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Volumn 176, Issue 2-3, 2008, Pages 196-203

La3+ binds to BiP/GRP78 and induces unfolded protein response in HepG2 cells

Author keywords

BiP GRP78; Endoplasmic reticulum; Lanthanum; Unfolded protein response

Indexed keywords

GLUCOSE REGULATED PROTEIN 78; LANTHANUM; PROTEIN IRE1; REACTIVE OXYGEN METABOLITE; X BOX BINDING PROTEIN 1; CALCIUM; CHAPERONE; DNA BINDING PROTEIN; HEAT SHOCK PROTEIN; IRE1ALPHA PROTEIN, HUMAN; LANTHANIDE; MESSENGER RNA; MOLECULAR CHAPERONE GRP78; PROTEIN SERINE THREONINE KINASE; REGULATORY FACTOR X TRANSCRIPTION FACTORS; RIBONUCLEASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 55249083008     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2008.07.014     Document Type: Article
Times cited : (9)

References (46)
  • 1
    • 33645996396 scopus 로고    scopus 로고
    • Protein folding in the endoplasmic reticulum and the unfolded protein response
    • Zhang K., and Kaufman R.J. Protein folding in the endoplasmic reticulum and the unfolded protein response. Handb. Exp. Pharmacol. (2006) 69-91
    • (2006) Handb. Exp. Pharmacol. , pp. 69-91
    • Zhang, K.1    Kaufman, R.J.2
  • 2
    • 0035133393 scopus 로고    scopus 로고
    • ER calcium and the functions of intracellular organelles
    • Ashby M.C., and Tepikin A.V. ER calcium and the functions of intracellular organelles. Semin. Cell Dev. Biol. 12 (2001) 11-17
    • (2001) Semin. Cell Dev. Biol. , vol.12 , pp. 11-17
    • Ashby, M.C.1    Tepikin, A.V.2
  • 4
    • 34447558236 scopus 로고    scopus 로고
    • ER chaperones in mammalian development and human diseases
    • Ni M., and Lee A.S. ER chaperones in mammalian development and human diseases. FEBS Lett. 581 (2007) 3641-3651
    • (2007) FEBS Lett. , vol.581 , pp. 3641-3651
    • Ni, M.1    Lee, A.S.2
  • 7
    • 0038080911 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation
    • Reddy R.K., Mao C., Baumeister P., Austin R.C., Kaufman R.J., and Lee A.S. Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation. J. Biol. Chem. 278 (2003) 20915-20924
    • (2003) J. Biol. Chem. , vol.278 , pp. 20915-20924
    • Reddy, R.K.1    Mao, C.2    Baumeister, P.3    Austin, R.C.4    Kaufman, R.J.5    Lee, A.S.6
  • 9
  • 10
    • 0041687863 scopus 로고    scopus 로고
    • Rare earth elements-a new generation of growth promoters for pigs?
    • He M., and Rambeck W. Rare earth elements-a new generation of growth promoters for pigs?. Arch. Tierernahr. 53 (2000) 323-334
    • (2000) Arch. Tierernahr. , vol.53 , pp. 323-334
    • He, M.1    Rambeck, W.2
  • 12
    • 0031977945 scopus 로고    scopus 로고
    • Surface charge and lanthanum block of calcium current in bullfrog sympathetic neurons
    • Block B.M., Stacey W.C., and Jones S.W. Surface charge and lanthanum block of calcium current in bullfrog sympathetic neurons. Biophys. J. 74 (1998) 2278-2284
    • (1998) Biophys. J. , vol.74 , pp. 2278-2284
    • Block, B.M.1    Stacey, W.C.2    Jones, S.W.3
  • 13
    • 3242703940 scopus 로고    scopus 로고
    • Reducing high phosphate levels in patients with chronic renal failure undergoing dialysis: a 4-week, dose-finding, open-label study with lanthanum carbonate
    • Hutchison A.J., Speake M., and Al-Baaj F. Reducing high phosphate levels in patients with chronic renal failure undergoing dialysis: a 4-week, dose-finding, open-label study with lanthanum carbonate. Nephrol. Dial. Transplant 19 (2004) 1902-1906
    • (2004) Nephrol. Dial. Transplant , vol.19 , pp. 1902-1906
    • Hutchison, A.J.1    Speake, M.2    Al-Baaj, F.3
  • 14
    • 20844444775 scopus 로고    scopus 로고
    • Chronic renal failure is associated with increased tissue deposition of lanthanum after 28-day oral administration
    • Lacour B., Lucas A., Auchere D., Ruellan N., de Serre Patey N.M., and Drueke T.B. Chronic renal failure is associated with increased tissue deposition of lanthanum after 28-day oral administration. Kidney Int. 67 (2005) 1062-1069
    • (2005) Kidney Int. , vol.67 , pp. 1062-1069
    • Lacour, B.1    Lucas, A.2    Auchere, D.3    Ruellan, N.4    de Serre Patey, N.M.5    Drueke, T.B.6
  • 16
    • 33748857226 scopus 로고    scopus 로고
    • 3+-induced extracellular signal-regulated kinase (ERK) signaling via a metal-sensing mechanism linking proliferation and apoptosis in NIH 3T3 cells
    • 3+-induced extracellular signal-regulated kinase (ERK) signaling via a metal-sensing mechanism linking proliferation and apoptosis in NIH 3T3 cells. Biochemistry 45 (2006) 11217-11225
    • (2006) Biochemistry , vol.45 , pp. 11217-11225
    • Yu, S.1    Hu, J.2    Yang, X.3    Wang, K.4    Qian, Z.M.5
  • 17
    • 0042208330 scopus 로고    scopus 로고
    • 3+ induced changes in mitochondrial structure, membrane permeability, cytochrome c release and intracellular ROS level.
    • 3+ induced changes in mitochondrial structure, membrane permeability, cytochrome c release and intracellular ROS level. Chemico-Biol. Interact. 146 (2003) 27-37
    • (2003) Chemico-Biol. Interact. , vol.146 , pp. 27-37
    • Liu, H.1    Yuan, L.2    Yang, X.3    Wang, K.4
  • 18
    • 0028077551 scopus 로고
    • Lanthanum can be transported by the sodium-calcium exchange pathway and directly triggers catecholamine release from bovine chromaffin cells
    • Powis D.A., Clark C.L., and O'Brien K.J. Lanthanum can be transported by the sodium-calcium exchange pathway and directly triggers catecholamine release from bovine chromaffin cells. Cell Calcium 16 (1994) 377-390
    • (1994) Cell Calcium , vol.16 , pp. 377-390
    • Powis, D.A.1    Clark, C.L.2    O'Brien, K.J.3
  • 19
    • 0025317506 scopus 로고
    • Blockade of current through single calcium channels by trivalent lanthanide cations. Effect of ionic radius on the rates of ion entry and exit
    • Lansman J.B. Blockade of current through single calcium channels by trivalent lanthanide cations. Effect of ionic radius on the rates of ion entry and exit. J. Gen. Physiol. 95 (1990) 679-696
    • (1990) J. Gen. Physiol. , vol.95 , pp. 679-696
    • Lansman, J.B.1
  • 20
    • 0026710313 scopus 로고
    • Lanthanum influx into cultured human keratinocytes: effect on calcium flux and terminal differentiation
    • Pillai S., and Bikle D.D. Lanthanum influx into cultured human keratinocytes: effect on calcium flux and terminal differentiation. J. Cell Physiol. 151 (1992) 623-629
    • (1992) J. Cell Physiol. , vol.151 , pp. 623-629
    • Pillai, S.1    Bikle, D.D.2
  • 21
    • 0029858538 scopus 로고    scopus 로고
    • Gadolinium chloride inhibits Kupffer cell nitric oxide synthase (iNOS) induction
    • Roland C.R., Naziruddin B., Mohanakumar T., and Flye M.W. Gadolinium chloride inhibits Kupffer cell nitric oxide synthase (iNOS) induction. J. Leukoc. Biol. 60 (1996) 487-492
    • (1996) J. Leukoc. Biol. , vol.60 , pp. 487-492
    • Roland, C.R.1    Naziruddin, B.2    Mohanakumar, T.3    Flye, M.W.4
  • 23
    • 33751090878 scopus 로고    scopus 로고
    • Effects of La, Ce, Y, Tb on oxidation of ghost of human erythrocyte
    • Liu X., Li R., Chen J., and Wang K. Effects of La, Ce, Y, Tb on oxidation of ghost of human erythrocyte. J. Chinese Rare Earths Soc. 18 (2000) 88-90
    • (2000) J. Chinese Rare Earths Soc. , vol.18 , pp. 88-90
    • Liu, X.1    Li, R.2    Chen, J.3    Wang, K.4
  • 24
    • 26644450729 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha (TNF-α) induces the unfolded protein response (UPR) in a reactive oxygen species (ROS)-dependent fashion, and the UPR counteracts ROS accumulation by TNFα
    • Xue X., Piao J.H., Nakajima A., Sakon-Komazawa S., Kojima Y., Mori K., Yagita H., Okumura K., Harding H., and Nakano H. Tumor necrosis factor alpha (TNF-α) induces the unfolded protein response (UPR) in a reactive oxygen species (ROS)-dependent fashion, and the UPR counteracts ROS accumulation by TNFα. J. Biol. Chem. 280 (2005) 33917-33925
    • (2005) J. Biol. Chem. , vol.280 , pp. 33917-33925
    • Xue, X.1    Piao, J.H.2    Nakajima, A.3    Sakon-Komazawa, S.4    Kojima, Y.5    Mori, K.6    Yagita, H.7    Okumura, K.8    Harding, H.9    Nakano, H.10
  • 25
    • 0024239397 scopus 로고
    • Lanthanum as a calcium-substituting ion for binding to sarcoplasmic reticulum ATPase
    • Fernandez-Belda F. Lanthanum as a calcium-substituting ion for binding to sarcoplasmic reticulum ATPase. Arch. Biochem. Biophys. 267 (1988) 770-775
    • (1988) Arch. Biochem. Biophys. , vol.267 , pp. 770-775
    • Fernandez-Belda, F.1
  • 27
    • 0035991144 scopus 로고    scopus 로고
    • Immunoprecipitation techniques for the analysis of transcription factor complexes
    • Klenova E., Chernukhin I., Inoue T., Shamsuddin S., and Norton J. Immunoprecipitation techniques for the analysis of transcription factor complexes. Methods 26 (2002) 254-259
    • (2002) Methods , vol.26 , pp. 254-259
    • Klenova, E.1    Chernukhin, I.2    Inoue, T.3    Shamsuddin, S.4    Norton, J.5
  • 28
    • 0037083755 scopus 로고    scopus 로고
    • IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response
    • Lee K., Tirasophon W., Shen X., Michalak M., Prywes R., Okada T., Yoshida H., Mori K., and Kaufman R.J. IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev. 16 (2002) 452-466
    • (2002) Genes Dev. , vol.16 , pp. 452-466
    • Lee, K.1    Tirasophon, W.2    Shen, X.3    Michalak, M.4    Prywes, R.5    Okada, T.6    Yoshida, H.7    Mori, K.8    Kaufman, R.J.9
  • 29
    • 15944406434 scopus 로고    scopus 로고
    • Quantitative measurement of events in the mammalian unfolded protein response
    • Shang J. Quantitative measurement of events in the mammalian unfolded protein response. Methods 35 (2005) 390-394
    • (2005) Methods , vol.35 , pp. 390-394
    • Shang, J.1
  • 30
    • 15944366885 scopus 로고    scopus 로고
    • The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress
    • Lee A.S. The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress. Methods 35 (2005) 373-381
    • (2005) Methods , vol.35 , pp. 373-381
    • Lee, A.S.1
  • 32
    • 0035313896 scopus 로고    scopus 로고
    • Screening for human ADME/Tox drug properties in drug discovery
    • Li A.P. Screening for human ADME/Tox drug properties in drug discovery. Drug Discov. Today 6 (2001) 357-366
    • (2001) Drug Discov. Today , vol.6 , pp. 357-366
    • Li, A.P.1
  • 33
    • 0034312290 scopus 로고    scopus 로고
    • The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response
    • Tirasophon W., Lee K., Callaghan B., Welihinda A., and Kaufman R.J. The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response. Genes Dev. 14 (2000) 2725-2736
    • (2000) Genes Dev. , vol.14 , pp. 2725-2736
    • Tirasophon, W.1    Lee, K.2    Callaghan, B.3    Welihinda, A.4    Kaufman, R.J.5
  • 34
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida H., Matsui T., Yamamoto A., Okada T., and Mori K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107 (2001) 881-891
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 35
    • 29244462498 scopus 로고    scopus 로고
    • Coordination of ER and oxidative stress signaling: The PERK/Nrf2 signaling pathway
    • Cullinan S.B., and Diehl J.A. Coordination of ER and oxidative stress signaling: The PERK/Nrf2 signaling pathway. Int. J. Biochem. Cell Biol. 38 (2006) 317-332
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 317-332
    • Cullinan, S.B.1    Diehl, J.A.2
  • 38
    • 0026511824 scopus 로고
    • Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells
    • Dorner A.J., Wasley L.C., and Kaufman R.J. Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells. EMBO J. 11 (1992) 1563-1571
    • (1992) EMBO J. , vol.11 , pp. 1563-1571
    • Dorner, A.J.1    Wasley, L.C.2    Kaufman, R.J.3
  • 39
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen J., Chen X., Hendershot L., and Prywes R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell. 3 (2002) 99-111
    • (2002) Dev. Cell. , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 40
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti A., Zhang Y., Hendershot L.M., Harding H.P., and Ron D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat. Cell. Biol. 2 (2000) 326-332
    • (2000) Nat. Cell. Biol. , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 41
    • 0038308388 scopus 로고    scopus 로고
    • Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins
    • Kimata Y., Kimata Y.I., Shimizu Y., Abe H., Farcasanu I.C., Takeuchi M., Rose M.D., and Kohno K. Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins. Mol. Biol. Cell 14 (2003) 2559-2569
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2559-2569
    • Kimata, Y.1    Kimata, Y.I.2    Shimizu, Y.3    Abe, H.4    Farcasanu, I.C.5    Takeuchi, M.6    Rose, M.D.7    Kohno, K.8
  • 42
    • 8444250981 scopus 로고    scopus 로고
    • A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1
    • Kimata Y., Oikawa D., Shimizu Y., Ishiwata-Kimata Y., and Kohno K. A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1. J. Cell. Biol. 167 (2004) 445-456
    • (2004) J. Cell. Biol. , vol.167 , pp. 445-456
    • Kimata, Y.1    Oikawa, D.2    Shimizu, Y.3    Ishiwata-Kimata, Y.4    Kohno, K.5
  • 43
    • 0038043221 scopus 로고    scopus 로고
    • Structure and intermolecular interactions of the luminal dimerization domain of human IRE1alpha
    • Liu C.Y., Xu Z., and Kaufman R.J. Structure and intermolecular interactions of the luminal dimerization domain of human IRE1alpha. J. Biol. Chem. 278 (2003) 17680-17687
    • (2003) J. Biol. Chem. , vol.278 , pp. 17680-17687
    • Liu, C.Y.1    Xu, Z.2    Kaufman, R.J.3
  • 44
    • 26844439863 scopus 로고    scopus 로고
    • An essential dimer-forming subregion of the endoplasmic reticulum stress sensor Ire1
    • Oikawa D., Kimata Y., Takeuchi M., and Kohno K. An essential dimer-forming subregion of the endoplasmic reticulum stress sensor Ire1. Biochem. J. 391 (2005) 135-142
    • (2005) Biochem. J. , vol.391 , pp. 135-142
    • Oikawa, D.1    Kimata, Y.2    Takeuchi, M.3    Kohno, K.4
  • 45
    • 0030945046 scopus 로고    scopus 로고
    • Gene induction in response to unfolded protein in the endoplasmic reticulum is mediated through Ire1p kinase interaction with a transcriptional coactivator complex containing Ada5p
    • Welihinda A.A., Tirasophon W., Green S.R., and Kaufman R.J. Gene induction in response to unfolded protein in the endoplasmic reticulum is mediated through Ire1p kinase interaction with a transcriptional coactivator complex containing Ada5p. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 4289-4294
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 4289-4294
    • Welihinda, A.A.1    Tirasophon, W.2    Green, S.R.3    Kaufman, R.J.4
  • 46
    • 0029903049 scopus 로고    scopus 로고
    • Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
    • Shamu C.E., and Walter P. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 15 (1996) 3028-3039
    • (1996) EMBO J. , vol.15 , pp. 3028-3039
    • Shamu, C.E.1    Walter, P.2


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