메뉴 건너뛰기




Volumn 401, Issue 2, 2010, Pages 192-196

Activation of the unfolded protein response by a cataract-associated αA-crystallin mutation

Author keywords

Cataract; Crystallin; Lens; Mutation; Unfolded protein response

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 6; ALPHA CRYSTALLIN;

EID: 77957802295     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.09.023     Document Type: Article
Times cited : (22)

References (33)
  • 1
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls
    • Kaufman R.J. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 1999, 13:1211-1233.
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 2
    • 33751159209 scopus 로고    scopus 로고
    • Intracellular signaling by the unfolded protein response
    • Bernales S., Papa F.R., Walter P. Intracellular signaling by the unfolded protein response. Annu. Rev. Cell Dev. Biol. 2006, 22:487-508.
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 487-508
    • Bernales, S.1    Papa, F.R.2    Walter, P.3
  • 4
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T., Zhu H., Morishima N., Li E., Xu J., Yankner B.A., Yuan J. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 2000, 403:98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 5
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai Y., Soda M., Inoue H., Hattori N., Mizuno Y., Takahashi R. An unfolded putative transmembrane polypeptide which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 2001, 105:891-902.
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 7
    • 72149134488 scopus 로고    scopus 로고
    • Abnormal expression of collagen IV in lens activates unfolded protein response resulting in cataract
    • Firtina Z., Danysh B.P., Bai X., Gould D.B., Kobayashi T., Duncan M.K. Abnormal expression of collagen IV in lens activates unfolded protein response resulting in cataract. J. Biol. Chem. 2009, 284:35872-35884.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35872-35884
    • Firtina, Z.1    Danysh, B.P.2    Bai, X.3    Gould, D.B.4    Kobayashi, T.5    Duncan, M.K.6
  • 8
    • 33745135040 scopus 로고    scopus 로고
    • Role of the unfolded protein response (UPR) in cataract formation
    • Ikesugi K., Yamamoto R., Mulhern M.L., Shinohara T. Role of the unfolded protein response (UPR) in cataract formation. Exp. Eye Res. 2006, 83:508-516.
    • (2006) Exp. Eye Res. , vol.83 , pp. 508-516
    • Ikesugi, K.1    Yamamoto, R.2    Mulhern, M.L.3    Shinohara, T.4
  • 10
    • 0031970686 scopus 로고    scopus 로고
    • Multifunctional lens crystallins and corneal enzymes. More than meets the eye
    • Piatigorsky J. Multifunctional lens crystallins and corneal enzymes. More than meets the eye. Ann. NY Acad. Sci. 1998, 842:7-15.
    • (1998) Ann. NY Acad. Sci. , vol.842 , pp. 7-15
    • Piatigorsky, J.1
  • 11
    • 33845425645 scopus 로고    scopus 로고
    • Crystallins in the eye: function and pathology
    • Andley U.P. Crystallins in the eye: function and pathology. Prog. Retin. Eye Res. 2007, 26:78-98.
    • (2007) Prog. Retin. Eye Res. , vol.26 , pp. 78-98
    • Andley, U.P.1
  • 12
    • 0242287938 scopus 로고    scopus 로고
    • Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q
    • Mackay D.S., Andley U.P., Shiels A. Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q. Eur. J. Hum. Genet. 2003, 11:784-793.
    • (2003) Eur. J. Hum. Genet. , vol.11 , pp. 784-793
    • Mackay, D.S.1    Andley, U.P.2    Shiels, A.3
  • 13
    • 0031934121 scopus 로고    scopus 로고
    • Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA
    • Litt M., Kramer P., LaMorticella D.M., Murphey W., Lovrien E.W., Weleber R.G. Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. Hum. Mol. Genet. 1998, 7:471-474.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 471-474
    • Litt, M.1    Kramer, P.2    LaMorticella, D.M.3    Murphey, W.4    Lovrien, E.W.5    Weleber, R.G.6
  • 15
    • 33750203700 scopus 로고    scopus 로고
    • Crystallins and hereditary cataracts: molecular mechanisms and potential for therapy
    • Andley U.P. Crystallins and hereditary cataracts: molecular mechanisms and potential for therapy. Expert Rev. Mol. Med. 2006, 8:1-19.
    • (2006) Expert Rev. Mol. Med. , vol.8 , pp. 1-19
    • Andley, U.P.1
  • 16
    • 77952784281 scopus 로고    scopus 로고
    • In vivo lens deficiency of the R49C alphaA-crystallin mutant
    • Andley U.P., Reilly M.A. In vivo lens deficiency of the R49C alphaA-crystallin mutant. Exp. Eye Res. 2010, 90:699-702.
    • (2010) Exp. Eye Res. , vol.90 , pp. 699-702
    • Andley, U.P.1    Reilly, M.A.2
  • 17
    • 51549106696 scopus 로고    scopus 로고
    • Mechanism of insolubilization by a single-point mutation in alphaA-crystallin linked with hereditary human cataracts
    • Andley U.P., Hamilton P.D., Ravi N. Mechanism of insolubilization by a single-point mutation in alphaA-crystallin linked with hereditary human cataracts. Biochemistry 2008, 47:9697-9706.
    • (2008) Biochemistry , vol.47 , pp. 9697-9706
    • Andley, U.P.1    Hamilton, P.D.2    Ravi, N.3
  • 18
    • 77955625793 scopus 로고    scopus 로고
    • Quantitative biometric phenotype analysis in mouse lenses
    • Reilly M.A., Andley U.P. Quantitative biometric phenotype analysis in mouse lenses. Mol. Vis. 2010, 16:1041-1046.
    • (2010) Mol. Vis. , vol.16 , pp. 1041-1046
    • Reilly, M.A.1    Andley, U.P.2
  • 19
    • 41949133095 scopus 로고    scopus 로고
    • Mechanism of small heat shock protein function in vivo: a knock-in mouse model demonstrates that the R49C mutation in alpha A-crystallin enhances protein insolubility and cell death
    • Xi J.H., Bai F., Gross J., Townsend R.R., Menko A.S., Andley U.P. Mechanism of small heat shock protein function in vivo: a knock-in mouse model demonstrates that the R49C mutation in alpha A-crystallin enhances protein insolubility and cell death. J. Biol. Chem. 2008, 283:5801-5814.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5801-5814
    • Xi, J.H.1    Bai, F.2    Gross, J.3    Townsend, R.R.4    Menko, A.S.5    Andley, U.P.6
  • 20
    • 69049101229 scopus 로고    scopus 로고
    • AlphaA-crystallin R49Cneo mutation influences the architecture of lens fiber cell membranes and causes posterior and nuclear cataracts in mice
    • Andley U.P. AlphaA-crystallin R49Cneo mutation influences the architecture of lens fiber cell membranes and causes posterior and nuclear cataracts in mice. BMC Ophthalmol. 2009, 9:4.
    • (2009) BMC Ophthalmol. , vol.9 , pp. 4
    • Andley, U.P.1
  • 21
    • 67650110001 scopus 로고    scopus 로고
    • Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforin
    • Vernia S., Rubio T., Heredia M., Rodriguez de Cordoba S., Sanz P. Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforin. PLoS ONE 2009, 4:e5907.
    • (2009) PLoS ONE , vol.4
    • Vernia, S.1    Rubio, T.2    Heredia, M.3    Rodriguez de Cordoba, S.4    Sanz, P.5
  • 22
    • 0032553123 scopus 로고    scopus 로고
    • The molecular chaperone alphaA-crystallin enhances lens epithelial cell growth and resistance to UVA stress
    • Andley U.P., Song Z., Wawrousek E.F., Bassnett S. The molecular chaperone alphaA-crystallin enhances lens epithelial cell growth and resistance to UVA stress. J. Biol. Chem. 1998, 273:31252-31261.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31252-31261
    • Andley, U.P.1    Song, Z.2    Wawrousek, E.F.3    Bassnett, S.4
  • 23
    • 0034711260 scopus 로고    scopus 로고
    • Differential protective activity of alpha A- and alphaB-crystallin in lens epithelial cells
    • Andley U.P., Song Z., Wawrousek E.F., Fleming T.P., Bassnett S. Differential protective activity of alpha A- and alphaB-crystallin in lens epithelial cells. J. Biol. Chem. 2000, 275:36823-36831.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36823-36831
    • Andley, U.P.1    Song, Z.2    Wawrousek, E.F.3    Fleming, T.P.4    Bassnett, S.5
  • 24
    • 1842843855 scopus 로고    scopus 로고
    • Roles of CHOP/GADD153 in endoplasmic reticulum stress
    • Oyadomari S., Mori M. Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ. 2004, 11:381-389.
    • (2004) Cell Death Differ. , vol.11 , pp. 381-389
    • Oyadomari, S.1    Mori, M.2
  • 26
    • 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., 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. 2003, 278:20915-20924.
    • (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
  • 27
    • 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., 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 2001, 107:881-891.
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 28
    • 0035877643 scopus 로고    scopus 로고
    • Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation
    • He C.H., Gong P., Hu B., Stewart D., Choi M.E., Choi A.M., Alam J. Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation. J. Biol. Chem. 2001, 276:20858-20865.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20858-20865
    • He, C.H.1    Gong, P.2    Hu, B.3    Stewart, D.4    Choi, M.E.5    Choi, A.M.6    Alam, J.7
  • 29
    • 0025878233 scopus 로고
    • Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity
    • Hai T., Curran T. Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity. Proc. Natl. Acad. Sci. USA 1991, 88:3720-3724.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3720-3724
    • Hai, T.1    Curran, T.2
  • 30
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding H.P., Zhang Y., Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 1999, 397:271-274.
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 32
    • 77649239734 scopus 로고    scopus 로고
    • Trimethylamine N-oxide alleviates the severe aggregation and ER stress caused by G98R alphaA-crystallin
    • Gong B., Zhang L.Y., Pang C.P., Lam D.S., Yam G.H. Trimethylamine N-oxide alleviates the severe aggregation and ER stress caused by G98R alphaA-crystallin. Mol. Vis. 2009, 15:2829-2840.
    • (2009) Mol. Vis. , vol.15 , pp. 2829-2840
    • Gong, B.1    Zhang, L.Y.2    Pang, C.P.3    Lam, D.S.4    Yam, G.H.5
  • 33
    • 6044255043 scopus 로고    scopus 로고
    • The physiological unfolded protein response in the thyroid epithelial cells
    • Sargsyan E., Baryshev M., Mkrtchian S. The physiological unfolded protein response in the thyroid epithelial cells. Biochem. Biophys. Res. Commun. 2004, 322:570-576.
    • (2004) Biochem. Biophys. Res. Commun. , vol.322 , pp. 570-576
    • Sargsyan, E.1    Baryshev, M.2    Mkrtchian, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.