메뉴 건너뛰기




Volumn 338, Issue 2, 2005, Pages 973-980

Amyloid fibril formation by macrophage migration inhibitory factor

Author keywords

Acid denaturation; Alzheimer's disease; Amyloid; Amyloid fibrils; Apoptosis; Cytokine; Electron microscopy; Macrophage; Migration Inhibitory Factor; P53; Sedimentation velocity

Indexed keywords

ACID; ALPHA SYNUCLEIN; AMYLOID; AMYLOID BETA PROTEIN; CONGO RED; CYTOKINE; MACROPHAGE MIGRATION INHIBITION FACTOR; THIOFLAVINE;

EID: 27744445334     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.10.040     Document Type: Article
Times cited : (16)

References (42)
  • 1
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • J.W. Kelly The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways Curr. Opin. Struct. Biol. 8 1998 101 106
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 3
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • M. Stefani, and C.M. Dobson Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution J. Mol. Med. 81 2003 678 699
    • (2003) J. Mol. Med. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 4
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • C.M. Dobson Protein folding and misfolding Nature 426 2003 884 890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 6
    • 0037022297 scopus 로고    scopus 로고
    • Conformational Abs recognizing a generic amyloid fibril epitope
    • B. O'Nuallain, and R. Wetzel Conformational Abs recognizing a generic amyloid fibril epitope Proc. Natl. Acad. Sci. USA 99 2002 1485 1490
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1485-1490
    • O'Nuallain, B.1    Wetzel, R.2
  • 7
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behavior
    • J.W. Kelly Alternative conformations of amyloidogenic proteins govern their behavior Curr. Opin. Struct. Biol. 6 1996 11 17
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 11-17
    • Kelly, J.W.1
  • 8
    • 0030004644 scopus 로고    scopus 로고
    • The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
    • Z. Lai, W. Colon, and J.W. Kelly The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid Biochemistry 35 1996 6470 6482
    • (1996) Biochemistry , vol.35 , pp. 6470-6482
    • Lai, Z.1    Colon, W.2    Kelly, J.W.3
  • 10
    • 0030924448 scopus 로고    scopus 로고
    • Role of macrophage migration inhibitory factor in the regulation of the immune response
    • C.N. Metz, and R. Bucala Role of macrophage migration inhibitory factor in the regulation of the immune response Adv. Immunol. 66 1997 197 223
    • (1997) Adv. Immunol. , vol.66 , pp. 197-223
    • Metz, C.N.1    Bucala, R.2
  • 12
    • 0033580992 scopus 로고    scopus 로고
    • Sustained mitogen-activated protein kinase (MAPK) and cytoplasmic phospholipase A2 activation by macrophage migration inhibitory factor (MIF). Regulatory role in cell proliferation and glucocorticoid action
    • R.A. Mitchell, C.N. Metz, T. Peng, and R. Bucala Sustained mitogen-activated protein kinase (MAPK) and cytoplasmic phospholipase A2 activation by macrophage migration inhibitory factor (MIF). Regulatory role in cell proliferation and glucocorticoid action J. Biol. Chem. 274 1999 18100 18106
    • (1999) J. Biol. Chem. , vol.274 , pp. 18100-18106
    • Mitchell, R.A.1    Metz, C.N.2    Peng, T.3    Bucala, R.4
  • 14
    • 0037039308 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor (MIF) sustains macrophage proinflammatory function by inhibiting p53: Regulatory role in the innate immune response
    • R.A. Mitchell, H. Liao, J. Chesney, G. Fingerle-Rowson, J. Baugh, J. David, and R. Bucala Macrophage migration inhibitory factor (MIF) sustains macrophage proinflammatory function by inhibiting p53: regulatory role in the innate immune response Proc. Natl. Acad. Sci. USA 99 2002 345 350
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 345-350
    • Mitchell, R.A.1    Liao, H.2    Chesney, J.3    Fingerle-Rowson, G.4    Baugh, J.5    David, J.6    Bucala, R.7
  • 18
    • 0034660602 scopus 로고    scopus 로고
    • Glutamine synthetase, hemoglobin alpha-chain, and macrophage migration inhibitory factor binding to amyloid beta-protein: Their identification in rat brain by a novel affinity chromatography and in Alzheimer's disease brain by immunoprecipitation
    • R. Oyama, H. Yamamoto, and K. Titani Glutamine synthetase, hemoglobin alpha-chain, and macrophage migration inhibitory factor binding to amyloid beta-protein: their identification in rat brain by a novel affinity chromatography and in Alzheimer's disease brain by immunoprecipitation Biochim. Biophys. Acta 1479 2000 91 102
    • (2000) Biochim. Biophys. Acta , vol.1479 , pp. 91-102
    • Oyama, R.1    Yamamoto, H.2    Titani, K.3
  • 19
    • 0029812254 scopus 로고    scopus 로고
    • The subunit structure of human macrophage migration inhibitory factor: Evidence for a trimer
    • H.W. Sun, M. Swope, C. Cinquina, S. Bedarkar, J. Bernhagen, R. Bucala, and E. Lolis The subunit structure of human macrophage migration inhibitory factor: evidence for a trimer Protein Eng. 9 1996 631 635
    • (1996) Protein Eng. , vol.9 , pp. 631-635
    • Sun, H.W.1    Swope, M.2    Cinquina, C.3    Bedarkar, S.4    Bernhagen, J.5    Bucala, R.6    Lolis, E.7
  • 21
    • 0028908925 scopus 로고
    • The structure and physicochemical properties of rat liver macrophage migration inhibitory factor
    • J. Nishihira, T. Kuriyama, M. Sakai, S. Nishi, S. Ohki, and K. Hikichi The structure and physicochemical properties of rat liver macrophage migration inhibitory factor Biochim. Biophys. Acta 1247 1995 159 162
    • (1995) Biochim. Biophys. Acta , vol.1247 , pp. 159-162
    • Nishihira, J.1    Kuriyama, T.2    Sakai, M.3    Nishi, S.4    Ohki, S.5    Hikichi, K.6
  • 22
    • 0033559684 scopus 로고    scopus 로고
    • Equilibrium and transient intermediates in folding of human macrophage migration inhibitory factor
    • E. Zerovnik, V. Janjic, A. Francky, and B. Mozetic-Francky Equilibrium and transient intermediates in folding of human macrophage migration inhibitory factor Eur. J. Biochem. 260 1999 609 618
    • (1999) Eur. J. Biochem. , vol.260 , pp. 609-618
    • Zerovnik, E.1    Janjic, V.2    Francky, A.3    Mozetic-Francky, B.4
  • 23
    • 0032080006 scopus 로고    scopus 로고
    • Cross-linking and mutational analysis of the oligomerization state of the cytokine macrophage migration inhibitory factor (MIF)
    • R. Mischke, R. Kleemann, H. Brunner, and J. Bernhagen Cross-linking and mutational analysis of the oligomerization state of the cytokine macrophage migration inhibitory factor (MIF) FEBS Lett. 427 1998 85 90
    • (1998) FEBS Lett. , vol.427 , pp. 85-90
    • Mischke, R.1    Kleemann, R.2    Brunner, H.3    Bernhagen, J.4
  • 24
    • 0027787563 scopus 로고
    • Purification and characterization of human macrophage migration inhibitory factor: Evidence for specific binding to glutathione and formation of subunit structure
    • J. Nishihira, T. Kuriyama, H. Nishino, T. Ishibashi, M. Sakai, and S. Nishi Purification and characterization of human macrophage migration inhibitory factor: evidence for specific binding to glutathione and formation of subunit structure Biochem. Mol. Biol. Int. 31 1993 841 850
    • (1993) Biochem. Mol. Biol. Int. , vol.31 , pp. 841-850
    • Nishihira, J.1    Kuriyama, T.2    Nishino, H.3    Ishibashi, T.4    Sakai, M.5    Nishi, S.6
  • 25
    • 0027997701 scopus 로고
    • Purification, bioactivity, and secondary structure analysis of mouse and human macrophage migration inhibitory factor (MIF)
    • J. Bernhagen, R.A. Mitchell, T. Calandra, W. Voelter, A. Cerami, and R. Bucala Purification, bioactivity, and secondary structure analysis of mouse and human macrophage migration inhibitory factor (MIF) Biochemistry 33 1994 14144 14155
    • (1994) Biochemistry , vol.33 , pp. 14144-14155
    • Bernhagen, J.1    Mitchell, R.A.2    Calandra, T.3    Voelter, W.4    Cerami, A.5    Bucala, R.6
  • 26
    • 0028672523 scopus 로고
    • Boundary analysis in sedimentation experiments
    • W.F. Stafford Boundary analysis in sedimentation experiments Methods Enzymol. 240 1994 478 501
    • (1994) Methods Enzymol. , vol.240 , pp. 478-501
    • Stafford, W.F.1
  • 28
    • 0033677088 scopus 로고    scopus 로고
    • The proinflammatory mediator macrophage migration inhibitory factor induces glucose catabolism in muscle
    • F. Benigni, T. Atsumi, T. Calandra, C. Metz, B. Echtenacher, T. Peng, and R. Bucala The proinflammatory mediator macrophage migration inhibitory factor induces glucose catabolism in muscle J. Clin. Invest. 106 2000 1291 1300
    • (2000) J. Clin. Invest. , vol.106 , pp. 1291-1300
    • Benigni, F.1    Atsumi, T.2    Calandra, T.3    Metz, C.4    Echtenacher, B.5    Peng, T.6    Bucala, R.7
  • 30
    • 0030292993 scopus 로고    scopus 로고
    • Local and distant histopathological effects of unilateral amyloid-beta 25-35 injections into the amygdala of young F344 rats
    • E.M. Sigurdsson, S.A. Lorens, M.J. Hejna, X.W. Dong, and J.M. Lee Local and distant histopathological effects of unilateral amyloid-beta 25-35 injections into the amygdala of young F344 rats Neurobiol. Aging 17 1996 893 901
    • (1996) Neurobiol. Aging , vol.17 , pp. 893-901
    • Sigurdsson, E.M.1    Lorens, S.A.2    Hejna, M.J.3    Dong, X.W.4    Lee, J.M.5
  • 31
    • 0033550075 scopus 로고    scopus 로고
    • The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions
    • H.A. Lashuel, C. Wurth, L. Woo, and J.W. Kelly The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions Biochemistry 38 1999 13560 13573
    • (1999) Biochemistry , vol.38 , pp. 13560-13573
    • Lashuel, H.A.1    Wurth, C.2    Woo, L.3    Kelly, J.W.4
  • 32
    • 0035896018 scopus 로고    scopus 로고
    • Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin
    • F. Chiti, P. Mangione, A. Andreola, S. Giorgetti, M. Stefani, C.M. Dobson, V. Bellotti, and N. Taddei Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin J. Mol. Biol. 307 2001 379 391
    • (2001) J. Mol. Biol. , vol.307 , pp. 379-391
    • Chiti, F.1    Mangione, P.2    Andreola, A.3    Giorgetti, S.4    Stefani, M.5    Dobson, C.M.6    Bellotti, V.7    Taddei, N.8
  • 34
    • 0030822278 scopus 로고    scopus 로고
    • Amyloid precursor protein, a beta and amyloid-associated proteins involved in chloroquine retinopathy in rats-immunopathological studies
    • T. Yoshida, R. Fukatsu, K. Tsuzuki, Y. Aizawa, Y. Hayashi, N. Sasaki, Y. Takamaru, N. Fujii, and N. Takahata Amyloid precursor protein, A beta and amyloid-associated proteins involved in chloroquine retinopathy in rats-immunopathological studies Brain Res. 764 1997 283 288
    • (1997) Brain Res. , vol.764 , pp. 283-288
    • Yoshida, T.1    Fukatsu, R.2    Tsuzuki, K.3    Aizawa, Y.4    Hayashi, Y.5    Sasaki, N.6    Takamaru, Y.7    Fujii, N.8    Takahata, N.9
  • 35
    • 0033535983 scopus 로고    scopus 로고
    • Crystal structure of macrophage migration inhibitory factor complexed with (E)-2-fluoro-p-hydroxycinnamate at 1.8 Å resolution: Implications for enzymatic catalysis and inhibition
    • A.B. Taylor, W.H. Johnson Jr., R.M. Czerwinski, H.S. Li, M.L. Hackert, and C.P. Whitman Crystal structure of macrophage migration inhibitory factor complexed with (E)-2-fluoro-p-hydroxycinnamate at 1.8 Å resolution: implications for enzymatic catalysis and inhibition Biochemistry 38 1999 7444 7452
    • (1999) Biochemistry , vol.38 , pp. 7444-7452
    • Taylor, A.B.1    Johnson Jr., W.H.2    Czerwinski, R.M.3    Li, H.S.4    Hackert, M.L.5    Whitman, C.P.6
  • 37
    • 0029895838 scopus 로고    scopus 로고
    • Crystal structure at 2.6-Å resolution of human macrophage migration inhibitory factor
    • H.W. Sun, J. Bernhagen, R. Bucala, and E. Lolis Crystal structure at 2.6-Å resolution of human macrophage migration inhibitory factor Proc. Natl. Acad. Sci. USA 93 1996 5191 5196
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5191-5196
    • Sun, H.W.1    Bernhagen, J.2    Bucala, R.3    Lolis, E.4
  • 38
    • 1642384385 scopus 로고    scopus 로고
    • Re-examining the oligomerization state of macrophage migration inhibitory factor (MIF) in solution
    • J.S. Philo, T.H. Yang, and M. LaBarre Re-examining the oligomerization state of macrophage migration inhibitory factor (MIF) in solution Biophys. Chem. 108 2004 77 87
    • (2004) Biophys. Chem. , vol.108 , pp. 77-87
    • Philo, J.S.1    Yang, T.H.2    Labarre, M.3
  • 39
    • 0032510960 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor interactions with glutathione and S-hexylglutathione
    • M.D. Swope, H.W. Sun, B. Klockow, P. Blake, and E. Lolis Macrophage migration inhibitory factor interactions with glutathione and S-hexylglutathione J. Biol. Chem. 273 1998 14877 14884
    • (1998) J. Biol. Chem. , vol.273 , pp. 14877-14884
    • Swope, M.D.1    Sun, H.W.2    Klockow, B.3    Blake, P.4    Lolis, E.5
  • 40
    • 0033579884 scopus 로고    scopus 로고
    • Targeted disruption of migration inhibitory factor gene reveals its critical role in sepsis
    • M. Bozza, A.R. Satoskar, G. Lin, B. Lu, A.A. Humbles, C. Gerard, and J.R. David Targeted disruption of migration inhibitory factor gene reveals its critical role in sepsis J. Exp. Med. 189 1999 341 346
    • (1999) J. Exp. Med. , vol.189 , pp. 341-346
    • Bozza, M.1    Satoskar, A.R.2    Lin, G.3    Lu, B.4    Humbles, A.A.5    Gerard, C.6    David, J.R.7
  • 42
    • 0037085717 scopus 로고    scopus 로고
    • Borna disease virus-induced accumulation of macrophage migration inhibitory factor in rat brain astrocytes is associated with inhibition of macrophage infiltration
    • M. Bacher, E. Weihe, B. Dietzschold, A. Meinhardt, H. Vedder, D. Gemsa, and M. Bette Borna disease virus-induced accumulation of macrophage migration inhibitory factor in rat brain astrocytes is associated with inhibition of macrophage infiltration Glia 37 2002 291 306
    • (2002) Glia , vol.37 , pp. 291-306
    • Bacher, M.1    Weihe, E.2    Dietzschold, B.3    Meinhardt, A.4    Vedder, H.5    Gemsa, D.6    Bette, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.