메뉴 건너뛰기




Volumn 37, Issue 2, 2012, Pages 244-252

Protection against protein aggregation by alpha-crystallin as a mechanism of preconditioning

Author keywords

Alpha crystallin; Ethanol; Heat shock proteins; Preconditioning; Protein aggregation

Indexed keywords

ALCOHOL; ALPHA CRYSTALLIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE;

EID: 84856406148     PISSN: 03643190     EISSN: 15736903     Source Type: Journal    
DOI: 10.1007/s11064-011-0601-4     Document Type: Article
Times cited : (6)

References (39)
  • 1
    • 33846159435 scopus 로고    scopus 로고
    • Ischaemic preconditioning of the brain, mechanisms and applications
    • DOI 10.1007/s00701-006-1057-1
    • Steiger HJ, Hanggi D (2007) Ischaemic preconditioning of the brain, mechanisms and applications. Acta Neurochir (Wien) 149:1-10 (Pubitemid 46090183)
    • (2007) Acta Neurochirurgica , vol.149 , Issue.1 , pp. 1-10
    • Steiger, H.-J.1    Hanggi, D.2
  • 3
    • 79960844952 scopus 로고    scopus 로고
    • Isoflurane preconditioning involves upregulation of molecular chaperone genes
    • 21741358 10.1016/j.bbrc.2011.06.156 1:CAS:528:DC%2BC3MXps1ars7Y%3D
    • McClintick CA, Theisen CS, Ferns JE et al (2011) Isoflurane preconditioning involves upregulation of molecular chaperone genes. Biochem Biophys Res Commun 411:387-392
    • (2011) Biochem Biophys Res Commun , vol.411 , pp. 387-392
    • McClintick, C.A.1    Theisen, C.S.2    Ferns, J.E.3
  • 4
    • 77952958379 scopus 로고    scopus 로고
    • Isoflurane's effect on interfacial dynamics in GAPDH influences methylglyoxal reactivity
    • 20371360 10.1016/j.abb.2010.04.001 1:CAS:528:DC%2BC3cXmsVCqt7c%3D
    • Pattin AE, Ochs S, Theisen CS et al (2010) Isoflurane's effect on interfacial dynamics in GAPDH influences methylglyoxal reactivity. Arch Biochem Biophys 498:7-12
    • (2010) Arch Biochem Biophys , vol.498 , pp. 7-12
    • Pattin, A.E.1    Ochs, S.2    Theisen, C.S.3
  • 5
    • 80052724540 scopus 로고    scopus 로고
    • Inhaled anesthetics promote albumin dimerization through reciprocal exchange of subdomains
    • Pieters BJ, Fibuch EE, Eklund JD et al (2010) Inhaled anesthetics promote albumin dimerization through reciprocal exchange of subdomains. Biochem Res Int 2010:516704
    • (2010) Biochem Res Int 2010 , pp. 516-704
    • Pieters, B.J.1    Fibuch, E.E.2    Eklund, J.D.3
  • 6
    • 0023917935 scopus 로고
    • Lens crystallins: The evolution and expression of proteins for a highly specialized tissue
    • 3052280 10.1146/annurev.bi.57.070188.002403 1:CAS:528:DyaL1cXkvVOjt78%3D
    • Wistow GJ, Piatigorsky J (1988) Lens crystallins: the evolution and expression of proteins for a highly specialized tissue. Annu Rev Biochem 57:479-504
    • (1988) Annu Rev Biochem , vol.57 , pp. 479-504
    • Wistow, G.J.1    Piatigorsky, J.2
  • 8
    • 77955920499 scopus 로고    scopus 로고
    • In vitro renaturation of alkaline family G/11 xylanase via a folding intermediate: Alpha-crystallin facilitates refolding in an ATP-independent manner
    • 20703955 10.1007/s12010-009-8854-y 1:CAS:528:DC%2BC3cXhtFensrbK
    • Dutta T, Bhattacharjee A, Majumdar U et al (2010) In vitro renaturation of alkaline family G/11 xylanase via a folding intermediate: alpha-crystallin facilitates refolding in an ATP-independent manner. Appl Biochem Biotechnol 162:1238-1248
    • (2010) Appl Biochem Biotechnol , vol.162 , pp. 1238-1248
    • Dutta, T.1    Bhattacharjee, A.2    Majumdar, U.3
  • 9
    • 77953799932 scopus 로고    scopus 로고
    • Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation
    • 20484674 10.1073/pnas.0914773107 1:CAS:528:DC%2BC3cXnvV2isL4%3D
    • Robertson AL, Headey SJ, Saunders HM et al (2010) Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation. Proc Natl Acad Sci USA 107:10424-10429
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 10424-10429
    • Robertson, A.L.1    Headey, S.J.2    Saunders, H.M.3
  • 10
    • 0034141214 scopus 로고    scopus 로고
    • α-Crystallin assists the renaturation of glyceraldehyde-3-phosphate dehydrogenase
    • DOI 10.1042/0264-6021:3450467
    • Ganea E, Harding JJ (2000) Alpha-crystallin assists the renaturation of glyceraldehyde-3-phosphate dehydrogenase. Biochem J 345(Pt 3):467-472 (Pubitemid 30099074)
    • (2000) Biochemical Journal , vol.345 , Issue.3 , pp. 467-472
    • Ganea, E.1    Harding, J.J.2
  • 11
    • 77953360838 scopus 로고    scopus 로고
    • Hydration water/interfacial water in crystalline lens
    • 20412792 10.1016/j.exer.2010.04.005 1:CAS:528:DC%2BC3cXmslCjsrc%3D
    • Tompa K, Banki P, Bokor M et al (2010) Hydration water/interfacial water in crystalline lens. Exp Eye Res 91:76-84
    • (2010) Exp Eye Res , vol.91 , pp. 76-84
    • Tompa, K.1    Banki, P.2    Bokor, M.3
  • 12
    • 0348162674 scopus 로고    scopus 로고
    • Hydration properties of the molecular chaperone alpha-crystallin in the bovine lens
    • 10.1023/A:1026366830476 1:CAS:528:DC%2BD3sXosFWqu74%3D
    • Babizhayev MA, Nikolayev GM, Goryachev SN et al (2003) Hydration properties of the molecular chaperone alpha-crystallin in the bovine lens. Biochemistry (Mosc) 68:1145-1155
    • (2003) Biochemistry (Mosc) , vol.68 , pp. 1145-1155
    • Babizhayev, M.A.1    Nikolayev, G.M.2    Goryachev, S.N.3
  • 13
    • 77955664570 scopus 로고    scopus 로고
    • Stress response in tardigrades: Differential gene expression of molecular chaperones
    • 19943197 10.1007/s12192-009-0158-1 1:CAS:528:DC%2BC3cXntlKqurk%3D
    • Reuner A, Hengherr S, Mali B et al (2010) Stress response in tardigrades: differential gene expression of molecular chaperones. Cell Stress Chaperones 15:423-430
    • (2010) Cell Stress Chaperones , vol.15 , pp. 423-430
    • Reuner, A.1    Hengherr, S.2    Mali, B.3
  • 14
    • 78149247967 scopus 로고    scopus 로고
    • Identification of anhydrobiosis-related genes from an expressed sequence tag database in the cryptobiotic midge Polypedilum vanderplanki (Diptera; Chironomidae)
    • 20833722 10.1074/jbc.M110.150623 1:CAS:528:DC%2BC3cXhtlyntb7M
    • Cornette R, Kanamori Y, Watanabe M et al (2010) Identification of anhydrobiosis-related genes from an expressed sequence tag database in the cryptobiotic midge Polypedilum vanderplanki (Diptera; Chironomidae). J Biol Chem 285:35889-35899
    • (2010) J Biol Chem , vol.285 , pp. 35889-35899
    • Cornette, R.1    Kanamori, Y.2    Watanabe, M.3
  • 15
    • 0035960080 scopus 로고    scopus 로고
    • A trimeric protein complex functions as a synaptic chaperone machine
    • DOI 10.1016/S0896-6273(01)00427-5
    • Tobaben S, Thakur P, Fernandez-Chacon R et al (2001) A trimeric protein complex functions as a synaptic chaperone machine. Neuron 31:987-999 (Pubitemid 32925284)
    • (2001) Neuron , vol.31 , Issue.6 , pp. 987-999
    • Tobaben, S.1    Thakur, P.2    Fernandez-Chacon, R.3    Sudhof, T.C.4    Rettig, J.5    Stahl, B.6
  • 16
    • 0032894467 scopus 로고    scopus 로고
    • Molecular simulation of the effects of alcohols on peptide structure
    • DOI 10.1002/(SICI)1097-0282(199906) 49:7<635::AID-BIP8>3.0.CO;2-8
    • Dwyer DS (1999) Molecular simulation of the effects of alcohols on peptide structure. Biopolymers 49:635-645 (Pubitemid 29198159)
    • (1999) Biopolymers , vol.49 , Issue.7 , pp. 635-645
    • Dwyer, D.S.1
  • 17
    • 0034306109 scopus 로고    scopus 로고
    • Effect of human neuronal tau on denaturation and reactivation of rabbit muscle d-glyceraldehyde-3-phosphate dehydrogenase
    • 10998366 10.1042/0264-6021:3510233 1:CAS:528:DC%2BD3cXnslWltL0%3D
    • Chen YH, He RQ, Liu Y et al (2000) Effect of human neuronal tau on denaturation and reactivation of rabbit muscle d-glyceraldehyde-3-phosphate dehydrogenase. Biochem J 351:233-240
    • (2000) Biochem J , vol.351 , pp. 233-240
    • Chen, Y.H.1    He, R.Q.2    Liu, Y.3
  • 19
    • 0020676139 scopus 로고
    • Permeability of human red cells to a homologous series of aliphatic alcohols. Limitations of the continuous flow-tube method
    • DOI 10.1085/jgp.81.2.283
    • Brahm J (1983) Permeability of human red cells to a homologous series of aliphatic alcohols. Limitations of the continuous flow-tube method. J Gen Physiol 81:283-304 (Pubitemid 13157442)
    • (1983) Journal of General Physiology , vol.81 , Issue.2 , pp. 283-304
    • Brahm, J.1
  • 20
    • 0030069832 scopus 로고    scopus 로고
    • The early and late phases of preconditioning against myocardial stunning and the essential role of oxyradicals in the late phase: An overview
    • 8660262 10.1007/BF00795364 1:CAS:528:DyaK28Xitlags7s%3D
    • Bolli R (1996) The early and late phases of preconditioning against myocardial stunning and the essential role of oxyradicals in the late phase: an overview. Basic Res Cardiol 91:57-63
    • (1996) Basic Res Cardiol , vol.91 , pp. 57-63
    • Bolli, R.1
  • 21
    • 39149135555 scopus 로고    scopus 로고
    • Differential binding of mutant (R116C) and wildtype alphaA crystallin to actin
    • DOI 10.1080/02713680701769989, PII 788619550
    • Brown Z, Ponce A, Lampi K et al (2007) Differential binding of mutant (R116C) and wildtype alphaA crystallin to actin. Curr Eye Res 32:1051-1054 (Pubitemid 351412297)
    • (2007) Current Eye Research , vol.32 , Issue.12 , pp. 1051-1054
    • Brown, Z.1    Ponce, A.2    Lampi, K.3    Hancock, L.4    Takemoto, L.5
  • 23
    • 0036195722 scopus 로고    scopus 로고
    • α-Crystallin-type heat shock proteins: Socializing minichaperones in the context of a multichaperone network
    • DOI 10.1128/MMBR.66.1.64-93.2002
    • Narberhaus F (2002) Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Microbiol Mol Biol Rev 66:64-93 table of contents (Pubitemid 34213969)
    • (2002) Microbiology and Molecular Biology Reviews , vol.66 , Issue.1 , pp. 64-93
    • Narberhaus, F.1
  • 24
    • 0029876328 scopus 로고    scopus 로고
    • AlphaB-crystallin protects glial cells from hypertonic stress
    • 8638673 1:CAS:528:DyaK28XitVajt74%3D
    • Kegel KB, Iwaki A, Iwaki T et al (1996) AlphaB-crystallin protects glial cells from hypertonic stress. Am J Physiol 270:C903-C909
    • (1996) Am J Physiol , vol.270
    • Kegel, K.B.1    Iwaki, A.2    Iwaki, T.3
  • 25
    • 0029932037 scopus 로고    scopus 로고
    • Prevention of the fructation-induced inactivation of glutathione reductase by bovine alpha-crystallin acting as a molecular chaperone
    • 8727959 10.1159/000267938 1:CAS:528:DyaK28XivVKitbw%3D
    • Blakytny R, Harding JJ (1996) Prevention of the fructation-induced inactivation of glutathione reductase by bovine alpha-crystallin acting as a molecular chaperone. Ophthalmic Res 28(Suppl 1):19-22
    • (1996) Ophthalmic Res , vol.28 , Issue.SUPPL. 1 , pp. 19-22
    • Blakytny, R.1    Harding, J.J.2
  • 26
    • 55549104358 scopus 로고    scopus 로고
    • Trifluoroethanol increases albumin's susceptibility to chemical modification
    • 18831959 10.1016/j.abb.2008.09.009 1:CAS:528:DC%2BD1cXhtlGhu7%2FL
    • Craig HD, Eklund JD, Seidler NW (2008) Trifluoroethanol increases albumin's susceptibility to chemical modification. Arch Biochem Biophys 480:11-16
    • (2008) Arch Biochem Biophys , vol.480 , pp. 11-16
    • Craig, H.D.1    Eklund, J.D.2    Seidler, N.W.3
  • 27
    • 56449130948 scopus 로고    scopus 로고
    • Volatile anesthetic binding to proteins is influenced by solvent and aliphatic residues
    • 18808106 10.1021/ci800206a 1:CAS:528:DC%2BD1cXhtFChtr%2FK
    • Streiff JH, Jones KA (2008) Volatile anesthetic binding to proteins is influenced by solvent and aliphatic residues. J Chem Inf Model 48:2066-2073
    • (2008) J Chem Inf Model , vol.48 , pp. 2066-2073
    • Streiff, J.H.1    Jones, K.A.2
  • 28
    • 0034064407 scopus 로고    scopus 로고
    • Chemical properties of alcohols and their protein binding sites
    • Dwyer DS, Bradley RJ (2000) Chemical properties of alcohols and their protein binding sites. Cell Mol Life Sci 57:265-275 (Pubitemid 30311414)
    • (2000) Cellular and Molecular Life Sciences , vol.57 , Issue.2 , pp. 265-275
    • Dwyer, D.S.1    Bradley, R.J.2
  • 29
    • 0025361799 scopus 로고
    • Dehydration: A new alcohol theory
    • DOI 10.1016/0741-8329(90)90060-P
    • Klemm WR (1990) Dehydration: a new alcohol theory. Alcohol 7:49-59 (Pubitemid 20090079)
    • (1990) Alcohol , vol.7 , Issue.1 , pp. 49-59
    • Klemm, W.R.1
  • 30
    • 77952892044 scopus 로고    scopus 로고
    • Polyol additives modulate the in vitro stability and activity of recombinant human phenylalanine hydroxylase
    • 19937396 10.1007/s12010-009-8862-y 1:CAS:528:DC%2BC3cXlsVaiurs%3D
    • Nascimento C, Leandro J, Lino PR et al (2010) Polyol additives modulate the in vitro stability and activity of recombinant human phenylalanine hydroxylase. Appl Biochem Biotechnol 162:192-207
    • (2010) Appl Biochem Biotechnol , vol.162 , pp. 192-207
    • Nascimento, C.1    Leandro, J.2    Lino, P.R.3
  • 31
    • 79955975933 scopus 로고    scopus 로고
    • Cavity hydration as a gateway to unfolding: An NMR study of hen lysozyme at high pressure and low temperature
    • 21367514 10.1016/j.bpc.2011.01.009 1:CAS:528:DC%2BC3MXmtFehtrk%3D
    • Kamatari YO, Smith LJ, Dobson CM et al (2011) Cavity hydration as a gateway to unfolding: an NMR study of hen lysozyme at high pressure and low temperature. Biophys Chem 156:24-30
    • (2011) Biophys Chem , vol.156 , pp. 24-30
    • Kamatari, Y.O.1    Smith, L.J.2    Dobson, C.M.3
  • 32
    • 0016808917 scopus 로고
    • A statistical analysis of the relationship between degradative rates and molecular weights of proteins
    • 1164028 10.1016/0003-9861(75)90112-5 1:CAS:528:DyaE2MXlt1Ors7w%3D
    • Dice JF, Goldberg AL (1975) A statistical analysis of the relationship between degradative rates and molecular weights of proteins. Arch Biochem Biophys 170:213-219
    • (1975) Arch Biochem Biophys , vol.170 , pp. 213-219
    • Dice, J.F.1    Goldberg, A.L.2
  • 33
    • 78751673139 scopus 로고    scopus 로고
    • X-ray structures of general anaesthetics bound to a pentameric ligand-gated ion channel
    • 21248852 10.1038/nature09647 1:CAS:528:DC%2BC3MXnvVOgtg%3D%3D
    • Nury H, Van Renterghem C, Weng Y et al (2011) X-ray structures of general anaesthetics bound to a pentameric ligand-gated ion channel. Nature 469:428-431
    • (2011) Nature , vol.469 , pp. 428-431
    • Nury, H.1    Van Renterghem, C.2    Weng, Y.3
  • 34
    • 79959226194 scopus 로고    scopus 로고
    • On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: Biochemical mechanisms and regulatory control
    • 21640161 10.1016/j.bbagen.2011.05.010 1:CAS:528:DC%2BC3MXosVCktbs%3D
    • Sirover MA (2011) On the functional diversity of glyceraldehyde-3- phosphate dehydrogenase: biochemical mechanisms and regulatory control. Biochim Biophys Acta 1810:741-751
    • (2011) Biochim Biophys Acta , vol.1810 , pp. 741-751
    • Sirover, M.A.1
  • 35
    • 77956315573 scopus 로고    scopus 로고
    • Cysteine-string protein's neuroprotective role
    • 20583963 10.3109/01677063.2010.489625 1:CAS:528:DC%2BC3cXhtV2qsrzO
    • Zinsmaier KE (2010) Cysteine-string protein's neuroprotective role. J Neurogenet 24:120-132
    • (2010) J Neurogenet , vol.24 , pp. 120-132
    • Zinsmaier, K.E.1
  • 36
    • 0037101915 scopus 로고    scopus 로고
    • Relationship between intracellular ionic strength and expression of tonicity-responsive genes in rat papillary collecting duct cells
    • DOI 10.1113/jphysiol.2002.021931
    • Neuhofer W, Bartels H, Fraek ML et al (2002) Relationship between intracellular ionic strength and expression of tonicity-responsive genes in rat papillary collecting duct cells. J Physiol 543:147-153 (Pubitemid 34947302)
    • (2002) Journal of Physiology , vol.543 , Issue.1 , pp. 147-153
    • Neuhofer, W.1    Bartels, H.2    Fraek, M.-L.3    Beck, F.-X.4
  • 37
    • 0031934121 scopus 로고    scopus 로고
    • Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA
    • DOI 10.1093/hmg/7.3.471
    • Litt M, Kramer P, LaMorticella DM et al (1998) Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. Hum Mol Genet 7:471-474 (Pubitemid 28120638)
    • (1998) Human Molecular Genetics , vol.7 , Issue.3 , pp. 471-474
    • Litt, M.1    Kramer, P.2    LaMorticella, D.M.3    Murphey, W.4    Lovrien, E.W.5    Weleber, R.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.