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Volumn 6, Issue 10, 2011, Pages

Progranulin, a glycoprotein deficient in frontotemporal dementia, is a novel substrate of several protein disulfide isomerase family proteins

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; CALRETICULIN; CHAPERONE; ENDOPLASMIC RETICULUM P5 PROTEIN; ENDOPLASMIC RETICULUM P57 PROTEIN; ENDOPLASMIC RETICULUM P72 PROTEIN; GLUCOSE REGULATED PROTEIN 78; GLUCOSE REGULATED PROTEIN 94; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 70 1; PROGRANULIN; PROTEIN DISULFIDE ISOMERASE; UNCLASSIFIED DRUG; BIOLOGICAL MARKER; GLYCOPROTEIN; GRN PROTEIN, MOUSE; PDIA3 PROTEIN, HUMAN; PDIA6 PROTEIN, HUMAN; SIGNAL PEPTIDE;

EID: 80054737024     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0026454     Document Type: Article
Times cited : (60)

References (30)
  • 1
    • 56749095159 scopus 로고    scopus 로고
    • New approaches to the treatment of frontotemporal lobar degeneration
    • Vossel KA, Miller BL, (2008) New approaches to the treatment of frontotemporal lobar degeneration. Curr Opin Neurol 21: 708-716.
    • (2008) Curr Opin Neurol , vol.21 , pp. 708-716
    • Vossel, K.A.1    Miller, B.L.2
  • 3
    • 33746919083 scopus 로고    scopus 로고
    • Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17
    • Baker M, Mackenzie IR, Pickering-Brown SM, Gass J, Rademakers R, et al. (2006) Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17. Nature 442: 916-919.
    • (2006) Nature , vol.442 , pp. 916-919
    • Baker, M.1    Mackenzie, I.R.2    Pickering-Brown, S.M.3    Gass, J.4    Rademakers, R.5
  • 4
    • 33746910649 scopus 로고    scopus 로고
    • Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21
    • Cruts M, Gijselinck I, van der Zee J, Engelborghs S, Wils H, et al. (2006) Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21. Nature 442: 920-924.
    • (2006) Nature , vol.442 , pp. 920-924
    • Cruts, M.1    Gijselinck, I.2    van der Zee, J.3    Engelborghs, S.4    Wils, H.5
  • 6
    • 34247868937 scopus 로고    scopus 로고
    • Mutations other than null mutations producing a pathogenic loss of progranulin in frontotemporal dementia
    • van der Zee J, Le Ber I, Maurer-Stroh S, Engelborghs S, Gijselinck I, et al. (2007) Mutations other than null mutations producing a pathogenic loss of progranulin in frontotemporal dementia. Hum Mutat 28: 416.
    • (2007) Hum Mutat , vol.28 , pp. 416
    • van der Zee, J.1    Le Ber, I.2    Maurer-Stroh, S.3    Engelborghs, S.4    Gijselinck, I.5
  • 7
    • 45049084534 scopus 로고    scopus 로고
    • Deletion of the progranulin gene in patients with frontotemporal lobar degeneration or Parkinson disease
    • Rovelet-Lecrux A, Deramecourt V, Legallic S, Maurage CA, Le Ber I, et al. (2008) Deletion of the progranulin gene in patients with frontotemporal lobar degeneration or Parkinson disease. Neurobiol Dis 31: 41-45.
    • (2008) Neurobiol Dis , vol.31 , pp. 41-45
    • Rovelet-Lecrux, A.1    Deramecourt, V.2    Legallic, S.3    Maurage, C.A.4    Le Ber, I.5
  • 8
    • 75949130374 scopus 로고    scopus 로고
    • Pathogenic cysteine mutations affect progranulin function and production of mature granulins
    • Wang J, Van Damme P, Cruchaga C, Gitcho MA, Vidal JM, et al. (2010) Pathogenic cysteine mutations affect progranulin function and production of mature granulins. J Neurochem 112: 1305-1315.
    • (2010) J Neurochem , vol.112 , pp. 1305-1315
    • Wang, J.1    Van Damme, P.2    Cruchaga, C.3    Gitcho, M.A.4    Vidal, J.M.5
  • 9
    • 79955534069 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid (vorinostat) up-regulates progranulin transcription: rational therapeutic approach to frontotemporal dementia
    • Cenik B, Sephton CF, Dewey CM, Xian X, Wei S, et al. (2011) Suberoylanilide hydroxamic acid (vorinostat) up-regulates progranulin transcription: rational therapeutic approach to frontotemporal dementia. J Biol Chem 286: 16101-16108.
    • (2011) J Biol Chem , vol.286 , pp. 16101-16108
    • Cenik, B.1    Sephton, C.F.2    Dewey, C.M.3    Xian, X.4    Wei, S.5
  • 10
    • 77956270128 scopus 로고    scopus 로고
    • MicroRNA-29b regulates the expression level of human progranulin, a secreted glycoprotein implicated in frontotemporal dementia
    • Jiao J, Herl LD, Farese RV, Gao F-B, (2010) MicroRNA-29b regulates the expression level of human progranulin, a secreted glycoprotein implicated in frontotemporal dementia. PLoS One 5: e10551.
    • (2010) PLoS One , vol.5
    • Jiao, J.1    Herl, L.D.2    Farese, R.V.3    Gao, F.-B.4
  • 11
    • 77954619214 scopus 로고    scopus 로고
    • miR-107 regulates granulin/progranulin with implications for traumatic brain injury and neurodegenerative disease
    • Wang WX, Wilfred BR, Madathil SK, Tang G, Hu Y, et al. (2010) miR-107 regulates granulin/progranulin with implications for traumatic brain injury and neurodegenerative disease. Am J Pathol 177: 334-345.
    • (2010) Am J Pathol , vol.177 , pp. 334-345
    • Wang, W.X.1    Wilfred, B.R.2    Madathil, S.K.3    Tang, G.4    Hu, Y.5
  • 12
    • 56049083010 scopus 로고    scopus 로고
    • Common variation in the miR-659 binding-site of GRN is a major risk factor for TDP43-positive frontotemporal dementia
    • Rademakers R, Eriksen JL, Baker M, Robinson T, Ahmed Z, et al. (2008) Common variation in the miR-659 binding-site of GRN is a major risk factor for TDP43-positive frontotemporal dementia. Hum Mol Genet 17: 3631-3642.
    • (2008) Hum Mol Genet , vol.17 , pp. 3631-3642
    • Rademakers, R.1    Eriksen, J.L.2    Baker, M.3    Robinson, T.4    Ahmed, Z.5
  • 13
    • 79551543554 scopus 로고    scopus 로고
    • Rescue of progranulin deficiency associated with frontotemporal lobar degeneration by alkalizing reagents and inhibition of vacuolar ATPase
    • Capell A, Liebscher S, Fellerer K, Brouwers N, Willem M, et al. (2011) Rescue of progranulin deficiency associated with frontotemporal lobar degeneration by alkalizing reagents and inhibition of vacuolar ATPase. J Neurosci 31: 1885-1894.
    • (2011) J Neurosci , vol.31 , pp. 1885-1894
    • Capell, A.1    Liebscher, S.2    Fellerer, K.3    Brouwers, N.4    Willem, M.5
  • 14
    • 78449286213 scopus 로고    scopus 로고
    • Sortilin-mediated endocytosis determines levels of the frontotemporal dementia protein, progranulin
    • Hu F, Padukkavidana T, Vægter CB, Brady OA, Zheng Y, et al. (2010) Sortilin-mediated endocytosis determines levels of the frontotemporal dementia protein, progranulin. Neuron 68: 654-667.
    • (2010) Neuron , vol.68 , pp. 654-667
    • Hu, F.1    Padukkavidana, T.2    Vægter, C.B.3    Brady, O.A.4    Zheng, Y.5
  • 15
    • 78649796276 scopus 로고    scopus 로고
    • Genome-wide screen identifies rs646776 near sortilin as a regulator of progranulin levels in human plasma
    • Carrasquillo MM, Nicholson AM, Finch N, Gibbs JR, Baker M, et al. (2010) Genome-wide screen identifies rs646776 near sortilin as a regulator of progranulin levels in human plasma. Am J Hum Genet 87: 890-897.
    • (2010) Am J Hum Genet , vol.87 , pp. 890-897
    • Carrasquillo, M.M.1    Nicholson, A.M.2    Finch, N.3    Gibbs, J.R.4    Baker, M.5
  • 16
    • 0242320195 scopus 로고    scopus 로고
    • Progranulin (granulin-epithelin precursor, PC-cell-derived growth factor, acrogranin) mediates tissue repair and tumorigenesis
    • He Z, Bateman A, (2003) Progranulin (granulin-epithelin precursor, PC-cell-derived growth factor, acrogranin) mediates tissue repair and tumorigenesis. J Mol Med 81: 600-612.
    • (2003) J Mol Med , vol.81 , pp. 600-612
    • He, Z.1    Bateman, A.2
  • 18
    • 0042635680 scopus 로고    scopus 로고
    • Progranulin (acrogranin/PC cell-derived growth factor/granulin-epithelin precursor) is expressed in the placenta, epidermis, microvasculature, and brain during murine development
    • Daniel R, Daniels E, He Z, Bateman A, (2003) Progranulin (acrogranin/PC cell-derived growth factor/granulin-epithelin precursor) is expressed in the placenta, epidermis, microvasculature, and brain during murine development. Dev Dyn 227: 593-599.
    • (2003) Dev Dyn , vol.227 , pp. 593-599
    • Daniel, R.1    Daniels, E.2    He, Z.3    Bateman, A.4
  • 19
    • 35448929818 scopus 로고    scopus 로고
    • Alteration of behavioural phenotype in mice by targeted disruption of the progranulin gene
    • Kayasuga Y, Chiba S, Suzuki M, Kikusui T, Matsuwaki T, et al. (2007) Alteration of behavioural phenotype in mice by targeted disruption of the progranulin gene. Behav Brain Res 185: 110-118.
    • (2007) Behav Brain Res , vol.185 , pp. 110-118
    • Kayasuga, Y.1    Chiba, S.2    Suzuki, M.3    Kikusui, T.4    Matsuwaki, T.5
  • 20
    • 34447558236 scopus 로고    scopus 로고
    • ER chaperones in mammalian development and human diseases
    • Ni M, Amy S, Lee AS, (2007) ER chaperones in mammalian development and human diseases. FEBS Lett 581: 3641-3651.
    • (2007) FEBS Lett , vol.581 , pp. 3641-3651
    • Ni, M.1    Amy, S.2    Lee, A.S.3
  • 21
    • 0034194815 scopus 로고    scopus 로고
    • Pathways for protein disulphide bond formation
    • Frand AR, Cuozzo JW, Kaiser CA, (2000) Pathways for protein disulphide bond formation. Trends Cell Biol 10: 203-210.
    • (2000) Trends Cell Biol , vol.10 , pp. 203-210
    • Frand, A.R.1    Cuozzo, J.W.2    Kaiser, C.A.3
  • 22
    • 14044271131 scopus 로고    scopus 로고
    • The human protein disulphide isomerase family: substrate interactions and functional properties
    • Ellgaard L, Ruddock LW, (2005) The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep 6: 28-32.
    • (2005) EMBO Rep , vol.6 , pp. 28-32
    • Ellgaard, L.1    Ruddock, L.W.2
  • 23
    • 77953809347 scopus 로고    scopus 로고
    • ERp57, a multifunctional endoplasmic reticulum resident oxidoreductase
    • Coe H, Michalak M, (2010) ERp57, a multifunctional endoplasmic reticulum resident oxidoreductase. Int J Biochem Cell Biol 42: 796-799.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 796-799
    • Coe, H.1    Michalak, M.2
  • 24
    • 77953123663 scopus 로고    scopus 로고
    • Development and application of mass spectrometric methods for the analysis of progranulin N-glycosylation
    • Songsrirote K, Li Z, Ashford D, Bateman A, Thomas-Oates J, (2010) Development and application of mass spectrometric methods for the analysis of progranulin N-glycosylation. J Proteomics 73: 1479-1490.
    • (2010) J Proteomics , vol.73 , pp. 1479-1490
    • Songsrirote, K.1    Li, Z.2    Ashford, D.3    Bateman, A.4    Thomas-Oates, J.5
  • 25
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver JD, van der Wal FJ, Bulleid NJ, High S, (1997) Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 275: 86-88.
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    van der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 26
    • 0032482385 scopus 로고    scopus 로고
    • A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
    • Morrice NA, Powis SJ, (1998) A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules. Curr Biol 8: 713-716.
    • (1998) Curr Biol , vol.8 , pp. 713-716
    • Morrice, N.A.1    Powis, S.J.2
  • 27
    • 77956684691 scopus 로고    scopus 로고
    • Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins
    • Rutkevich LA, Cohen-Doyle MF, Brockmeier U, Williams DB, (2010) Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins. Mol Biol Cell 21: 3093-3105.
    • (2010) Mol Biol Cell , vol.21 , pp. 3093-3105
    • Rutkevich, L.A.1    Cohen-Doyle, M.F.2    Brockmeier, U.3    Williams, D.B.4
  • 28
    • 65149091065 scopus 로고    scopus 로고
    • Structure of the noncatalytic domains and global fold of the protein disulfide isomerase ERp72
    • Kozlov G, Maattanen P, Schrag JD, Hura GL, Gabrielli L, et al. (2009) Structure of the noncatalytic domains and global fold of the protein disulfide isomerase ERp72. Structure 17: 651-659.
    • (2009) Structure , vol.17 , pp. 651-659
    • Kozlov, G.1    Maattanen, P.2    Schrag, J.D.3    Hura, G.L.4    Gabrielli, L.5
  • 29
    • 77955320885 scopus 로고    scopus 로고
    • Structure of the catalytic a(0)a fragment of the protein disulfide isomerase ERp72
    • Kozlov G, Azeroual S, Rosenauer A, Määttänen P, Denisov AY, et al. (2010) Structure of the catalytic a(0)a fragment of the protein disulfide isomerase ERp72. J Mol Biol 401: 618-625.
    • (2010) J Mol Biol , vol.401 , pp. 618-625
    • Kozlov, G.1    Azeroual, S.2    Rosenauer, A.3    Määttänen, P.4    Denisov, A.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.