization via induction of BiP/GRP78. PLOS ONE 2013, 8:e60517.
    • (2013) PLOS ONE , vol.8 , pp. e60517
    • Nakamura, S.1    Takizawa, H.2    Shimazawa, M.3    Hashimoto, Y.4    Sugitani, S.5    Tsuruma, K.6
  • 175
  • 176
    • 84874415720 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress plays a key role in the pathogenesis of diabetic peripheral neuropathy
    • Lupachyk S., Watcho P., Stavniichuk R., Shevalye H., Obrosova I.G. Endoplasmic reticulum stress plays a key role in the pathogenesis of diabetic peripheral neuropathy. Diabetes 2013, 62:944-952.
    • (2013) Diabetes , vol.62 , pp. 944-952
    • Lupachyk, S.1    Watcho, P.2    Stavniichuk, R.3    Shevalye, H.4    Obrosova, I.G.5
  • 177
    • 50249172431 scopus 로고    scopus 로고
    • STIM1 converts TRPC1 from a receptor-operated to a store-operated channel: moving TRPC1 in and out of lipid rafts
    • Alicia S., Angélica Z., Carlos S., Alfonso S., Vaca L. STIM1 converts TRPC1 from a receptor-operated to a store-operated channel: moving TRPC1 in and out of lipid rafts. Cell Calcium 2008, 44:479-491.
    • (2008) Cell Calcium , vol.44 , pp. 479-491
    • Alicia, S.1    Angélica, Z.2    Carlos, S.3    Alfonso, S.4    Vaca, L.5
  • 178
    • 45149098247 scopus 로고    scopus 로고
    • Functional requirement for Orai1 in store-operated TRPC1-STIM1 channels
    • Cheng K.T., Liu X., Ong H.L., Ambudkar I.S. Functional requirement for Orai1 in store-operated TRPC1-STIM1 channels. J. Biol. Chem. 2008, 283:12935-12940.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12935-12940
    • Cheng, K.T.1    Liu, X.2    Ong, H.L.3    Ambudkar, I.S.4
  • 179
    • 84889814777 scopus 로고    scopus 로고
    • Role of endoplasmic reticulum stress in the loss of retinal ganglion cells in diabetic retinopathy
    • Yang L., Wu L., Wang D., Li Y., Dou H., Tso M.O.M. Role of endoplasmic reticulum stress in the loss of retinal ganglion cells in diabetic retinopathy. Neural Regen. Res. 2013, 8.
    • (2013) Neural Regen. Res. , vol.8
    • Yang, L.1    Wu, L.2    Wang, D.3    Li, Y.4    Dou, H.5    Tso, M.O.M.6
  • 180
    • 84912144132 scopus 로고    scopus 로고
    • Registration number CECA-D-14-00074
    • Zarain et al., Regulation of SERCA pumps expression in diabetes. (2014) Registration number CECA-D-14-00074.
    • (2014)
    • Zarain1
  • 182
    • 84912127169 scopus 로고    scopus 로고
    • Calcium signaling in pancreatic b-cells in health and in type 2 diabetes
    • Gilon P., Chae H.-Y., Rutter G.A., Ravier M.A. Calcium signaling in pancreatic b-cells in health and in type 2 diabetes. Cell Calcium 2014, 10.1016/j.ceca.2014.09.001.
    • (2014) Cell Calcium
    • Gilon, P.1    Chae, H.-Y.2    Rutter, G.A.3    Ravier, M.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.