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Volumn 147, Issue 6, 1999, Pages 1195-1204

Stress-associated endoplasmic reticulum protein 1 (SERP1)/ribosome- associated membrane protein 4 (RAMP4) stabilizes membrane proteins during stress and facilitates subsequent glycosylation

Author keywords

Aggregation degradation; Endoplasmic reticulum stress; Hypoxia; Refolding; Translocon

Indexed keywords

CALCIMYCIN; CALNEXIN; CHAPERONE; COMPLEMENTARY DNA; MEMBRANE PROTEIN; POLYPEPTIDE; TUNICAMYCIN;

EID: 0033552594     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.147.6.1195     Document Type: Article
Times cited : (106)

References (42)
  • 2
    • 0032491397 scopus 로고    scopus 로고
    • The mechanism underlying cystic fibrosis transmembrane conductance regulator transport from the endoplasmic reticulum to the proteasome includes Sec61β and a cytosolic, deglycosylated intermediary
    • Bebok, Z., C. Mazzochi, S.A. King, J.S. Hong, and E.J. Sorscher. 1998. The mechanism underlying cystic fibrosis transmembrane conductance regulator transport from the endoplasmic reticulum to the proteasome includes Sec61β and a cytosolic, deglycosylated intermediary. J. Biol. Chem. 273: 29873-29878.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29873-29878
    • Bebok, Z.1    Mazzochi, C.2    King, S.A.3    Hong, J.S.4    Sorscher, E.J.5
  • 3
    • 0028052160 scopus 로고
    • Induction of FK506-binding protein, FKBP13, under conditions which misfold proteins in endoplasmic reticulum
    • Bush, K.T., B.A. Hendrickson, and S.K. Nigam. 1994. Induction of FK506-binding protein, FKBP13, under conditions which misfold proteins in endoplasmic reticulum. Biochem. J. 303:705-708.
    • (1994) Biochem. J. , vol.303 , pp. 705-708
    • Bush, K.T.1    Hendrickson, B.A.2    Nigam, S.K.3
  • 4
    • 0028799654 scopus 로고
    • Calcium still center-stage in hypoxic-ischemic neuronal death
    • Choi, D.W. 1995. Calcium still center-stage in hypoxic-ischemic neuronal death. Trends Neurosci. 18:58-60.
    • (1995) Trends Neurosci. , vol.18 , pp. 58-60
    • Choi, D.W.1
  • 5
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's Aβ (1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • Coor, D.G., M.S. Forman, J.C. Sung, S. Leight, D.L. Kolson, T. Iwatsubo, V.M.Y. Lee, and R.W. Doms. 1997. Alzheimer's Aβ (1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nat. Med. 3:1021-1023.
    • (1997) Nat. Med. , vol.3 , pp. 1021-1023
    • Coor, D.G.1    Forman, M.S.2    Sung, J.C.3    Leight, S.4    Kolson, D.L.5    Iwatsubo, T.6    Lee, V.M.Y.7    Doms, R.W.8
  • 6
    • 0027397693 scopus 로고
    • Progression from ischemic injury to infarct following middle cerebral artery occlusion in the rat
    • Garcia, J.H., Y. Yoshida, H. Chen, Y. Li, Z.G. Zhang, J. Lian, S. Chen, and M. Chopp. 1993. Progression from ischemic injury to infarct following middle cerebral artery occlusion in the rat. Am. J. Pathol. 142:623-635.
    • (1993) Am. J. Pathol. , vol.142 , pp. 623-635
    • Garcia, J.H.1    Yoshida, Y.2    Chen, H.3    Li, Y.4    Zhang, Z.G.5    Lian, J.6    Chen, S.7    Chopp, M.8
  • 7
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
    • Görlich, D., and T.A. Rapoport. 1993. Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell. 75:615-630.
    • (1993) Cell , vol.75 , pp. 615-630
    • Görlich, D.1    Rapoport, T.A.2
  • 8
    • 0026466143 scopus 로고
    • A mammalian homologue of sec61p and secYp is associated with ribosomes and nascent polypeptides during translocation
    • Görlich, D., S. Prehn, E. Hartmann, U.K. Kalies, and T.A. Rapoport. 1992. A mammalian homologue of sec61p and secYp is associated with ribosomes and nascent polypeptides during translocation. Cell. 71:489-503.
    • (1992) Cell , vol.71 , pp. 489-503
    • Görlich, D.1    Prehn, S.2    Hartmann, E.3    Kalies, U.K.4    Rapoport, T.A.5
  • 9
    • 0342351613 scopus 로고
    • Predicting the orientation of eukaryotic membrane spanning proteins
    • Hartmann, E., T.A. Rapoport, and H.F. Lodish. 1989. Predicting the orientation of eukaryotic membrane spanning proteins. Proc. Natl. Acad. Sci. USA. 86:5786-5790.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5786-5790
    • Hartmann, E.1    Rapoport, T.A.2    Lodish, H.F.3
  • 10
    • 0027958547 scopus 로고
    • Evolutionary conservation of components of the protein translocalion complex
    • Hartmann, E., T. Sommer, S. Prehn, D. Gorlich, S. Jentsch, and T.A. Rapoport. 1994. Evolutionary conservation of components of the protein translocalion complex. Nature. 367:654-657.
    • (1994) Nature , vol.367 , pp. 654-657
    • Hartmann, E.1    Sommer, T.2    Prehn, S.3    Gorlich, D.4    Jentsch, S.5    Rapoport, T.A.6
  • 12
    • 0001318257 scopus 로고
    • Astrocytes
    • 2nd ed. A. Lajtha, editor. Plenum Press. New York
    • Hertz, L. 1982. Astrocytes. In Handbook of Neurochemistry. Vol. 1. 2nd ed. A. Lajtha, editor. Plenum Press. New York. 603-661.
    • (1982) Handbook of Neurochemistry , vol.1 , pp. 603-661
    • Hertz, L.1
  • 13
  • 14
    • 13244300647 scopus 로고    scopus 로고
    • Exposure of astrocytes to hypoxia/reoxygenation enhances expression of glucose-regulated protein 78 facilitating astrocyte release of the neuroprotective cytokine interleukin 6
    • Hori, O., M. Matsumoto, K. Kuwabara, Y. Maeda, H. Ueda, T. Ohtsuki, T. Kinoshita, S. Ogawa, D. Stern, and T. Kamada. 1996. Exposure of astrocytes to hypoxia/reoxygenation enhances expression of glucose-regulated protein 78 facilitating astrocyte release of the neuroprotective cytokine interleukin 6. J. Neurochem. 66:973-979.
    • (1996) J. Neurochem. , vol.66 , pp. 973-979
    • Hori, O.1    Matsumoto, M.2    Kuwabara, K.3    Maeda, Y.4    Ueda, H.5    Ohtsuki, T.6    Kinoshita, T.7    Ogawa, S.8    Stern, D.9    Kamada, T.10
  • 15
    • 0031889323 scopus 로고    scopus 로고
    • Induction of 72-kDa inducible heat shock protein (HSP72) in cultured rat astrocytes after energy depletion
    • Imuta, N., S. Ogawa, Y. Maeda, K. Kuwabara, O. Hori, H. Ueda, T. Yanagihara, and M. Tohyama. 1998. Induction of 72-kDa inducible heat shock protein (HSP72) in cultured rat astrocytes after energy depletion. J. Neurochem. 70:550-557.
    • (1998) J. Neurochem. , vol.70 , pp. 550-557
    • Imuta, N.1    Ogawa, S.2    Maeda, Y.3    Kuwabara, K.4    Hori, O.5    Ueda, H.6    Yanagihara, T.7    Tohyama, M.8
  • 16
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen, T.J., M.A. Loo, S. Pind, D.B. Williams, A.L. Goldberg, and J.R. Riordan. 1995. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell. 83:129-135.
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 17
    • 0031781639 scopus 로고    scopus 로고
    • The β subunit of the sec61 complex facilitates cotranslational protein transport and interacts with the signal peptidase during translocation
    • Kalies, U.K., T.A. Rapoport, and E. Hartmann. 1998. The β subunit of the sec61 complex facilitates cotranslational protein transport and interacts with the signal peptidase during translocation. J. Cell Biol. 141:887-894.
    • (1998) J. Cell Biol. , vol.141 , pp. 887-894
    • Kalies, U.K.1    Rapoport, T.A.2    Hartmann, E.3
  • 18
    • 0030609883 scopus 로고    scopus 로고
    • Altered gene expression in brain ischemia
    • Koistinaho, J., and T. Hokfelt. 1997. Altered gene expression in brain ischemia. Neuroreport. 8:1-8.
    • (1997) Neuroreport , vol.8 , pp. 1-8
    • Koistinaho, J.1    Hokfelt, T.2
  • 19
    • 0027401769 scopus 로고
    • A class of membrane proteins with a c-terminal anchor
    • Kutay, U., E. Hartmann, and T.A. Rapoport. 1993. A class of membrane proteins with a c-terminal anchor. Trends Cell Biol. 3:72-75.
    • (1993) Trends Cell Biol. , vol.3 , pp. 72-75
    • Kutay, U.1    Hartmann, E.2    Rapoport, T.A.3
  • 20
    • 0029915707 scopus 로고    scopus 로고
    • Purification and characterization of a novel stress protein, the 150-kDa oxygen-regulated protein (ORP150), from cultured rat astrocytes and its expression in ischemic mouse brain
    • Kuwabara, K., M. Matsumoto, J. Ikeda, O. Hori, S. Ogawa, Y. Maeda, K. Kitagawa, N. Imuta, T. Kinoshita, D. Stern, et al. 1996. Purification and characterization of a novel stress protein, the 150-kDa oxygen-regulated protein (ORP150), from cultured rat astrocytes and its expression in ischemic mouse brain. J. Biol. Chem. 27:5025-5032.
    • (1996) J. Biol. Chem. , vol.27 , pp. 5025-5032
    • Kuwabara, K.1    Matsumoto, M.2    Ikeda, J.3    Hori, O.4    Ogawa, S.5    Maeda, Y.6    Kitagawa, K.7    Imuta, N.8    Kinoshita, T.9    Stern, D.10
  • 21
    • 0026674886 scopus 로고
    • Differential display of eukaryotic messenger RNA by means of the polymerase chain reaction
    • Liang, P., and A.B. Pardee. 1992. Differential display of eukaryotic messenger RNA by means of the polymerase chain reaction. Science. 257:967-971.
    • (1992) Science , vol.257 , pp. 967-971
    • Liang, P.1    Pardee, A.B.2
  • 22
    • 0028044860 scopus 로고
    • Increased expression of mRNA encoding calbindin-D28K, the glucose-regulated proteins, or 72 kDa heat shock protein in three models of acute CNS injury
    • Lowenstein, D.H., R.P. Gwinn, and M.S. Seren. 1994. Increased expression of mRNA encoding calbindin-D28K, the glucose-regulated proteins, or 72 kDa heat shock protein in three models of acute CNS injury. Mol. Brain Res. 22: 299-308.
    • (1994) Mol. Brain Res. , vol.22 , pp. 299-308
    • Lowenstein, D.H.1    Gwinn, R.P.2    Seren, M.S.3
  • 24
    • 0028902781 scopus 로고
    • Cloning of rat grp75, an hsp 70-family member, and its expression in neuronal and ischemic brain
    • Massa, S.M., F.M. Longo, J. Zuo, W.J. Chen, and F.R. Sharp. 1995. Cloning of rat grp75, an hsp 70-family member, and its expression in neuronal and ischemic brain. J. Neurosci. Res. 40:807-819.
    • (1995) J. Neurosci. Res. , vol.40 , pp. 807-819
    • Massa, S.M.1    Longo, F.M.2    Zuo, J.3    Chen, W.J.4    Sharp, F.R.5
  • 25
    • 0028807463 scopus 로고
    • Cloning of a novel RNA binding poly-peptide (RA301) induced by hypoxia/reoxygenation
    • Matsuo, N., S. Ogawa, Y. Imai, T. Takagi, M. Tohyama, D. Stern, and A. Wanaka. 1995. Cloning of a novel RNA binding poly-peptide (RA301) induced by hypoxia/reoxygenation. J. Biol. Chem. 270:28216-28222.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28216-28222
    • Matsuo, N.1    Ogawa, S.2    Imai, Y.3    Takagi, T.4    Tohyama, M.5    Stern, D.6    Wanaka, A.7
  • 26
    • 0030972146 scopus 로고    scopus 로고
    • Cloning of a putative vesicle transport-related protein. RA410, from cultured rat astrocytes and its expression in ischemic rat brain
    • Matsuo, N., S. Ogawa, T. Takagi, A. Wanaka, T. Mori, M. Matsuyama, D. Pinsky, D. Stern, and M. Tohyama. 1997. Cloning of a putative vesicle transport-related protein. RA410, from cultured rat astrocytes and its expression in ischemic rat brain. J. Biol. Chem. 272:16438-16444.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16438-16444
    • Matsuo, N.1    Ogawa, S.2    Takagi, T.3    Wanaka, A.4    Mori, T.5    Matsuyama, M.6    Pinsky, D.7    Stern, D.8    Tohyama, M.9
  • 27
    • 0019313317 scopus 로고
    • Preparation of separate and astroglial and oligodendroglial cell cultures from rat cerebral tissue
    • McCarthy, K.D., and J. de Vellis. 1980. Preparation of separate and astroglial and oligodendroglial cell cultures from rat cerebral tissue. J. Cell Biol. 85: 890-902.
    • (1980) J. Cell Biol. , vol.85 , pp. 890-902
    • McCarthy, K.D.1    De Vellis, J.2
  • 28
    • 0023277174 scopus 로고
    • Oxygen-derived radicals: A link between reperfusion injury and inflammation
    • McCord, J.M. 1987. Oxygen-derived radicals: a link between reperfusion injury and inflammation. Fed. Proc. 46:2402-2406.
    • (1987) Fed. Proc. , vol.46 , pp. 2402-2406
    • McCord, J.M.1
  • 30
    • 0025348272 scopus 로고
    • Hypoxia modulates the barrier and coagulant function of cultures of bovine endothelium
    • Ogawa, S., G. Herwig, C. Esposito, A.P. Macaulay, J. Brett, and D. Stern. 1990. Hypoxia modulates the barrier and coagulant function of cultures of bovine endothelium. J. Clin. Invest. 69:1090-1098.
    • (1990) J. Clin. Invest. , vol.69 , pp. 1090-1098
    • Ogawa, S.1    Herwig, G.2    Esposito, C.3    Macaulay, A.P.4    Brett, J.5    Stern, D.6
  • 31
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou, W.J., P.H. Cameron, D.Y. Thomas, and J.J.M. Bergeron. 1993. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature. 364:771-776.
    • (1993) Nature , vol.364 , pp. 771-776
    • Ou, W.J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.M.4
  • 33
    • 0028872674 scopus 로고
    • Excitotoxity and the NMDA receptor -still lethal alter eight years
    • Rothman, S.M., and J.W. Olney. 1995. Excitotoxity and the NMDA receptor -still lethal alter eight years. Trends Neurosci. 18:57-58.
    • (1995) Trends Neurosci. , vol.18 , pp. 57-58
    • Rothman, S.M.1    Olney, J.W.2
  • 34
    • 0025761728 scopus 로고
    • Yeast gene which suppresses the defect in protein transport of a secY mutant of E. coli
    • Sakaguchi, M., C. Ueguchi, K. Ito, and T. Omura. 1991. Yeast gene which suppresses the defect in protein transport of a secY mutant of E. coli. J. Biochem. 109:799-802.
    • (1991) J. Biochem. , vol.109 , pp. 799-802
    • Sakaguchi, M.1    Ueguchi, C.2    Ito, K.3    Omura, T.4
  • 35
    • 0028233384 scopus 로고
    • The endothelial cell binding site for advanced glycation end products consists of a complex: An integral membrane protein and a lactoferrin-like polypeptide
    • Schmidt, A.M., R. Mora, R. Cao, S.D. Yan, J. Brett, R. Ramakrishnan, T.C. Tsang, M. Simionescu, and D. Stern. 1994. The endothelial cell binding site for advanced glycation end products consists of a complex: an integral membrane protein and a lactoferrin-like polypeptide. J. Biol. Chem. 269:9882-9888.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9882-9888
    • Schmidt, A.M.1    Mora, R.2    Cao, R.3    Yan, S.D.4    Brett, J.5    Ramakrishnan, R.6    Tsang, T.C.7    Simionescu, M.8    Stern, D.9
  • 36
    • 0029088742 scopus 로고
    • Advanced glycation endproducts interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM-1) in cultured human endothelial cells and in mice: A potential mechanism for the accelerated vasculopathy of diabetes
    • Schmidt, A.M., O. Hori, J.X. Chen, J.F. Li, J. Crandall, J. Zhang, R. Cao, S.D. Yan, J. Brett, and D. Stern. 1995. Advanced glycation endproducts interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM-1) in cultured human endothelial cells and in mice: a potential mechanism for the accelerated vasculopathy of diabetes. J. Clin. Invest. 96:1395-1403.
    • (1995) J. Clin. Invest. , vol.96 , pp. 1395-1403
    • Schmidt, A.M.1    Hori, O.2    Chen, J.X.3    Li, J.F.4    Crandall, J.5    Zhang, J.6    Cao, R.7    Yan, S.D.8    Brett, J.9    Stern, D.10
  • 38
    • 0031441165 scopus 로고    scopus 로고
    • Differential hydroxylation of salicylate in core and penumbra regions during focal reversible cerebral ischemia
    • Solenski, N.J., A.L. Kwan, H. Yamamoto, J.P. Bennett, N.F. Kassell, and K.S. Lee. 1997. Differential hydroxylation of salicylate in core and penumbra regions during focal reversible cerebral ischemia. Stroke. 28:2545-2552.
    • (1997) Stroke , vol.28 , pp. 2545-2552
    • Solenski, N.J.1    Kwan, A.L.2    Yamamoto, H.3    Bennett, J.P.4    Kassell, N.F.5    Lee, K.S.6
  • 39
    • 0029961386 scopus 로고    scopus 로고
    • 150-kD oxygen-regulated protein is expressed in human atherosclerotic plaques and allows mononuclear phagocytes to withstand cellular stress on exposure to hypoxia and modified low density lipoprotein
    • Tsukamoto, Y., K. Kuwabara, S. Hirota, J. Ikeda, D. Stern, H. Yanagi, M. Matsumoto, S. Ogawa, and Y. Kitamura. 1996. 150-kD oxygen-regulated protein is expressed in human atherosclerotic plaques and allows mononuclear phagocytes to withstand cellular stress on exposure to hypoxia and modified low density lipoprotein. J. Clin. Invest. 98:1930-1941.
    • (1996) J. Clin. Invest. , vol.98 , pp. 1930-1941
    • Tsukamoto, Y.1    Kuwabara, K.2    Hirota, S.3    Ikeda, J.4    Stern, D.5    Yanagi, H.6    Matsumoto, M.7    Ogawa, S.8    Kitamura, Y.9
  • 40
    • 0030815129 scopus 로고    scopus 로고
    • Promotion of transferrin folding by cyclic interaction with calnexin and calreticulin
    • Wada, I., M. Kai, S. Imai, F. Sakane, and H. Kanoh. 1997. Promotion of transferrin folding by cyclic interaction with calnexin and calreticulin. EMBO (Eur. Mol. Biol Organ.) J. 16:5420-5432.
    • (1997) EMBO (Eur. Mol. Biol Organ.) J. , vol.16 , pp. 5420-5432
    • Wada, I.1    Kai, M.2    Imai, S.3    Sakane, F.4    Kanoh, H.5
  • 41
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C.L., S. Omura, and R.R. Kopito. 1995. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell. 83:121-127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3


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