메뉴 건너뛰기




Volumn 91, Issue 6, 2010, Pages 515-521

αB-crystallin (HspB5) in familial amyloidotic polyneuropathy

Author keywords

Amyloid; Crystallin; Heat shock response; Transthyretin

Indexed keywords

ALPHA CRYSTALLIN; ALPHAB CRYSTALLIN; PREALBUMIN; UNCLASSIFIED DRUG;

EID: 78649515958     PISSN: 09599673     EISSN: 13652613     Source Type: Journal    
DOI: 10.1111/j.1365-2613.2010.00735.x     Document Type: Article
Times cited : (14)

References (35)
  • 1
    • 77957180065 scopus 로고
    • A peculiar form of peripheral neuropathy. Familial atypical generalized amyloidosis with special involvement of the peripheral nerves
    • Andrade C. (1952) A peculiar form of peripheral neuropathy. Familial atypical generalized amyloidosis with special involvement of the peripheral nerves. Brain 75, 408-427.
    • (1952) Brain , vol.75 , pp. 408-427
    • Andrade, C.1
  • 2
    • 42449091462 scopus 로고    scopus 로고
    • Small heat shock proteins Hsp27 or αB-crystallin and the protein components of neurofibrillary tangles: tau and neurofilaments
    • Björkdahl C., Sjögren M.J., Zhou X. et al. (2008) Small heat shock proteins Hsp27 or αB-crystallin and the protein components of neurofibrillary tangles: tau and neurofilaments. J. Neurosci. Res. 86, 1343-1352.
    • (2008) J. Neurosci. Res. , vol.86 , pp. 1343-1352
    • Björkdahl, C.1    Sjögren, M.J.2    Zhou, X.3
  • 3
    • 0036295080 scopus 로고    scopus 로고
    • Transthyretin fibrillogenesis entails the assembly of monomers: a molecular model for in vitro assembled transthyretin amyloid-like fibrils
    • Cardoso I., Goldsbury C.S., Müller S.A. et al. (2002) Transthyretin fibrillogenesis entails the assembly of monomers: a molecular model for in vitro assembled transthyretin amyloid-like fibrils. J. Mol. Biol. 317, 683-695.
    • (2002) J. Mol. Biol. , vol.317 , pp. 683-695
    • Cardoso, I.1    Goldsbury, C.S.2    Müller, S.A.3
  • 4
    • 0010551538 scopus 로고
    • Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy
    • Costa P.P., Figueira A.S., Bravo F.R. (1978) Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy. Proc. Natl. Acad. Sci. U S A 75, 4499-4503.
    • (1978) Proc. Natl. Acad. Sci. U S A , vol.75 , pp. 4499-4503
    • Costa, P.P.1    Figueira, A.S.2    Bravo, F.R.3
  • 5
    • 58149506229 scopus 로고    scopus 로고
    • Crystallin proteins and amyloid fibrils
    • Ecroyd H., Carver J. (2009) Crystallin proteins and amyloid fibrils. Cell. Mol. Life Sci. 66, 62-81.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 62-81
    • Ecroyd, H.1    Carver, J.2
  • 6
    • 33846278382 scopus 로고    scopus 로고
    • Mimicking phosphorylation of αB-crystallin affects its chaperone activity
    • Ecroyd H., Meehan S., Horwitz J. et al. (2007) Mimicking phosphorylation of αB-crystallin affects its chaperone activity. Biochem. J. 401, 129-141.
    • (2007) Biochem. J. , vol.401 , pp. 129-141
    • Ecroyd, H.1    Meehan, S.2    Horwitz, J.3
  • 8
    • 0025825160 scopus 로고
    • Production of recombinant human transthyretin with biological activities toward the understanding of the molecular basis of familial amyloidotic polyneuropathy (FAP)
    • Furuya H., Saraiva M.J., Gawinowicz M.A. et al. (1991) Production of recombinant human transthyretin with biological activities toward the understanding of the molecular basis of familial amyloidotic polyneuropathy (FAP). Biochemistry 30, 2415-2421.
    • (1991) Biochemistry , vol.30 , pp. 2415-2421
    • Furuya, H.1    Saraiva, M.J.2    Gawinowicz, M.A.3
  • 9
    • 40149107721 scopus 로고    scopus 로고
    • Interactive sequences in the molecular chaperone, human αb crystallin modulate the fibrillation of amyloidogenic proteins
    • Ghosh J.G., Houck S.A., Clark J.I. (2008) Interactive sequences in the molecular chaperone, human αb crystallin modulate the fibrillation of amyloidogenic proteins. Int. J. Biochem. Cell Biol. 40, 954-967.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 954-967
    • Ghosh, J.G.1    Houck, S.A.2    Clark, J.I.3
  • 10
    • 0027198862 scopus 로고
    • Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases
    • Henzel W.J., Billeci T.M., Stults J.T., Wond S.C., Grimley C., Watanabe C. (1993) Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc. Natl. Acad. Sci. U S A 90, 5011-5015.
    • (1993) Proc. Natl. Acad. Sci. U S A , vol.90 , pp. 5011-5015
    • Henzel, W.J.1    Billeci, T.M.2    Stults, J.T.3    Wond, S.C.4    Grimley, C.5    Watanabe, C.6
  • 11
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob U., Gaestel M., Engel K., Buchner J. (1993) Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268, 1517-1520.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 12
    • 20144374696 scopus 로고    scopus 로고
    • The small heat shock protein αB-crystallin is a novel inhibitor of TRAIL-induced apoptosis that suppresses the activation of caspase-3
    • Kamradt M.C., Lu M., Werner M.E. et al. (2005) The small heat shock protein αB-crystallin is a novel inhibitor of TRAIL-induced apoptosis that suppresses the activation of caspase-3. J. Biol. Chem. 280, 11059-11066.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11059-11066
    • Kamradt, M.C.1    Lu, M.2    Werner, M.E.3
  • 13
    • 0028041578 scopus 로고
    • Determination of amyloid type by ELISA using milligram amounts of tissue
    • Kaplan B., German G., Ravid M., Pras M. (1994) Determination of amyloid type by ELISA using milligram amounts of tissue. Clin. Chim. Acta 229, 171-179.
    • (1994) Clin. Chim. Acta , vol.229 , pp. 171-179
    • Kaplan, B.1    German, G.2    Ravid, M.3    Pras, M.4
  • 15
    • 0030971508 scopus 로고    scopus 로고
    • Analysis of amyloid deposition in a transgenic mouse model of homozygous familial amyloidotic polyneuropathy
    • Kohno K., Palha J.A., Miyakawa K. et al. (1997) Analysis of amyloid deposition in a transgenic mouse model of homozygous familial amyloidotic polyneuropathy. Am. J. Pathol. 150, 1497-1508.
    • (1997) Am. J. Pathol. , vol.150 , pp. 1497-1508
    • Kohno, K.1    Palha, J.A.2    Miyakawa, K.3
  • 16
    • 33846297971 scopus 로고    scopus 로고
    • Small heat shock protein AlphaB-crystallin binds to p53 to sequester its translocation to mitochondria during hydrogen peroxide-induced apoptosis
    • Liu S., Li J., Tao Y., Xiao X. (2007) Small heat shock protein AlphaB-crystallin binds to p53 to sequester its translocation to mitochondria during hydrogen peroxide-induced apoptosis. Biochem. Biophys. Res. Commun. 354, 109-114.
    • (2007) Biochem. Biophys. Res. Commun. , vol.354 , pp. 109-114
    • Liu, S.1    Li, J.2    Tao, Y.3    Xiao, X.4
  • 17
    • 36849096153 scopus 로고    scopus 로고
    • Biomarkers in the assessment of therapies for Familial Amyloidotic Polyneuropathy
    • Macedo B., Batista A.R., Do Amaral J.B., Saraiva M.J. (2007) Biomarkers in the assessment of therapies for Familial Amyloidotic Polyneuropathy. Mol. Med. 13, 584-591.
    • (2007) Mol. Med. , vol.13 , pp. 584-591
    • Macedo, B.1    Batista, A.R.2    Do Amaral, J.B.3    Saraiva, M.J.4
  • 18
    • 1242274389 scopus 로고    scopus 로고
    • Heat shock protein 70 participates in the neuroprotective response to intracellularly expressed beta-amyloid in neurons
    • Magrané J., Smith R.C., Walsh K., Querfurth H.W. (2004) Heat shock protein 70 participates in the neuroprotective response to intracellularly expressed beta-amyloid in neurons. J. Neurosci. 24, 1700-1706.
    • (2004) J. Neurosci. , vol.24 , pp. 1700-1706
    • Magrané, J.1    Smith, R.C.2    Walsh, K.3    Querfurth, H.W.4
  • 19
    • 2442681777 scopus 로고    scopus 로고
    • Human AlphaA- and AlphaB-crystallins bind to Bax and Bcl-X(S) to sequester their translocation during staurosporine-induced apoptosis
    • Mao Y.W., Liu J.P., Xiang H., Li D.W. (2004) Human AlphaA- and AlphaB-crystallins bind to Bax and Bcl-X(S) to sequester their translocation during staurosporine-induced apoptosis. Cell Death Differ. 11, 512-526.
    • (2004) Cell Death Differ. , vol.11 , pp. 512-526
    • Mao, Y.W.1    Liu, J.P.2    Xiang, H.3    Li, D.W.4
  • 20
    • 0029933741 scopus 로고    scopus 로고
    • Human hsp27, Drosophila hsp27 and human αb-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNFalpha-induced cell death
    • Mehlen P., Kretz-Remy C., Préville X., Arrigo A.P. (1996) Human hsp27, Drosophila hsp27 and human αb-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNFalpha-induced cell death. EMBO J. 15, 2695-2706.
    • (1996) EMBO J. , vol.15 , pp. 2695-2706
    • Mehlen, P.1    Kretz-Remy, C.2    Préville, X.3    Arrigo, A.P.4
  • 21
    • 33751216491 scopus 로고    scopus 로고
    • Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation
    • Outeiro T.F., Klucken J., Strathearn K.E. et al. (2006) Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation. Biochem. Biophys. Res. Commun. 351, 631-638.
    • (2006) Biochem. Biophys. Res. Commun. , vol.351 , pp. 631-638
    • Outeiro, T.F.1    Klucken, J.2    Strathearn, K.E.3
  • 22
    • 34547969339 scopus 로고    scopus 로고
    • Misfolded transthyretin causes behavioral changes in a Drosophila model for transthyretin-associated amyloidosis
    • Pokrzywa M., Dacklin I., Hultmark D., Lundgren E. (2007) Misfolded transthyretin causes behavioral changes in a Drosophila model for transthyretin-associated amyloidosis. Eur. J. Neurosci. 26, 913-924.
    • (2007) Eur. J. Neurosci. , vol.26 , pp. 913-924
    • Pokrzywa, M.1    Dacklin, I.2    Hultmark, D.3    Lundgren, E.4
  • 23
    • 29644445485 scopus 로고    scopus 로고
    • αB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin
    • Raman B., Ban T., Sakai M. et al. (2005) αB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin. Biochem. J. 392, 573-581.
    • (2005) Biochem. J. , vol.392 , pp. 573-581
    • Raman, B.1    Ban, T.2    Sakai, M.3
  • 25
    • 35348937731 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system associated with extracellular transthyretin aggregates in familial amyloidotic polyneuropathy
    • Santos S.D., Cardoso I., Magalhães J., Saraiva M.J. (2007) Impairment of the ubiquitin-proteasome system associated with extracellular transthyretin aggregates in familial amyloidotic polyneuropathy. J. Pathol. 213, 200-209.
    • (2007) J. Pathol. , vol.213 , pp. 200-209
    • Santos, S.D.1    Cardoso, I.2    Magalhães, J.3    Saraiva, M.J.4
  • 26
    • 43249124993 scopus 로고    scopus 로고
    • Activation of the heat shock response in familial amyloidotic polyneuropathy
    • Santos S.D., Magalhães J., Saraiva M.J. (2008) Activation of the heat shock response in familial amyloidotic polyneuropathy. J. Neuropathol. Exp. Neurol. 67, 449-455.
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 449-455
    • Santos, S.D.1    Magalhães, J.2    Saraiva, M.J.3
  • 27
    • 71349088766 scopus 로고    scopus 로고
    • The heat shock response modulates transthyretin deposition in the peripheral and autonomic nervous systems
    • Santos S.D., Fernandes R., Saraiva M.J. (2010) The heat shock response modulates transthyretin deposition in the peripheral and autonomic nervous systems. Neurobiol. Aging 31, 280-309.
    • (2010) Neurobiol. Aging , vol.31 , pp. 280-309
    • Santos, S.D.1    Fernandes, R.2    Saraiva, M.J.3
  • 28
    • 0021667431 scopus 로고
    • Family studies of the genetic abnormality in transthyretin (prealbumin) in Portuguese patients with familial amyloidotic polyneuropathy
    • Saraiva M.J., Birken S., Costa P.P., Goodman D.S. (1984) Family studies of the genetic abnormality in transthyretin (prealbumin) in Portuguese patients with familial amyloidotic polyneuropathy. Ann. N Y Acad. Sci. 435, 86-100.
    • (1984) Ann. N Y Acad. Sci. , vol.435 , pp. 86-100
    • Saraiva, M.J.1    Birken, S.2    Costa, P.P.3    Goodman, D.S.4
  • 29
    • 28844451001 scopus 로고    scopus 로고
    • Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice
    • Shen H.Y., He J.C., Wang Y., Huang Q.Y., Chen J.F. (2005) Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice. J. Biol. Chem. 280, 39962-39969.
    • (2005) J. Biol. Chem. , vol.280 , pp. 39962-39969
    • Shen, H.Y.1    He, J.C.2    Wang, Y.3    Huang, Q.Y.4    Chen, J.F.5
  • 30
    • 0035363805 scopus 로고    scopus 로고
    • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease
    • Sittler A., Lurz R., Lueder G. et al. (2001) Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum. Mol. Genet. 10, 1307-1315.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1307-1315
    • Sittler, A.1    Lurz, R.2    Lueder, G.3
  • 31
    • 0035180285 scopus 로고    scopus 로고
    • Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates
    • Sousa M.M., Cardoso I., Fernandes R., Guimarães A., Saraiva M.J. (2001a) Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates. Am. J. Pathol. 159, 1993-2000.
    • (2001) Am. J. Pathol. , vol.159 , pp. 1993-2000
    • Sousa, M.M.1    Cardoso, I.2    Fernandes, R.3    Guimarães, A.4    Saraiva, M.J.5
  • 32
    • 0035478665 scopus 로고    scopus 로고
    • Familial amyloid polyneuropathy: receptor for advanced glycation end products-dependent triggering of neuronal inflammatory and apoptotic pathways
    • Sousa M.M., Du Yan S., Fernandes R., Guimaraes A., Stern D., Saraiva M.J. (2001b) Familial amyloid polyneuropathy: receptor for advanced glycation end products-dependent triggering of neuronal inflammatory and apoptotic pathways. J. Neurosci. 21, 7576-7586.
    • (2001) J. Neurosci. , vol.21 , pp. 7576-7586
    • Sousa, M.M.1    Du Yan, S.2    Fernandes, R.3    Guimaraes, A.4    Stern, D.5    Saraiva, M.J.6
  • 33
    • 0036841818 scopus 로고    scopus 로고
    • Evidence for early cytotoxic aggregates in transgenic mice for human transthyretin Leu55Pro
    • Sousa M.M., Fernandes R., Palha J.A., Taboada A., Vieira P., Saraiva M.J. (2002) Evidence for early cytotoxic aggregates in transgenic mice for human transthyretin Leu55Pro. Am. J. Pathol. 161, 1935-1948.
    • (2002) Am. J. Pathol. , vol.161 , pp. 1935-1948
    • Sousa, M.M.1    Fernandes, R.2    Palha, J.A.3    Taboada, A.4    Vieira, P.5    Saraiva, M.J.6
  • 34
    • 33746814859 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress associated with extracellular aggregates. Evidence from transthyretin deposition in familial amyloid polyneuropathy
    • Teixeira P.F., Cerca F., Santos S.D., Saraiva M.J. (2006) Endoplasmic reticulum stress associated with extracellular aggregates. Evidence from transthyretin deposition in familial amyloid polyneuropathy. J. Biol. Chem. 281, 21998-22003.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21998-22003
    • Teixeira, P.F.1    Cerca, F.2    Santos, S.D.3    Saraiva, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.