Immunolocalization of Smurf1 in Hirano bodies

Alzheimer’s disease (AD) is a degenerative neurological disease and has an inconspicuous onset and progressive development. Clinically, it is characterized by severe dementia manifestations, including memory impairment, aphasia, apraxia, loss of recognition, impairment of visual-spatial skills, executive dysfunction, and changes in personality and behavior. Its etiology is unknown to date. However, several cellular biological signatures of AD have been identified such as synaptic dysfunction, β-amyloid plaques, hyperphosphorylated tau, cofilin-actin rods, and Hirano bodies which are related to the actin cytoskeleton. Cofilin is one of the most affluent and common actin-binding proteins and plays a role in cell motility, migration, shape, and metabolism. They also play an important role in severing actin filament, nucleating, depolymerizing, and bundling activities. In this review, we summarize the structure of cofilins and their functional and regulating roles, focusing on the synaptic dysfunction, β-amyloid plaques, hyperphosphorylated tau, cofilin-actin rods, and Hirano bodies of AD.

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The structure analysis of Hirano bodies by digital processing on electron micrographs

Acta Neuropathologica ◽

10.1007/bf00687959 ◽

1986 ◽

Vol 71 (1-2) ◽

pp. 32-37 ◽

Cited By ~ 14

Author(s):

H. Mori ◽

M. Tomonaga ◽

N. Baba ◽

K. Kanaya

Keyword(s):

Structure Analysis ◽

Electron Micrographs ◽

Digital Processing ◽

Hirano Bodies

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Model Hirano Bodies Protect against Tau-Independent and Tau-Dependent Cell Death Initiated by the Amyloid Precursor Protein Intracellular Domain

PLoS ONE ◽

10.1371/journal.pone.0044996 ◽

2012 ◽

Vol 7 (9) ◽

pp. e44996 ◽

Cited By ~ 13

Author(s):

Matthew Furgerson ◽

Marcus Fechheimer ◽

Ruth Furukawa

Keyword(s):

Cell Death ◽

Amyloid Precursor Protein ◽

Precursor Protein ◽

Hirano Bodies ◽

Intracellular Domain ◽

Dependent Cell

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Formation of Hirano Bodies after Inducible Expression of a Modified Form of an Actin-Cross-Linking Protein

Eukaryotic Cell ◽

10.1128/ec.00379-08 ◽

2009 ◽

Vol 8 (6) ◽

pp. 852-857 ◽

Cited By ~ 10

Author(s):

Juan F. Reyes ◽

Karen Stone ◽

Jeanie Ramos ◽

Andrew Maselli

Keyword(s):

Neurodegenerative Disorders ◽

Molecular Mechanisms ◽

Expression System ◽

Inducible Expression ◽

Postmortem Brain ◽

Vector System ◽

Actin Binding ◽

Cell Cortex ◽

Hirano Bodies ◽

Cytoplasmic Inclusions

ABSTRACT Hirano bodies are cytoplasmic inclusions composed mainly of actin and actin-associated proteins. The formation of Hirano bodies during various neurodegenerative disorders, including Alzheimer's disease and amyotrophic lateral sclerosis, has been reported. Although the underlying molecular mechanisms that lead to the formation of these inclusions in the brain are not known, expression of the C-terminal fragment (CT) (amino acids 124 to 295) from the endogenous 34-kDa actin-binding protein of Dictyostelium discoideum leads to the formation of actin inclusions in vivo. In the current study, we report the development of an inducible expression system to study the early phases of Hirano body formation using an inducible promoter system (rnrB). By fusing the CT to a green fluorescent protein (CT-GFP), we monitored protein expression and localization by fluorescence microscopy, flow cytometry, and Western blot analysis. We observed an increase in the number and size of inclusions formed following induction of the CT-GFP vector system. Time-lapse microscopy studies revealed that the CT-GFP foci associated with the cell cortex and fused to form a single large aggregate. Transmission electron microscopy further demonstrates that these inclusions have a highly ordered ultrastructure, a pathological hallmark of Hirano bodies observed in postmortem brain samples from patients with various neurodegenerative disorders. Collectively, this system provides a method to visualize and characterize the events that surround early actin inclusion formation in a eukaryotic model.

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Unusual, rod-shaped cytoplasmic inclusions (Hirano bodies) in a cerebellar hemangioblastoma

Acta Neuropathologica ◽

10.1007/bf00688147 ◽

1975 ◽

Vol 31 (2) ◽

pp. 129-135 ◽

Cited By ~ 15

Author(s):

Yao-Shi Fu ◽

John Ward ◽

Harold F. Young

Keyword(s):

Hirano Bodies ◽

Cytoplasmic Inclusions ◽

Cerebellar Hemangioblastoma

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Peripheral Nerve Findings in Rett Syndrome

Journal of Child Neurology ◽

10.1177/0883073888003001s06 ◽

1988 ◽

Vol 3 (1_suppl) ◽

pp. S25-S30 ◽

Cited By ~ 13

Author(s):

Richard H. Haas ◽

Seth Love

Keyword(s):

Rett Syndrome ◽

Sural Nerve ◽

Enzyme Histochemistry ◽

Axonal Neuropathy ◽

Type I ◽

Normal Density ◽

Hirano Bodies ◽

Peroneus Brevis ◽

Type I Fibers ◽

Muscle Biopsies

Sural nerve and peroneus brevis muscle biopsies were studied in 12 patients with Rett syndrome, ten with the typical form of the disorder according to 1985 criteria, and two with atypical features. Ages ranged from 23 months to 25 years. All stages of the disease were represented. There was evidence of a mild axonal neuropathy in seven of 12 patients. Degenerative and occasional regenerative changes were seen in five sural nerve biopsies, including one from the youngest patient in the series, who was normally nourished and fully ambulatory. Occasional nonspecific ultrastructural abnormalities were present, including accumulation of pi granules in Schwann cells and Hirano bodies within axons. However, morphometric analysis of the four nerves in which these alterations were most prominent showed a normal density and size distribution of myelinated fibers. Enzyme histochemistry of the peroneus brevis biopsies demonstrated abnormal predominance of type II muscle fibers in three of the 12 biopsies and atrophy of type I fibers in one patient. (J Child Neurol 1988;3(Suppl):S25-S30).

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