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Volumn 6, Issue 8, 2011, Pages

Protein C mutation (A267T) results in ER retention and unfolded protein response activation

Author keywords

[No Author keywords available]

Indexed keywords

CALRETICULIN; CHAPERONE; DNA; GLUCOSE REGULATED PROTEIN 94; IMMUNOGLOBULIN BINDING FACTOR; INITIATION FACTOR 2ALPHA; PROTEASOME; PROTEIN C;

EID: 80052060531     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0024009     Document Type: Article
Times cited : (10)

References (40)
  • 1
    • 18244417756 scopus 로고    scopus 로고
    • Molecular recognition in the protein C anticoagulant pathway
    • Dahlback B, Villoutreix BO, (2003) Molecular recognition in the protein C anticoagulant pathway. J Thromb Haemost 1: 1525-1534.
    • (2003) J Thromb Haemost , vol.1 , pp. 1525-1534
    • Dahlback, B.1    Villoutreix, B.O.2
  • 4
    • 0026645428 scopus 로고
    • Protein C deficiency Hong Kong 1 and 2: hereditary protein C deficiency caused by two mutant alleles, a 5-nucleotide deletion and a missense mutation
    • Sugahara Y, Miura O, Yuen P, Aoki N, (1992) Protein C deficiency Hong Kong 1 and 2: hereditary protein C deficiency caused by two mutant alleles, a 5-nucleotide deletion and a missense mutation. Blood 80: 126-133.
    • (1992) Blood , vol.80 , pp. 126-133
    • Sugahara, Y.1    Miura, O.2    Yuen, P.3    Aoki, N.4
  • 5
    • 0028609488 scopus 로고
    • Compound heterozygous protein C deficiency caused by two mutations, Arg-178 to Gln and Cys-331 to Arg, leading to impaired secretion of mutant protein C
    • Sugahara Y, Miura O, Hirosawa S, Aoki N, (1994) Compound heterozygous protein C deficiency caused by two mutations, Arg-178 to Gln and Cys-331 to Arg, leading to impaired secretion of mutant protein C. Thrombosis and Haemostasis 72: 814-818.
    • (1994) Thrombosis and Haemostasis , vol.72 , pp. 814-818
    • Sugahara, Y.1    Miura, O.2    Hirosawa, S.3    Aoki, N.4
  • 6
    • 0029680791 scopus 로고    scopus 로고
    • Cellular basis for protein C deficiency caused by a single amino acid substitution at Arg15 in the gamma-carboxyglutamic acid domain
    • Tokunaga F, Tsukamoto T, Koide T, (1996) Cellular basis for protein C deficiency caused by a single amino acid substitution at Arg15 in the gamma-carboxyglutamic acid domain. J Biochem 120: 360-368.
    • (1996) J Biochem , vol.120 , pp. 360-368
    • Tokunaga, F.1    Tsukamoto, T.2    Koide, T.3
  • 7
    • 0029947353 scopus 로고    scopus 로고
    • Protein C Nagoya, an elongated mutant of protein C, is retained within the endoplasmic reticulum and is associated with GRP78 and GRP94
    • Katsumi A, Senda T, Yamashita Y, Yamazaki T, Hamaguchi M, et al. (1996) Protein C Nagoya, an elongated mutant of protein C, is retained within the endoplasmic reticulum and is associated with GRP78 and GRP94. Blood 87: 4164-4175.
    • (1996) Blood , vol.87 , pp. 4164-4175
    • Katsumi, A.1    Senda, T.2    Yamashita, Y.3    Yamazaki, T.4    Hamaguchi, M.5
  • 8
    • 0034994095 scopus 로고    scopus 로고
    • Symptomatic type 1 protein C deficiency caused by a de novo Ser270Leu mutation in the catalytic domain
    • Lind B, Koefoed P, Thorsen S, (2001) Symptomatic type 1 protein C deficiency caused by a de novo Ser270Leu mutation in the catalytic domain. British Journal of Haematology 113: 642-648.
    • (2001) British Journal of Haematology , vol.113 , pp. 642-648
    • Lind, B.1    Koefoed, P.2    Thorsen, S.3
  • 9
    • 0036799853 scopus 로고    scopus 로고
    • Protein C deficiency caused by homozygosity for a novel PROC D180G mutation--in vitro expression and structural analysis of the mutation
    • Lind B, Gedde-Dahl T, Tjonnfjord G, Villoutreix BO, Brosstad F, (2002) Protein C deficiency caused by homozygosity for a novel PROC D180G mutation--in vitro expression and structural analysis of the mutation. Thrombosis and Haemostasis 88: 632-638.
    • (2002) Thrombosis and Haemostasis , vol.88 , pp. 632-638
    • Lind, B.1    Gedde-Dahl, T.2    Tjonnfjord, G.3    Villoutreix, B.O.4    Brosstad, F.5
  • 10
    • 0037630008 scopus 로고    scopus 로고
    • Defective sorting to secretory vesicles in trans-Golgi network is partly responsible for protein C deficiency: molecular mechanisms of impaired secretion of abnormal protein C R169W, R352W, and G376D
    • Naito M, Mimuro J, Endo H, Madoiwa S, Ogata K, et al. (2003) Defective sorting to secretory vesicles in trans-Golgi network is partly responsible for protein C deficiency: molecular mechanisms of impaired secretion of abnormal protein C R169W, R352W, and G376D. Circulation Research 92: 865-872.
    • (2003) Circulation Research , vol.92 , pp. 865-872
    • Naito, M.1    Mimuro, J.2    Endo, H.3    Madoiwa, S.4    Ogata, K.5
  • 11
    • 33645647884 scopus 로고    scopus 로고
    • Molecular mechanism for hereditary protein C deficiency in two Chinese families with thrombosis
    • Zhou RF, Cai XH, Xie S, Wang XF, Wang HL, (2006) Molecular mechanism for hereditary protein C deficiency in two Chinese families with thrombosis. J Thromb Haemost 4: 1154-1156.
    • (2006) J Thromb Haemost , vol.4 , pp. 1154-1156
    • Zhou, R.F.1    Cai, X.H.2    Xie, S.3    Wang, X.F.4    Wang, H.L.5
  • 12
    • 10444279177 scopus 로고    scopus 로고
    • Gradually glycosylated protein C mutants (Arg178Gln and Cys331Arg) are degraded by proteasome after mannose trimming
    • Nakahara M, Koyama T, Nakazawa F, Nishio M, Shibamiya A, et al. (2004) Gradually glycosylated protein C mutants (Arg178Gln and Cys331Arg) are degraded by proteasome after mannose trimming. Thrombosis and Haemostasis 92: 1284-1290.
    • (2004) Thrombosis and Haemostasis , vol.92 , pp. 1284-1290
    • Nakahara, M.1    Koyama, T.2    Nakazawa, F.3    Nishio, M.4    Shibamiya, A.5
  • 17
    • 2342584657 scopus 로고    scopus 로고
    • Apoptosis-inducing signal sequence mutation in carbonic anhydrase IV identified in patients with the RP17 form of retinitis pigmentosa
    • Rebello G, Ramesar R, Vorster A, Roberts L, Ehrenreich L, et al. (2004) Apoptosis-inducing signal sequence mutation in carbonic anhydrase IV identified in patients with the RP17 form of retinitis pigmentosa. Proc Natl Acad Sci U S A 101: 6617-6622.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 6617-6622
    • Rebello, G.1    Ramesar, R.2    Vorster, A.3    Roberts, L.4    Ehrenreich, L.5
  • 18
    • 33644863652 scopus 로고    scopus 로고
    • Retention of mutant low density lipoprotein receptor in endoplasmic reticulum (ER) leads to ER stress
    • Sorensen S, Ranheim T, Bakken KS, Leren TP, Kulseth MA, (2006) Retention of mutant low density lipoprotein receptor in endoplasmic reticulum (ER) leads to ER stress. J Biol Chem 281: 468-476.
    • (2006) J Biol Chem , vol.281 , pp. 468-476
    • Sorensen, S.1    Ranheim, T.2    Bakken, K.S.3    Leren, T.P.4    Kulseth, M.A.5
  • 19
    • 0033864420 scopus 로고    scopus 로고
    • Intracellular degradation of histidine-rich glycoprotein mutants: tokushima-1 and 2 mutants are degraded by different proteolytic systems
    • Wakabayashi S, Yoshida H, Shigekiyo T, Koide T, (2000) Intracellular degradation of histidine-rich glycoprotein mutants: tokushima-1 and 2 mutants are degraded by different proteolytic systems. J Biochem 128: 201-206.
    • (2000) J Biochem , vol.128 , pp. 201-206
    • Wakabayashi, S.1    Yoshida, H.2    Shigekiyo, T.3    Koide, T.4
  • 20
    • 13244271981 scopus 로고    scopus 로고
    • Two novel mutations in EGF-like domains of human factor IX dramatically impair intracellular processing and secretion
    • Enjolras N, Plantier JL, Rodriguez MH, Rea M, Attali O, et al. (2004) Two novel mutations in EGF-like domains of human factor IX dramatically impair intracellular processing and secretion. J Thromb Haemost 2: 1143-1154.
    • (2004) J Thromb Haemost , vol.2 , pp. 1143-1154
    • Enjolras, N.1    Plantier, J.L.2    Rodriguez, M.H.3    Rea, M.4    Attali, O.5
  • 21
    • 29244468279 scopus 로고    scopus 로고
    • Characterization of endoplasmic reticulum-associated degradation of a protein S mutant identified in a family of quantitative protein S deficiency
    • Tsuda H, Tokunaga F, Nagamitsu H, Koide T, (2006) Characterization of endoplasmic reticulum-associated degradation of a protein S mutant identified in a family of quantitative protein S deficiency. Thrombosis Research 117: 323-331.
    • (2006) Thrombosis Research , vol.117 , pp. 323-331
    • Tsuda, H.1    Tokunaga, F.2    Nagamitsu, H.3    Koide, T.4
  • 22
    • 62549147038 scopus 로고    scopus 로고
    • The E693Delta mutation in amyloid precursor protein increases intracellular accumulation of amyloid beta oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells
    • Nishitsuji K, Tomiyama T, Ishibashi K, Ito K, Teraoka R, et al. (2009) The E693Delta mutation in amyloid precursor protein increases intracellular accumulation of amyloid beta oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells. Am J Pathol 174: 957-969.
    • (2009) Am J Pathol , vol.174 , pp. 957-969
    • Nishitsuji, K.1    Tomiyama, T.2    Ishibashi, K.3    Ito, K.4    Teraoka, R.5
  • 23
    • 0037969934 scopus 로고    scopus 로고
    • Mutation (D472Y) in the type 3 repeat domain of cartilage oligomeric matrix protein affects its early vesicle trafficking in endoplasmic reticulum and induces apoptosis
    • Hashimoto Y, Tomiyama T, Yamano Y, Mori H, (2003) Mutation (D472Y) in the type 3 repeat domain of cartilage oligomeric matrix protein affects its early vesicle trafficking in endoplasmic reticulum and induces apoptosis. Am J Pathol 163: 101-110.
    • (2003) Am J Pathol , vol.163 , pp. 101-110
    • Hashimoto, Y.1    Tomiyama, T.2    Yamano, Y.3    Mori, H.4
  • 24
    • 73949154312 scopus 로고    scopus 로고
    • Mutant proinsulin proteins associated with neonatal diabetes are retained in the endoplasmic reticulum and not efficiently secreted
    • Park SY, Ye H, Steiner DF, Bell GI, (2010) Mutant proinsulin proteins associated with neonatal diabetes are retained in the endoplasmic reticulum and not efficiently secreted. Biochem Biophys Res Commun 391: 1449-1454.
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 1449-1454
    • Park, S.Y.1    Ye, H.2    Steiner, D.F.3    Bell, G.I.4
  • 25
    • 20044378690 scopus 로고    scopus 로고
    • A surfactant protein C precursor protein BRICHOS domain mutation causes endoplasmic reticulum stress, proteasome dysfunction, and caspase 3 activation
    • Mulugeta S, Nguyen V, Russo SJ, Muniswamy M, Beers MF, (2005) A surfactant protein C precursor protein BRICHOS domain mutation causes endoplasmic reticulum stress, proteasome dysfunction, and caspase 3 activation. Am J Respir Cell Mol Biol 32: 521-530.
    • (2005) Am J Respir Cell Mol Biol , vol.32 , pp. 521-530
    • Mulugeta, S.1    Nguyen, V.2    Russo, S.J.3    Muniswamy, M.4    Beers, M.F.5
  • 26
    • 35448933677 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress caused by aggregate-prone proteins containing homopolymeric amino acids
    • Uchio N, Oma Y, Toriumi K, Sasagawa N, Tanida I, et al. (2007) Endoplasmic reticulum stress caused by aggregate-prone proteins containing homopolymeric amino acids. FEBS J 274: 5619-5627.
    • (2007) FEBS J , vol.274 , pp. 5619-5627
    • Uchio, N.1    Oma, Y.2    Toriumi, K.3    Sasagawa, N.4    Tanida, I.5
  • 27
    • 67649859658 scopus 로고    scopus 로고
    • Deletions and missense mutations of EPM2A exacerbate unfolded protein response and apoptosis of neuronal cells induced by endoplasm reticulum stress
    • Liu Y, Wang Y, Wu C, Liu Y, Zheng P, (2009) Deletions and missense mutations of EPM2A exacerbate unfolded protein response and apoptosis of neuronal cells induced by endoplasm reticulum stress. Hum Mol Genet 18: 2622-2631.
    • (2009) Hum Mol Genet , vol.18 , pp. 2622-2631
    • Liu, Y.1    Wang, Y.2    Wu, C.3    Liu, Y.4    Zheng, P.5
  • 28
    • 77956495529 scopus 로고    scopus 로고
    • Functional characterization of the protein C A267T mutation: evidence for impaired secretion due to defective intracellular transport
    • Tjeldhorn L, Iversen N, Sandvig K, Bergan J, Sandset PM, et al. (2010) Functional characterization of the protein C A267T mutation: evidence for impaired secretion due to defective intracellular transport. BMC Cell Biol 11: 67.
    • (2010) BMC Cell Biol , vol.11 , pp. 67
    • Tjeldhorn, L.1    Iversen, N.2    Sandvig, K.3    Bergan, J.4    Sandset, P.M.5
  • 29
    • 33646195309 scopus 로고    scopus 로고
    • Temperature sensitive secretion of mutant myocilins
    • Vollrath D, Liu Y, (2006) Temperature sensitive secretion of mutant myocilins. Exp Eye Res 82: 1030-1036.
    • (2006) Exp Eye Res , vol.82 , pp. 1030-1036
    • Vollrath, D.1    Liu, Y.2
  • 30
    • 34447103301 scopus 로고    scopus 로고
    • 4-Phenylbutyrate rescues trafficking incompetent mutant alpha-galactosidase A without restoring its functionality
    • Yam GH, Roth J, Zuber C, (2007) 4-Phenylbutyrate rescues trafficking incompetent mutant alpha-galactosidase A without restoring its functionality. Biochem Biophys Res Commun 360: 375-380.
    • (2007) Biochem Biophys Res Commun , vol.360 , pp. 375-380
    • Yam, G.H.1    Roth, J.2    Zuber, C.3
  • 31
    • 43749115379 scopus 로고    scopus 로고
    • Niemann-Pick type C1 I1061T mutant encodes a functional protein that is selected for endoplasmic reticulum-associated degradation due to protein misfolding
    • Gelsthorpe ME, Baumann N, Millard E, Gale SE, Langmade SJ, et al. (2008) Niemann-Pick type C1 I1061T mutant encodes a functional protein that is selected for endoplasmic reticulum-associated degradation due to protein misfolding. J Biol Chem 283: 8229-8236.
    • (2008) J Biol Chem , vol.283 , pp. 8229-8236
    • Gelsthorpe, M.E.1    Baumann, N.2    Millard, E.3    Gale, S.E.4    Langmade, S.J.5
  • 32
    • 40849134264 scopus 로고    scopus 로고
    • Manipulating the quality control pathway in transfected cells: low temperature allows rescue of secretion-defective fibrinogen mutants
    • Vu D, Di SC, Neerman-Arbez M, (2008) Manipulating the quality control pathway in transfected cells: low temperature allows rescue of secretion-defective fibrinogen mutants. Haematologica 93: 224-231.
    • (2008) Haematologica , vol.93 , pp. 224-231
    • Vu, D.1    Di, S.C.2    Neerman-Arbez, M.3
  • 33
    • 0034717072 scopus 로고    scopus 로고
    • Degradation of human thyroperoxidase in the endoplasmic reticulum involves two different pathways depending on the folding state of the protein
    • Fayadat L, Siffroi-Fernandez S, Lanet J, Franc JL, (2000) Degradation of human thyroperoxidase in the endoplasmic reticulum involves two different pathways depending on the folding state of the protein. Journal of Biological Chemistry 275: 15948-15954.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 15948-15954
    • Fayadat, L.1    Siffroi-Fernandez, S.2    Lanet, J.3    Franc, J.L.4
  • 34
    • 0029665491 scopus 로고    scopus 로고
    • A Thr359Met mutation in factor VII of a patient with a hereditary deficiency causes defective secretion of the molecule
    • Arbini AA, Mannucci M, Bauer KA, (1996) A Thr359Met mutation in factor VII of a patient with a hereditary deficiency causes defective secretion of the molecule. Blood 87: 5085-5094.
    • (1996) Blood , vol.87 , pp. 5085-5094
    • Arbini, A.A.1    Mannucci, M.2    Bauer, K.A.3
  • 35
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: endoplasmic reticulum-associated degradation
    • Vembar SS, Brodsky JL, (2008) One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 9: 944-957.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 36
    • 67649745807 scopus 로고    scopus 로고
    • The Endoplasmic Reticulum-associated Degradation of Transthyretin Variants Is Negatively Regulated by BiP in Mammalian Cells
    • Susuki S, Sato T, Miyata M, Momohara M, Suico MA, et al. (2009) The Endoplasmic Reticulum-associated Degradation of Transthyretin Variants Is Negatively Regulated by BiP in Mammalian Cells. J Biol Chem 284: 8312-8321.
    • (2009) J Biol Chem , vol.284 , pp. 8312-8321
    • Susuki, S.1    Sato, T.2    Miyata, M.3    Momohara, M.4    Suico, M.A.5
  • 37
    • 34248997838 scopus 로고    scopus 로고
    • N-glycan structure dictates extension of protein folding or onset of disposal
    • Molinari M, (2007) N-glycan structure dictates extension of protein folding or onset of disposal. Nat Chem Biol 3: 313-320.
    • (2007) Nat Chem Biol , vol.3 , pp. 313-320
    • Molinari, M.1
  • 38
    • 17044402604 scopus 로고    scopus 로고
    • The biological and chemical basis for tissue-selective amyloid disease
    • Sekijima Y, Wiseman RL, Matteson J, Hammarstrom P, Miller SR, et al. (2005) The biological and chemical basis for tissue-selective amyloid disease. Cell 121: 73-85.
    • (2005) Cell , vol.121 , pp. 73-85
    • Sekijima, Y.1    Wiseman, R.L.2    Matteson, J.3    Hammarstrom, P.4    Miller, S.R.5
  • 39
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: protein folding, quality control, degradation, and related human diseases
    • Hebert DN, Molinari M, (2007) In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol Rev 87: 1377-1408.
    • (2007) Physiol Rev , vol.87 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 40
    • 70350323730 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress reduces the export from the ER and alters the architecture of post-ER compartments
    • Amodio G, Renna M, Paladino S, Venturi C, Tacchetti C, et al. (2009) Endoplasmic reticulum stress reduces the export from the ER and alters the architecture of post-ER compartments. Int J Biochem Cell Biol 41: 2511-2521.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 2511-2521
    • Amodio, G.1    Renna, M.2    Paladino, S.3    Venturi, C.4    Tacchetti, C.5


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