Structural Regulation of a Peptide‐Conjugated Graft Copolymer: A Simple Model for Amyloid Formation

Koga, Tomoyuki; Taguchi, Kazuhiro; Kobuke, Yoshiaki; Kinoshita, Takatoshi; Higuchi, Masahiro

doi:10.1002/chem.200390132

Cited by 51 publications

(40 citation statements)

References 59 publications

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“…The similarity among the different amyloid deposits and their ubiquity suggests that such structures might represent a generic form of the noncovalent packing of polypeptide chains (6,7,14). It may be possible that the aggregation into such well defined, nanoordered assemblies represents a state of an efficient minimal energy arrangement of polypeptide chains (15)(16)(17). Recent results have shown that fibrillar structures similar to amyloid fibrils are formed by sequences like poly(XGlyGlyYGly) (X, Y ϭ Val, Leu, or Ala), which are highly repeated in the hydrophobic domains of elastin (18,19).…”

Section: Charge Transport and Intrinsic Fluorescence In Amyloid-like mentioning

confidence: 99%

Charge transport and intrinsic fluorescence in amyloid-like fibrils

Mercato

Pompa²,

Maruccio³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

204

203

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Section: Charge Transport and Intrinsic Fluorescence In Amyloid-like mentioning

confidence: 99%

Charge transport and intrinsic fluorescence in amyloid-like fibrils

Mercato

Pompa²,

Maruccio³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

204

203

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“…The Aggresomal Bodies in Cardiomyocytes Are Amyloidphilic. In an attempt to define further the relationship of these electron-dense bodies to the amyloid-based degenerative diseases, we tested their ability to react positively to the amyloidphilic dye Congo red (26,27). Congo red-positive inclusions were abundant in CryAB R120G -transfected cardiomyocytes and were undetectable in cells that were transfected with either empty adenovirus or with CryAB adenovirus (Fig.…”

Section: Resultsmentioning

confidence: 99%

Desmin-related cardiomyopathy in transgenic mice: A cardiac amyloidosis

Sanbe

Osińska

Saffitz

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

266

321

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An R120G missense mutation in the small heat shock protein ␣-B-crystallin (CryAB R120G ) causes desmin-related cardiomyopathy (DRM). DRM is characterized by the formation of aggregates containing CryAB and desmin, and it can be recapitulated in transgenic mice by cardiac-specific expression of the mutant protein. In this article, we show that expression of CryAB R120G leads to the formation of electron-dense bodies characteristic of the DRMs and identify these bodies as aggresomes, which are characteristic of the neurodegenerative diseases. Cardiomyocytes transfected with adenovirus containing CryAB R120G establish the necessity and sufficiency of CryAB R120G expression for aggresome formation. The commonality of these aggresomes with oligomeric protein aggregates found in the amyloid-related degenerative diseases was corroborated by the presence of high levels of amyloid oligomers that may represent a primary toxic species in the amyloid diseases. These oligomeric amyloid intermediates are present also in cardiomyocytes derived from many human dilated and hypertrophic cardiomyopathies.H uman heart failure is the leading cause of death in the developed world, and it represents a final common endpoint for several disease entities, including hypertension, coronary artery disease, and the cardiomyopathies (1, 2). A lack of pathogenic commonality is underscored by the large number of mutations in different classes of cardiac proteins that have been linked to dilated and hypertrophic cardiomyopathy (HCM) (3). Mutations in the cytoskeletal and associated proteins can be causative because these proteins function in structural, sensor, and signaling roles in the normal and diseased cardiomyocyte (4). For example, up-regulation of the intermediate filament protein desmin occurs in cardiac disorders such as cardiac hypertrophy and congestive heart failure (CHF) (5), and desmin mutations are associated with desmin-related cardiomyopathy (DRM) and idiopathic dilated cardiomyopathy (6, 7). Mutations in other proteins also have been associated with the DRMs, and genetic evidence linking an R120G mutation in ␣-B-crystallin (CryAB, CryAB R120G ) to human DRM (8) prompted a series of experiments in which we showed that cardiac-restricted transgenic (TG) expression of CryAB R120G was sufficient to cause heart failure in a mouse model (9). Although up-regulation of CryAB is associated with disease states including DRM, its synthesis probably represents a general cellular response to stress because CryAB has chaperone-like activity. Indeed, CryAB, which binds to both desmin and cytoplasmic actin, probably participates normally as a chaperone in intermediate filament formation and maintenance in the heart.The ␣-crystallins (␣-A and ␣-B) were of interest initially as major structural proteins present in the lens of the vertebrate eye. However, the discovery that they were related to the small heat shock proteins (hsps) in Drosophila (10) prompted reevaluation of their broader role(s), and it is now known that CryAB belongs to the sma...

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“…Nanoparticles having organic molecules such as peptides [8], oligonucleotides [9,10], and oligosaccharides [11] as building blocks have been utilized to form ordered and periodic arrangements of the nanoparticles. Especially, the structure of peptide assemblies can be controlled by external stimuli such as pH and solution composition [12,13]. Therefore, the functions of peptide-coated nanoparticle assemblies may be controlled by the stimulus induced rearrangement of the nanoparticles owing to the structural changes of the surface peptide chains.…”

Section: Introductionmentioning

confidence: 99%