Immunohistochemical localization of aggresomal proteins in glial cytoplasmic inclusions in multiple system atrophy

Chiba, Yoichi; Takei, Shiro; Kawamura, Noriko; Kawaguchi, Yoshiharu; Sasaki, Kenji; Hasegawa-Ishii, Sanae; Furukawa, Ayako; Hosokawa, Masanori; Shimada, Atsuyoshi

doi:10.1111/j.1365-2990.2011.01229.x

Cited by 42 publications

(33 citation statements)

References 65 publications

(139 reference statements)

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“…A model for microtubule-based delivery of protein aggregates to aggresomes has been described (Kopito, 2000;Kopito and Sitia, 2000). In agreement with our results, it has been described the presence of -tubulin, as an aggresomerelated protein in -synuclein-containing aggresomes (Chiba et al 2012) and in perinuclear aggregate bodies formed by a truncated protein containing expanded polyQ stretches (Shimohata et al 2002). All these studies corroborate our findings about the presence of Hsp70 chaperone, actin and tubulin as aggresomes-related proteins.…”

supporting

confidence: 82%

A novel bio-functional material based on mammalian cell aggresomes

Rodríguez‐Carmona

Mendoza

Ruiz-Cánovas

et al. 2015

Appl Microbiol Biotechnol

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Aggresomes are protein aggregates found in mammalian cells when the intracellular protein degradation machinery is over-titred. Despite they abound in cells producing recombinant proteins of biomedical and biotechnological interest, the physiological roles of these protein clusters and the functional status of the embedded proteins remain basically unexplored. In this work, we have determined for the first time that, like in bacterial inclusion bodies, deposition of recombinant proteins into aggresomes does not imply functional inactivation. As a model , human -galactosidase A (GLA) has been expressed in mammalian cells as enzymatically active, mechanically stable aggresomes showing higher thermal stability than the soluble GLA version. Since aggresomes are easily produced and purified, we propose these particles as novel functional biomaterials with potential as carrier-free, self-immobilized catalyzers in biotechnology and biomedicine.

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supporting

confidence: 82%

A novel bio-functional material based on mammalian cell aggresomes

Rodríguez‐Carmona

Mendoza

Ruiz-Cánovas

et al. 2015

Appl Microbiol Biotechnol

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“…Some authors assume that oligodendrocytes adopt a modified process of aggresome formation and may upgrade the expression of synucleins selectively in response to some diseasespecific signal. Another possibility is that oligodendrocytes may actively take up synucleins released from adjacent neurons (Chiba et al, 2012).…”

Section: Discussionmentioning

confidence: 99%

Role of synucleins in traumatic brain injury — An experimental in vitro and in vivo study in mice

Surgucheva

He²,

Rich

et al. 2014

Molecular and Cellular Neuroscience

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“…In contrast thereto, Odagiri et al (2013) could not observe differences in the levels of HDAC6 between control and patients with AD or DLB (Dementia with Lewy Bodies). In MSA GCIs were positively labeled by antibodies against HDAC6; they also displayed immunoreactivity against p62, the 20S proteasome and gamma-tubulin, indicating that GCIs share common features with aggresomes (Chiba et al, 2012). Data from our laboratory further depicted that GCIs in MSA brains contain the autophagy marker LC3, which sustains the idea that autophagy is involved in GCI formation and oligodendroglial cell death (Schwarz et al, 2012).…”

Section: Hdac6 and Neurodegenerationmentioning

confidence: 76%