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Volumn 5, Issue OCT, 2014, Pages

Deletion of P58IPK, the cellular inhibitor of the protein kinases PKR and PERK, causes bone changes and joint degeneration in mice

Author keywords

Articular cartilage; Bone; Osteoarthritis; P58IPK; PERK; PKR

Indexed keywords

CYTOKINE; ENDOPLASMIC RETICULUM STRESS INDUCIBLE PROTEIN; PROTEIN KINASE; PROTEIN KINASE LIKE ENDOPLASMIC RETICULUM KINASE; PROTEIN KINASE R; TOLONIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 84934878152     PISSN: None     EISSN: 16642392     Source Type: Journal    
DOI: 10.3389/fendo.2014.00174     Document Type: Article
Times cited : (19)

References (64)
  • 1
    • 27244432788 scopus 로고    scopus 로고
    • The role of mechanical loading in the onset and progression of osteoarthritis
    • Griffin TM, Guilak F. The role of mechanical loading in the onset and progression of osteoarthritis. Exerc Sport Sci Rev (2005) 33:195-200. doi:10.1097/00003677-200510000-00008
    • (2005) Exerc Sport Sci Rev , vol.33 , pp. 195-200
    • Griffin, T.M.1    Guilak, F.2
  • 2
    • 52449113008 scopus 로고    scopus 로고
    • Why is obesity associated with osteoarthritis? Insights from mouse models of obesity
    • Griffin TM, Guilak F. Why is obesity associated with osteoarthritis? Insights from mouse models of obesity. Biorheology (2008) 45:387-98. doi:10.3233/BIR-2008-0485
    • (2008) Biorheology , vol.45 , pp. 387-398
    • Griffin, T.M.1    Guilak, F.2
  • 3
    • 4444244843 scopus 로고    scopus 로고
    • Does protein kinase R mediate TNF-alpha- and ceramide-induced increases in expression and activation of matrix metalloproteinases in articular cartilage by a novel mechanism?
    • Gilbert SJ, Duance VC, Mason DJ. Does protein kinase R mediate TNF-alpha- and ceramide-induced increases in expression and activation of matrix metalloproteinases in articular cartilage by a novel mechanism? Arthritis Res Ther (2004) 6:R46-55. doi:10.1186/ar1381
    • (2004) Arthritis Res Ther , vol.6 , pp. R46-R55
    • Gilbert, S.J.1    Duance, V.C.2    Mason, D.J.3
  • 4
    • 35348945870 scopus 로고    scopus 로고
    • Requirement for protein kinase R in interleukin-1alpha-stimulated effects in cartilage
    • Tam CL, Hofbauer M, Towle CA. Requirement for protein kinase R in interleukin-1alpha-stimulated effects in cartilage. Biochem Pharmacol (2007) 74:1636-41. doi:10.1016/j.bcp.2007.08.002
    • (2007) Biochem Pharmacol , vol.74 , pp. 1636-1641
    • Tam, C.L.1    Hofbauer, M.2    Towle, C.A.3
  • 5
    • 39149086750 scopus 로고    scopus 로고
    • Proteomic analysis of human osteoarthritic chondrocytes reveals protein changes in stress and glycolysis
    • Ruiz-Romero C, Carreira V, Rego I, Remeseiro S, Lopez-Armada MJ, Blanco FJ. Proteomic analysis of human osteoarthritic chondrocytes reveals protein changes in stress and glycolysis. Proteomics (2008) 8:495-507. doi:10.1002/pmic.200700249
    • (2008) Proteomics , vol.8 , pp. 495-507
    • Ruiz-Romero, C.1    Carreira, V.2    Rego, I.3    Remeseiro, S.4    Lopez-Armada, M.J.5    Blanco, F.J.6
  • 6
    • 70349908409 scopus 로고    scopus 로고
    • Advanced osteoarthritis in humans is associated with altered collagen VI expression and upregulation of ER-stress markers Grp78 and bag-1
    • Nugent AE, Speicher DM, Gradisar I, McBurney DL, Baraga A, Doane KJ, et al. Advanced osteoarthritis in humans is associated with altered collagen VI expression and upregulation of ER-stress markers Grp78 and bag-1. J Histochem Cytochem (2009) 57:923-31. doi:10.1369/jhc.2009.953893
    • (2009) J Histochem Cytochem , vol.57 , pp. 923-931
    • Nugent, A.E.1    Speicher, D.M.2    Gradisar, I.3    McBurney, D.L.4    Baraga, A.5    Doane, K.J.6
  • 7
    • 79959867275 scopus 로고    scopus 로고
    • Enhanced apoptotic and reduced protective response in chondrocytes following endoplasmic reticulum stress in osteoarthritic cartilage
    • Takada K, Hirose J, Senba K, Yamabe S, Oike Y, Gotoh T, et al. Enhanced apoptotic and reduced protective response in chondrocytes following endoplasmic reticulum stress in osteoarthritic cartilage. Int J Exp Pathol (2011) 92:232-42. doi:10.1111/j.1365-2613.2010.00758.x
    • (2011) Int J Exp Pathol , vol.92 , pp. 232-242
    • Takada, K.1    Hirose, J.2    Senba, K.3    Yamabe, S.4    Oike, Y.5    Gotoh, T.6
  • 8
    • 84863183489 scopus 로고    scopus 로고
    • Protein kinase R plays a pivotal role in oncostatin M and interleukin-1 signalling in bovine articular cartilage chondrocytes
    • Gilbert SJ, Blain EJ, Al-Sabah A, Zhang Y, Duance VC, Mason DJ. Protein kinase R plays a pivotal role in oncostatin M and interleukin-1 signalling in bovine articular cartilage chondrocytes. Eur Cell Mater (2012) 23:41-57.
    • (2012) Eur Cell Mater , vol.23 , pp. 41-57
    • Gilbert, S.J.1    Blain, E.J.2    Al-Sabah, A.3    Zhang, Y.4    Duance, V.C.5    Mason, D.J.6
  • 9
    • 84861755093 scopus 로고    scopus 로고
    • A novel pathogenic role of the ER chaperone GRP78/BiP in rheumatoid arthritis
    • Yoo SA, You S, Yoon HJ, Kim DH, Kim HS, Lee K, et al. A novel pathogenic role of the ER chaperone GRP78/BiP in rheumatoid arthritis. J Exp Med (2012) 209:871-86. doi:10.1084/jem.20111783
    • (2012) J Exp Med , vol.209 , pp. 871-886
    • Yoo, S.A.1    You, S.2    Yoon, H.J.3    Kim, D.H.4    Kim, H.S.5    Lee, K.6
  • 10
    • 33745922351 scopus 로고    scopus 로고
    • Protein kinase R: a novel mediator of articular cartilage degradation in arthritis
    • Gilbert SJ, Duance VC, Mason D. Protein kinase R: a novel mediator of articular cartilage degradation in arthritis. Curr Rheumatol Rev (2006) 2:9-21. doi:10.2174/157339706775697026
    • (2006) Curr Rheumatol Rev , vol.2 , pp. 9-21
    • Gilbert, S.J.1    Duance, V.C.2    Mason, D.3
  • 11
    • 0036863317 scopus 로고    scopus 로고
    • Tumour necrosis factor alpha up-regulates protein kinase R (PKR)-activating protein (PACT) and increases phosphorylation of PKR and eukaryotic initiation factor 2-alpha in articular chondrocytes
    • Gilbert SJ, Duance VC, Mason DJ. Tumour necrosis factor alpha up-regulates protein kinase R (PKR)-activating protein (PACT) and increases phosphorylation of PKR and eukaryotic initiation factor 2-alpha in articular chondrocytes. Biochem Soc Trans (2002) 30:886-9. doi:10.1042/BST0300886
    • (2002) Biochem Soc Trans , vol.30 , pp. 886-889
    • Gilbert, S.J.1    Duance, V.C.2    Mason, D.J.3
  • 12
    • 12244278071 scopus 로고    scopus 로고
    • Differential expression in early stages of osteoarthritis in vivo
    • Gilbert SJ, Duance VC, Mason DJ. Differential expression in early stages of osteoarthritis in vivo. J Bone Miner Res (1999) 14:1044.
    • (1999) J Bone Miner Res , vol.14 , pp. 1044
    • Gilbert, S.J.1    Duance, V.C.2    Mason, D.J.3
  • 13
    • 0036979333 scopus 로고    scopus 로고
    • Animal models of osteoarthritis in an era of molecular biology
    • Bendele AM. Animal models of osteoarthritis in an era of molecular biology. J Musculoskelet Neuronal Interact (2002) 2:501-3.
    • (2002) J Musculoskelet Neuronal Interact , vol.2 , pp. 501-503
    • Bendele, A.M.1
  • 14
    • 84857124537 scopus 로고    scopus 로고
    • Cyclic mechanical load causes global translational arrest in articular chondrocytes: a process which is partially dependent upon PKR phosphorylation
    • Lomas C, Tang XD, Chanalaris A, Saklatvala J, Vincent TL. Cyclic mechanical load causes global translational arrest in articular chondrocytes: a process which is partially dependent upon PKR phosphorylation. Eur Cell Mater (2011) 22:178-89.
    • (2011) Eur Cell Mater , vol.22 , pp. 178-189
    • Lomas, C.1    Tang, X.D.2    Chanalaris, A.3    Saklatvala, J.4    Vincent, T.L.5
  • 15
    • 0034643081 scopus 로고    scopus 로고
    • Tissue specific expression of PKR protein kinase in aging B6D2F1 mice
    • Ladiges W, Morton J, Blakely C, Gale M. Tissue specific expression of PKR protein kinase in aging B6D2F1 mice. Mech Ageing Dev (2000) 114:123-32. doi:10.1016/S0047-6374(00)00097-X
    • (2000) Mech Ageing Dev , vol.114 , pp. 123-132
    • Ladiges, W.1    Morton, J.2    Blakely, C.3    Gale, M.4
  • 16
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding HP, Zhang Y, Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature (1999) 397:271-4. doi:10.1038/16729
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 17
    • 0028938425 scopus 로고
    • Activation of the double-stranded RNA-regulated protein kinase by depletion of endoplasmic reticular calcium stores
    • Prostko CR, Dholakia JN, Brostrom MA, Brostrom CO. Activation of the double-stranded RNA-regulated protein kinase by depletion of endoplasmic reticular calcium stores. J Biol Chem (1995) 270:6211-5. doi:10.1074/jbc.270.11.6211
    • (1995) J Biol Chem , vol.270 , pp. 6211-6215
    • Prostko, C.R.1    Dholakia, J.N.2    Brostrom, M.A.3    Brostrom, C.O.4
  • 18
    • 34548124820 scopus 로고    scopus 로고
    • The double-strand RNA-dependent protein kinase PKR plays a significant role in a sustained ER stress-induced apoptosis
    • Lee ES, Yoon CH, Kim YS, Bae YS. The double-strand RNA-dependent protein kinase PKR plays a significant role in a sustained ER stress-induced apoptosis. FEBS Lett (2007) 581:4325-32. doi:10.1016/j.febslet.2007.08.001
    • (2007) FEBS Lett , vol.581 , pp. 4325-4332
    • Lee, E.S.1    Yoon, C.H.2    Kim, Y.S.3    Bae, Y.S.4
  • 19
    • 0036091476 scopus 로고    scopus 로고
    • The PERK eukaryotic initiation factor 2 alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas
    • Zhang P, McGrath B, Li S, Frank A, Zambito F, Reinert J, et al. The PERK eukaryotic initiation factor 2 alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas. Mol Cell Biol (2002) 22:3864-74. doi:10.1128/MCB.22.11.3864-3874.2002
    • (2002) Mol Cell Biol , vol.22 , pp. 3864-3874
    • Zhang, P.1    McGrath, B.2    Li, S.3    Frank, A.4    Zambito, F.5    Reinert, J.6
  • 20
    • 24744438696 scopus 로고    scopus 로고
    • Multiple signals induce endoplasmic reticulum stress in both primary and immortalized chondrocytes resulting in loss of differentiation, impaired cell growth, and apoptosis
    • Yang L, Carlson SG, McBurney D, Horton WE Jr. Multiple signals induce endoplasmic reticulum stress in both primary and immortalized chondrocytes resulting in loss of differentiation, impaired cell growth, and apoptosis. J Biol Chem (2005) 280:31156-65. doi:10.1074/jbc. M501069200
    • (2005) J Biol Chem , vol.280 , pp. 31156-31165
    • Yang, L.1    Carlson, S.G.2    McBurney, D.3    Horton, W.E.4
  • 21
    • 72449160579 scopus 로고    scopus 로고
    • The unfolded protein response and its relevance to connective tissue diseases
    • Boot-Handford RP, Briggs MD. The unfolded protein response and its relevance to connective tissue diseases. Cell Tissue Res (2010) 339:197-211. doi:10.1007/s00441-009-0877-8
    • (2010) Cell Tissue Res , vol.339 , pp. 197-211
    • Boot-Handford, R.P.1    Briggs, M.D.2
  • 22
    • 0029996422 scopus 로고    scopus 로고
    • Cloning, expression, and cellular localization of the oncogenic 58-kDa inhibitor of the RNA-activated human and mouse protein kinase
    • Korth MJ, Lyons CN, Wambach M, Katze MG. Cloning, expression, and cellular localization of the oncogenic 58-kDa inhibitor of the RNA-activated human and mouse protein kinase. Gene (1996) 170:181-8. doi:10.1016/0378-1119(95)00883-7
    • (1996) Gene , vol.170 , pp. 181-188
    • Korth, M.J.1    Lyons, C.N.2    Wambach, M.3    Katze, M.G.4
  • 24
    • 0038182518 scopus 로고    scopus 로고
    • IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2alpha signaling
    • IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2alpha signaling. J Biol Chem (2003) 278:15558-64. doi:10.1074/jbc. M212074200
    • (2003) J Biol Chem , vol.278 , pp. 15558-15564
    • van Huizen, R.1    Martindale, J.L.2    Gorospe, M.3    Holbrook, N.J.4
  • 26
    • 67249119884 scopus 로고    scopus 로고
    • P58(IPK): a novel "CIHD" member of the host innate defense response against pathogenic virus infection
    • Goodman AG, Fornek JL, Medigeshi GR, Perrone LA, Peng X, Dyer MD, et al. P58(IPK): a novel "CIHD" member of the host innate defense response against pathogenic virus infection. PLoS Pathog (2009) 5:e1000438. doi:10.1371/journal.ppat.1000438
    • (2009) PLoS Pathog , vol.5
    • Goodman, A.G.1    Fornek, J.L.2    Medigeshi, G.R.3    Perrone, L.A.4    Peng, X.5    Dyer, M.D.6
  • 27
    • 79551719155 scopus 로고    scopus 로고
    • Functional characterization of 58-kilodalton inhibitor of protein kinase in protecting against diabetic retinopathy via the endoplasmic reticulum stress pathway
    • Yang H, Liu R, Cui Z, Chen ZQ, Yan S, Pei H, et al. Functional characterization of 58-kilodalton inhibitor of protein kinase in protecting against diabetic retinopathy via the endoplasmic reticulum stress pathway. Mol Vis (2011) 17:78-84.
    • (2011) Mol Vis , vol.17 , pp. 78-84
    • Yang, H.1    Liu, R.2    Cui, Z.3    Chen, Z.Q.4    Yan, S.5    Pei, H.6
  • 28
    • 79251470769 scopus 로고    scopus 로고
    • Structural insight into the protective role of P58(IPK) during unfolded protein response
    • Tao J, Sha B. Structural insight into the protective role of P58(IPK) during unfolded protein response. Methods Enzymol (2011) 490:259-70. doi:10.1016/B978-0-12-385114-7.00015-5
    • (2011) Methods Enzymol , vol.490 , pp. 259-270
    • Tao, J.1    Sha, B.2
  • 30
    • 55549141494 scopus 로고    scopus 로고
    • Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3
    • Petrova K, Oyadomari S, Hendershot LM, Ron D. Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3. EMBO J (2008) 27:2862-72. doi:10.1038/emboj.2008.199
    • (2008) EMBO J , vol.27 , pp. 2862-2872
    • Petrova, K.1    Oyadomari, S.2    Hendershot, L.M.3    Ron, D.4
  • 31
    • 33747175431 scopus 로고    scopus 로고
    • Cotranslocational degradation protects the stressed endoplasmic reticulum from protein overload
    • Oyadomari S, Yun C, Fisher EA, Kreglinger N, Kreibich G, Oyadomari M, et al. Cotranslocational degradation protects the stressed endoplasmic reticulum from protein overload. Cell (2006) 126:727-39. doi:10.1016/j.cell.2006.06.051
    • (2006) Cell , vol.126 , pp. 727-739
    • Oyadomari, S.1    Yun, C.2    Fisher, E.A.3    Kreglinger, N.4    Kreibich, G.5    Oyadomari, M.6
  • 32
    • 0037117746 scopus 로고    scopus 로고
    • Inactivation of the PKR protein kinase and stimulation of mRNA translation by the cellular co-chaperone P58(IPK) does not require J domain function
    • Yan W, Gale MJ Jr, Tan SL, Katze MG. Inactivation of the PKR protein kinase and stimulation of mRNA translation by the cellular co-chaperone P58(IPK) does not require J domain function. Biochemistry (2002) 41:4938-45. doi:10.1021/bi0121499
    • (2002) Biochemistry , vol.41 , pp. 4938-4945
    • Yan, W.1    Gale, M.J.2    Tan, S.L.3    Katze, M.G.4
  • 33
    • 84918503361 scopus 로고    scopus 로고
    • AMPA/kainate glutamate receptors contribute to inflammation, degeneration and pain related behaviour in inflammatory stages of arthritis
    • Bonnet CS, Williams AS, Gilbert SJ, Harvey AK, Evans BA, Mason DJ. AMPA/kainate glutamate receptors contribute to inflammation, degeneration and pain related behaviour in inflammatory stages of arthritis. Ann Rheum Dis (2013). doi:10.1136/annrheumdis-2013-203670
    • (2013) Ann Rheum Dis
    • Bonnet, C.S.1    Williams, A.S.2    Gilbert, S.J.3    Harvey, A.K.4    Evans, B.A.5    Mason, D.J.6
  • 34
    • 77956924858 scopus 로고    scopus 로고
    • The OARSI histopathology initiative - recommendations for histological assessments of osteoarthritis in the mouse
    • Glasson SS, Chambers MG, van den Berg WB, Little CB. The OARSI histopathology initiative - recommendations for histological assessments of osteoarthritis in the mouse. Osteoarthritis Cartilage (2010) 18(Suppl 3):S17-23. doi:10.1016/j.joca.2010.05.025
    • (2010) Osteoarthritis Cartilage , vol.18 , pp. S17-S23
    • Glasson, S.S.1    Chambers, M.G.2    Van Den Berg, W.B.3    Little, C.B.4
  • 36
    • 84874395901 scopus 로고    scopus 로고
    • Male mice housed in groups engage in frequent fighting and show a lower response to additional bone loading than females or individually housed males that do not fight
    • Meakin LB, Sugiyama T, Galea GL, Browne WJ, Lanyon LE, Price JS. Male mice housed in groups engage in frequent fighting and show a lower response to additional bone loading than females or individually housed males that do not fight. Bone (2013) 54:113-7. doi:10.1016/j.bone.2013.01.029
    • (2013) Bone , vol.54 , pp. 113-117
    • Meakin, L.B.1    Sugiyama, T.2    Galea, G.L.3    Browne, W.J.4    Lanyon, L.E.5    Price, J.S.6
  • 38
    • 0017160321 scopus 로고
    • Suitability of C57 black mouse as an experimental animal for study of skeletal changes due to aging, with special reference to osteo-arthrosis and its response to tribenoside
    • Wilhelmi G, Faust R. Suitability of C57 black mouse as an experimental animal for study of skeletal changes due to aging, with special reference to osteo-arthrosis and its response to tribenoside. Pharmacology (1976) 14:289-96. doi:10.1159/000136607
    • (1976) Pharmacology , vol.14 , pp. 289-296
    • Wilhelmi, G.1    Faust, R.2
  • 39
    • 0033513065 scopus 로고    scopus 로고
    • Type II collagen degradation in spontaneous osteoarthritis in C57Bl/6 and BALB/c mice
    • Stoop R, van der Kraan PM, Buma P, Hollander AP, Billinghurst RC, Poole AR, et al. Type II collagen degradation in spontaneous osteoarthritis in C57Bl/6 and BALB/c mice. Arthritis Rheum (1999) 42:2381-9. doi:10.1002/1529-0131(199911)42:11<2381::AID-ANR17>3.0.CO;2-E
    • (1999) Arthritis Rheum , vol.42 , pp. 2381-2389
    • Stoop, R.1    Van Der Kraan, P.M.2    Buma, P.3    Hollander, A.P.4    Billinghurst, R.C.5    Poole, A.R.6
  • 40
    • 0035092322 scopus 로고    scopus 로고
    • Expression of type X collagen in young and old C57Bl/6 and Balb/c mice. Relation with articular cartilage degeneration
    • van der Kraan PM, Stoop R, Meijers TH, Poole AR, van den Berg WB. Expression of type X collagen in young and old C57Bl/6 and Balb/c mice. Relation with articular cartilage degeneration. Osteoarthritis Cartilage (2001) 9:92-100. doi:10.1053/joca.2000.0364
    • (2001) Osteoarthritis Cartilage , vol.9 , pp. 92-100
    • Van Der Kraan, P.M.1    Stoop, R.2    Meijers, T.H.3    Poole, A.R.4    Van Den Berg, W.B.5
  • 41
    • 0036048632 scopus 로고    scopus 로고
    • Transgenic mouse models for studying the role of cartilage macromolecules in osteoarthritis
    • Helminen HJ, Saamanen AM, Salminen H, Hyttinen MM. Transgenic mouse models for studying the role of cartilage macromolecules in osteoarthritis. Rheumatology (2002) 41:848-56. doi:10.1093/rheumatology/41.8.848
    • (2002) Rheumatology , vol.41 , pp. 848-856
    • Helminen, H.J.1    Saamanen, A.M.2    Salminen, H.3    Hyttinen, M.M.4
  • 42
    • 34848889931 scopus 로고    scopus 로고
    • The relationship between toe-out angle during gait and progression of medial tibiofemoral osteoarthritis
    • Chang A, Hurwitz D, Dunlop D, Song J, Cahue S, Hayes K, et al. The relationship between toe-out angle during gait and progression of medial tibiofemoral osteoarthritis. Ann Rheum Dis (2007) 66:1271-5. doi:10.1136/ard.2006.062927
    • (2007) Ann Rheum Dis , vol.66 , pp. 1271-1275
    • Chang, A.1    Hurwitz, D.2    Dunlop, D.3    Song, J.4    Cahue, S.5    Hayes, K.6
  • 43
    • 78650786038 scopus 로고    scopus 로고
    • Characterizing a novel and adjustable noninvasive murine joint loading model
    • Poulet B, Hamilton RW, Shefelbine S, Pitsillides AA. Characterizing a novel and adjustable noninvasive murine joint loading model. Arthritis Rheum (2011) 63:137-47. doi:10.1002/art.27765
    • (2011) Arthritis Rheum , vol.63 , pp. 137-147
    • Poulet, B.1    Hamilton, R.W.2    Shefelbine, S.3    Pitsillides, A.A.4
  • 44
    • 0024510729 scopus 로고
    • Correlation between alkaline and acid phosphatase activities and age-related osteopenia in murine vertebrae
    • Bar-Shira-Maymon B, Coleman R, Steinhagen-Thiessen E, Silbermann M. Correlation between alkaline and acid phosphatase activities and age-related osteopenia in murine vertebrae. Calcif Tissue Int (1989) 44:99-107. doi:10.1007/BF02556468
    • (1989) Calcif Tissue Int , vol.44 , pp. 99-107
    • Bar-Shira-Maymon, B.1    Coleman, R.2    Steinhagen-Thiessen, E.3    Silbermann, M.4
  • 45
    • 0031743918 scopus 로고    scopus 로고
    • Serum levels of insulin-like growth factor system components and relationship to bone metabolism in Type 1 and Type 2 diabetes mellitus patients
    • Jehle PM, Jehle DR, Mohan S, Bohm BO. Serum levels of insulin-like growth factor system components and relationship to bone metabolism in Type 1 and Type 2 diabetes mellitus patients. J Endocrinol (1998) 159:297-306. doi:10.1677/joe.0.1590297
    • (1998) J Endocrinol , vol.159 , pp. 297-306
    • Jehle, P.M.1    Jehle, D.R.2    Mohan, S.3    Bohm, B.O.4
  • 46
    • 0032977597 scopus 로고    scopus 로고
    • Bone mineral density in patients with type 1 and type 2 diabetes
    • Tuominen JT, Impivaara O, Puukka P, Ronnemaa T. Bone mineral density in patients with type 1 and type 2 diabetes. Diabetes Care (1999) 22:1196-200. doi:10.2337/diacare.22.7.1196
    • (1999) Diabetes Care , vol.22 , pp. 1196-1200
    • Tuominen, J.T.1    Impivaara, O.2    Puukka, P.3    Ronnemaa, T.4
  • 47
    • 54049133335 scopus 로고    scopus 로고
    • PERK is essential for neonatal skeletal development to regulate osteoblast proliferation and differentiation
    • Wei J, Sheng X, Feng D, McGrath B, Cavener DR. PERK is essential for neonatal skeletal development to regulate osteoblast proliferation and differentiation. J Cell Physiol (2008) 217:693-707. doi:10.1002/jcp.21543
    • (2008) J Cell Physiol , vol.217 , pp. 693-707
    • Wei, J.1    Sheng, X.2    Feng, D.3    McGrath, B.4    Cavener, D.R.5
  • 48
    • 27344438340 scopus 로고    scopus 로고
    • Double-stranded RNA-dependent protein kinase is required for bone calcification in MC3T3-E1 cells in vitro
    • Yoshida K, Okamura H, Amorim BR, Ozaki A, Tanaka H, Morimoto H, et al. Double-stranded RNA-dependent protein kinase is required for bone calcification in MC3T3-E1 cells in vitro. Exp Cell Res (2005) 311:117-25. doi:10.1016/j.yexcr.2005.09.006
    • (2005) Exp Cell Res , vol.311 , pp. 117-125
    • Yoshida, K.1    Okamura, H.2    Amorim, B.R.3    Ozaki, A.4    Tanaka, H.5    Morimoto, H.6
  • 49
    • 67349116079 scopus 로고    scopus 로고
    • PKR-mediated degradation of STAT1 regulates osteoblast differentiation
    • Yoshida K, Okamura H, Amorim BR, Hinode D, Yoshida H, Haneji T. PKR-mediated degradation of STAT1 regulates osteoblast differentiation. Exp Cell Res (2009) 315:2105-14. doi:10.1016/j.yexcr.2009.02.003
    • (2009) Exp Cell Res , vol.315 , pp. 2105-2114
    • Yoshida, K.1    Okamura, H.2    Amorim, B.R.3    Hinode, D.4    Yoshida, H.5    Haneji, T.6
  • 50
    • 84864327531 scopus 로고    scopus 로고
    • PKR plays a positive role in osteoblast differentiation by regulating GSK-3beta activity through a beta-catenin-independent pathway
    • Yoshida K, Okamura H, Ochiai K, Hoshino Y, Haneji T, Yoshioka M, et al. PKR plays a positive role in osteoblast differentiation by regulating GSK-3beta activity through a beta-catenin-independent pathway. Mol Cell Endocrinol (2012) 361(1-2):99-105. doi:10.1016/j.mce.2012.03.019
    • (2012) Mol Cell Endocrinol , vol.361 , Issue.1-2 , pp. 99-105
    • Yoshida, K.1    Okamura, H.2    Ochiai, K.3    Hoshino, Y.4    Haneji, T.5    Yoshioka, M.6
  • 51
    • 77958087289 scopus 로고    scopus 로고
    • Double stranded RNA-dependent protein kinase is involved in osteoclast differentiation of RAW264.7 cells in vitro
    • Teramachi J, Morimoto H, Baba R, Doi Y, Hirashima K, Haneji T. Double stranded RNA-dependent protein kinase is involved in osteoclast differentiation of RAW264.7 cells in vitro. Exp Cell Res (2010) 316:3254-62. doi:10.1016/j.yexcr.2010.08.006
    • (2010) Exp Cell Res , vol.316 , pp. 3254-3262
    • Teramachi, J.1    Morimoto, H.2    Baba, R.3    Doi, Y.4    Hirashima, K.5    Haneji, T.6
  • 52
    • 0031404079 scopus 로고    scopus 로고
    • Spontaneous osteoarthritis in Dunkin Hartley guinea pigs: histologic, radiologic, and biochemical changes
    • Jimenez PA, Glasson SS, Trubetskoy OV, Haimes HB. Spontaneous osteoarthritis in Dunkin Hartley guinea pigs: histologic, radiologic, and biochemical changes. Lab Anim Sci (1997) 47:598-601.
    • (1997) Lab Anim Sci , vol.47 , pp. 598-601
    • Jimenez, P.A.1    Glasson, S.S.2    Trubetskoy, O.V.3    Haimes, H.B.4
  • 53
    • 0017657685 scopus 로고
    • Degenerative joint disease in the mouse knee; histological observations
    • Walton M. Degenerative joint disease in the mouse knee; histological observations. J Pathol (1977) 123:109-22. doi:10.1002/path.1711230403
    • (1977) J Pathol , vol.123 , pp. 109-122
    • Walton, M.1
  • 54
    • 0017695588 scopus 로고
    • Degenerative joint disease in the mouse knee; radiological and morphological observations
    • Walton M. Degenerative joint disease in the mouse knee; radiological and morphological observations. J Pathol (1977) 123:97-107. doi:10.1002/path.1711230207
    • (1977) J Pathol , vol.123 , pp. 97-107
    • Walton, M.1
  • 55
    • 0028237468 scopus 로고
    • Chondro-osseous metaplasia, bone density and patellar cartilage proteoglycan content in the osteoarthritis of STR/ORT mice
    • Collins C, Evans RG, Ponsford F, Miller P, Elson CJ. Chondro-osseous metaplasia, bone density and patellar cartilage proteoglycan content in the osteoarthritis of STR/ORT mice. Osteoarthritis Cartilage (1994) 2:111-8. doi:10.1016/S1063-4584(05)80061-5
    • (1994) Osteoarthritis Cartilage , vol.2 , pp. 111-118
    • Collins, C.1    Evans, R.G.2    Ponsford, F.3    Miller, P.4    Elson, C.J.5
  • 57
    • 34548566958 scopus 로고    scopus 로고
    • The surgical destabilization of the medial meniscus (DMM) model of osteoarthritis in the 129/SvEv mouse
    • Glasson SS, Blanchet TJ, Morris EA. The surgical destabilization of the medial meniscus (DMM) model of osteoarthritis in the 129/SvEv mouse. Osteoarthritis Cartilage (2007) 15:1061-9. doi:10.1016/j.joca.2007.03.006
    • (2007) Osteoarthritis Cartilage , vol.15 , pp. 1061-1069
    • Glasson, S.S.1    Blanchet, T.J.2    Morris, E.A.3
  • 58
    • 84862125236 scopus 로고    scopus 로고
    • Musculoskeletal changes following non-invasive knee injury using a novel mouse model of post-traumatic osteoarthritis
    • Christiansen BA, Anderson MJ, Lee CA, Williams JC, Yik JH, Haudenschild DR. Musculoskeletal changes following non-invasive knee injury using a novel mouse model of post-traumatic osteoarthritis. Osteoarthritis Cartilage (2012) 20(7):773-82. doi:10.1016/j.joca.2012.04.014
    • (2012) Osteoarthritis Cartilage , vol.20 , Issue.7 , pp. 773-782
    • Christiansen, B.A.1    Anderson, M.J.2    Lee, C.A.3    Williams, J.C.4    Yik, J.H.5    Haudenschild, D.R.6
  • 59
    • 84890547397 scopus 로고    scopus 로고
    • Joint instability and cartilage compression in a mouse model of posttraumatic osteoarthritis
    • Onur TS, Wu R, Chu S, Chang W, Kim HT, Dang AB. Joint instability and cartilage compression in a mouse model of posttraumatic osteoarthritis. J Orthop Res (2014) 32:318-23. doi:10.1002/jor.22509
    • (2014) J Orthop Res , vol.32 , pp. 318-323
    • Onur, T.S.1    Wu, R.2    Chu, S.3    Chang, W.4    Kim, H.T.5    Dang, A.B.6
  • 62
    • 6444245091 scopus 로고    scopus 로고
    • The influence of ageing and exercise on tendon growth and degeneration - hypotheses for the initiation and prevention of strain-induced tendinopathies
    • Smith RK, Birch HL, Goodman S, Heinegard D, Goodship AE. The influence of ageing and exercise on tendon growth and degeneration - hypotheses for the initiation and prevention of strain-induced tendinopathies. Comp Biochem Physiol A Mol Integr Physiol (2002) 133:1039-50. doi:10.1016/S1095-6433(02)00148-4
    • (2002) Comp Biochem Physiol A Mol Integr Physiol , vol.133 , pp. 1039-1050
    • Smith, R.K.1    Birch, H.L.2    Goodman, S.3    Heinegard, D.4    Goodship, A.E.5
  • 63
    • 0036863317 scopus 로고    scopus 로고
    • Tumour necrosis factor alpha up-regulates protein kinase R (PKR)-activating protein (PACT) and increases phosphorylation of PKR and eukaryotic initiation factor 2-alpha in articular chondrocytes
    • Gilbert SJ, Duance VC, Mason DJ. Tumour necrosis factor alpha up-regulates protein kinase R (PKR)-activating protein (PACT) and increases phosphorylation of PKR and eukaryotic initiation factor 2-alpha in articular chondrocytes. Biochem Soc Trans (2001) 30:886-9. doi:10.1042/BST0300886
    • (2001) Biochem Soc Trans , vol.30 , pp. 886-889
    • Gilbert, S.J.1    Duance, V.C.2    Mason, D.J.3
  • 64
    • 8644224931 scopus 로고    scopus 로고
    • Resistance to vesicular stomatitis virus infection requires a functional cross talk between the eukaryotic translation initiation factor 2alpha kinases PERK and PKR
    • Baltzis D, Qu LK, Papadopoulou S, Blais JD, Bell JC, Sonenberg N, et al. Resistance to vesicular stomatitis virus infection requires a functional cross talk between the eukaryotic translation initiation factor 2alpha kinases PERK and PKR. J Virol (2004) 78:12747-61. doi:10.1128/JVI.78.23.12747-12761.2004
    • (2004) J Virol , vol.78 , pp. 12747-12761
    • Baltzis, D.1    Qu, L.K.2    Papadopoulou, S.3    Blais, J.D.4    Bell, J.C.5    Sonenberg, N.6


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