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cofilin rod

Hellen C Ishikawa-Ankerhold, Wioleta Daszkiewicz, Michael Schleicher, Annette Müller-Taubenberger
Intranuclear rods are aggregates consisting of actin and cofilin that are formed in the nucleus in consequence of chemical or mechanical stress conditions. The formation of rods is implicated in a variety of pathological conditions, such as certain myopathies and some neurological disorders. It is still not well understood what exactly triggers the formation of intranuclear rods, whether other proteins are involved, and what the underlying mechanisms of rod assembly or disassembly are. In this study, Dictyostelium discoideum was used to examine appearance, stages of assembly, composition, stability, and dismantling of rods...
January 11, 2017: Scientific Reports
Leonid A Serebryannyy, Michaela Yuen, Megan Parilla, Sandra T Cooper, Primal de Lanerolle
Actin plays a crucial role in regulating multiple processes within the nucleus, including transcription and chromatin organization. However, the polymerization state of nuclear actin remains controversial, and there is no evidence for persistent actin filaments in a normal interphase nucleus. Further, several disease pathologies are characterized by polymerization of nuclear actin into stable filaments or rods. These include filaments that stain with phalloidin, resulting from point mutations in skeletal α-actin, detected in the human skeletal disease intranuclear rod myopathy, and cofilin/actin rods that form in response to cellular stressors like heatshock...
2016: Frontiers in Physiology
Weiwei Wang, Ellen Townes-Anderson
The structural plasticity of synaptic terminals contributes to normal nervous system function but also to neural degeneration, in the form of terminal retraction, and regeneration, due to process growth. Synaptic morphological change is mediated through the actin cytoskeleton, which is enriched in axonal and dendritic terminals. Whereas the three RhoGTPases, RhoA, Cdc42 and Rac, function as upstream signaling nodes sensitive to extracellular stimuli, LIMK-cofilin activity serves as a common downstream effector to up-regulate actin turnover, which is necessary for both polymerization and depolymerization...
July 2016: Neural Regeneration Research
Daniel J Kelpsch, Christopher M Groen, Tiffany N Fagan, Sweta Sudhir, Tina L Tootle
Drosophila oogenesis provides a developmental system with which to study nuclear actin. During Stages 5-9, nuclear actin levels are high in the oocyte and exhibit variation within the nurse cells. Cofilin and Profilin, which regulate the nuclear import and export of actin, also localize to the nuclei. Expression of GFP-tagged Actin results in nuclear actin rod formation. These findings indicate that nuclear actin must be tightly regulated during oogenesis. One factor mediating this regulation is Fascin. Overexpression of Fascin enhances nuclear GFP-Actin rod formation, and Fascin colocalizes with the rods...
October 1, 2016: Molecular Biology of the Cell
Junjiang Jin, Ying Dong, Ying Wang, Lin Xia, Weihong Gu, Xue Bai, Yanan Chang, Mingyi Zhang, Kui Chen, Juan Li, Lina Zhao, Gengmei Xing
Fullerenol nanoparticles are promising for various biological applications; many studies have shown that they induce variable and diverse biological effects including side effects. Separation and purification of two fractions of fullerenols has demonstrated that they have varied chemical structures on the surfaces of their carbon cages. Actin is an important structural protein that is able to transform functional structures under varied physiological conditions. We assessed the abilities of the two fractions of fullerenols to attach to actin and induce variable morphological features in actin filament structures...
June 2016: Journal of Biomedical Nanotechnology
James R Bamburg, Barbara W Bernstein
Cytoskeletal abnormalities and synaptic loss, typical of both familial and sporadic Alzheimer disease (AD), are induced by diverse stresses such as neuroinflammation, oxidative stress, and energetic stress, each of which may be initiated or enhanced by proinflammatory cytokines or amyloid-β (Aβ) peptides. Extracellular Aβ-containing plaques and intracellular phospho-tau-containing neurofibrillary tangles are postmortem pathologies required to confirm AD and have been the focus of most studies. However, AD brain, but not normal brain, also have increased levels of cytoplasmic rod-shaped bundles of filaments composed of ADF/cofilin-actin in a 1:1 complex (rods)...
September 2016: Cytoskeleton
Buer Sen, Zhihui Xie, Gunes Uzer, William R Thompson, Maya Styner, Xin Wu, Janet Rubin
Depolymerization of the actin cytoskeleton induces nuclear trafficking of regulatory proteins and global effects on gene transcription. We here show that in mesenchymal stem cells (MSCs), cytochalasin D treatment causes rapid cofilin-/importin-9-dependent transfer of G-actin into the nucleus. The continued presence of intranuclear actin, which forms rod-like structures that stain with phalloidin, is associated with induction of robust expression of the osteogenic genes osterix and osteocalcin in a Runx2-dependent manner, and leads to acquisition of osteogenic phenotype...
October 2015: Stem Cells
Ben Chen, Yun Wang
Cofilin-1 is a major actin depolymerizer in the central nervous system. It is a member of the ADF/cofilin family that regulates the dynamics of actin filaments. The activity of cofilin-1 is regulated by the modulation of phosphorylation at its Ser3 residue, and its proper function is crucial for the structure and proper function of neurons. Cofilin rods, pathological structures composed of cofilin and actin, form under stress conditions. A high cofilin/F-actin ratio, cofilin dephosphorylation and/or cofilin oxidation are three major mechanisms of cofilin rod formation...
2015: CNS & Neurological Disorders Drug Targets
Irina Surgucheva, Shuangteng He, Megan C Rich, Ram Sharma, Natalia N Ninkina, Philip F Stahel, Andrei Surguchov
Synucleins are small prone to aggregate proteins associated with several neurodegenerative diseases (NDDs), however their role in traumatic brain injury (TBI) is an emerging area of investigation. Using in vitro scratch injury model and in vivo mouse weight-drop model we have found that the injury causes alterations in the expression and localization of synucleins near the damaged area. Before injury, α-synuclein is diffused in the cytoplasm of neurons and γ-synuclein is both in the cytoplasm and nucleus of oligodendrocytes...
November 2014: Molecular and Cellular Neurosciences
Keifer P Walsh, Thomas B Kuhn, James R Bamburg
Increasing evidence suggests that proteins exhibiting "prion-like" behavior cause distinct neurodegenerative diseases, including inherited, sporadic and acquired types. The conversion of cellular prion protein (PrP(C)) to its infectious protease resistant counterpart (PrP(Res)) is the essential feature of prion diseases. However, PrP(C) also performs important functions in transmembrane signaling, especially in neurodegenerative processes. Beta-amyloid (Aβ) synaptotoxicity and cognitive dysfunction in mouse models of Alzheimer disease are mediated by a PrP(C)-dependent pathway...
2014: Prion
Tasnim Rahman, Danielle S Davies, Rudi K Tannenberg, Sandra Fok, Claire Shepherd, Peter R Dodd, Karen M Cullen, Claire Goldsbury
BACKGROUND: Imaging of human brain as well as cellular and animal models has highlighted a role for the actin cytoskeleton in the development of cell pathology in Alzheimer's disease (AD). Rods and aggregates of the actin-associated protein cofilin are abundant in grey matter of postmortem AD brain and rods are found inside neurites in animal and cell models of AD. OBJECTIVE: We sought further understanding of the significance of cofilin rods/aggregates to the disease process: Do rods/aggregates correlate with AD progression and the development of hallmark neurofibrillary tangles and neuropil threads? Are cofilin rods/aggregates found in the same neurites as hyperphosphorylated tau? METHODS: The specificity of rods/aggregates to AD compared with general aging and their spatial relationship to tau protein was examined in postmortem human hippocampus, inferior temporal cortex, and anterior cingulate cortex...
2014: Journal of Alzheimer's Disease: JAD
Patrícia Schönhofen, Liana Marengo de Medeiros, Carolina Piletti Chatain, Ivi Juliana Bristot, Fábio Klamt
Cofilin-1 protein, which main function is to regulate actin cytoskeleton dynamics, appears to be involved with many steps in the neurotoxicity processes found in neurodegenerative diseases such as Alzheimer's disease (AD), Parkinson's disease (PD) and Huntington's disease (HD). As the dynamics of actin filaments play a major role in several cellular processes, the primary involvement of cofilin-1 dysfunctions in the pathophysiology of these disorders may be related to a cytoskeleton stress. However, recently cofilin-1 has also been related to other biological processes such as cell death by apoptosis...
May 2014: Mini Reviews in Medicinal Chemistry
Keifer P Walsh, Laurie S Minamide, Sarah J Kane, Alisa E Shaw, David R Brown, Bruce Pulford, Mark D Zabel, J David Lambeth, Thomas B Kuhn, James R Bamburg
Neurites of neurons under acute or chronic stress form bundles of filaments (rods) containing 1∶1 cofilin∶actin, which impair transport and synaptic function. Rods contain disulfide cross-linked cofilin and are induced by treatments resulting in oxidative stress. Rods form rapidly (5-30 min) in >80% of cultured hippocampal or cortical neurons treated with excitotoxic levels of glutamate or energy depleted (hypoxia/ischemia or mitochondrial inhibitors). In contrast, slow rod formation (50% of maximum response in ∼6 h) occurs in a subpopulation (∼20%) of hippocampal neurons upon exposure to soluble human amyloid-β dimer/trimer (Aβd/t) at subnanomolar concentrations...
2014: PloS One
Yan-Ting Zhang, Li-Hui Xu, Qun Lu, Kun-Peng Liu, Pei-Yan Liu, Fang Ji, Xiao-Ming Liu, Dong-Yun Ouyang, Xian-Hui He
Cucurbitacin B (CuB), a potent antineoplastic agent of cucurbitacin triterpenoids, induces rapid disruption of actin cytoskeleton and aberrant cell cycle inhibiting carcinogenesis. However, the underlying molecular mechanism of such anticancer effects remains incompletely understood. In this study, we showed that CuB treatment rapidly induced vasodilator-stimulated phosphoprotein (VASP) phosphorylation (i.e. activation) at the Ser157 residue and generated VASP clumps which were co-localized with amorphous actin aggregates prior to the formation of highly-ordered cofilin-actin rods in melanoma cells...
2014: PloS One
Jianjie Mi, Alisa E Shaw, Chi W Pak, Keifer P Walsh, Laurie S Minamide, Barbara W Bernstein, Thomas B Kuhn, James R Bamburg
Filament bundles (rods) of cofilin and actin (1:1) form in neurites of stressed neurons where they inhibit synaptic function. Live-cell imaging of rod formation is hampered by the fact that overexpression of a chimera of wild type cofilin with a fluorescent protein causes formation of spontaneous and persistent rods, which is exacerbated by the photostress of imaging. The study of rod induction in living cells calls for a rod reporter that does not cause spontaneous rods. From a study in which single cofilin surface residues were mutated, we identified a mutant, cofilinR21Q, which when fused with monomeric Red Fluorescent Protein (mRFP) and expressed several fold above endogenous cofilin, does not induce spontaneous rods even during the photostress of imaging...
2013: PloS One
Yan-Ting Zhang, Dong-Yun Ouyang, Li-Hui Xu, Qing-Bing Zha, Xian-Hui He
Accumulating evidence indicates that cucurbitacin B (CuB), as well as other cucurbitacins, damages the actin cytoskeleton in a variety of cell types. However, the underlying mechanism of such an effect is not well understood. In this study, we showed that CuB rapidly induced actin aggregation followed by actin rod formation in melanoma cells. Cofilin, a critical regulator of actin dynamics, was dramatically dephosphorylated (i.e., activated) upon CuB treatment. Notably, the activated cofilin subsequently formed rod-like aggregates, which were highly colocalized with actin rods, indicating the formation of cofilin-actin rods...
October 2013: Journal of Cellular Biochemistry
János Kállmán, Magdolna Pákáski, Szabina Szucs, Sára Kálmán, Orsike Fazekas, Petra Santha, Gyula Szabó, Zoltán Janka, János Kálmán
Stress, depending on its level and quality, may cause adaptive and maladaptive alterations in brain functioning. As one of its multiple effects, elevated blood cortisol levels decrease the synthesis of the neuroprotective BDNF, thus leading to hippocampal atrophy and synapse loss, and rendering it a possible cause for the Alzheimer's disease (AD) related neuropathological and cognitive changes. As a result of the stress response, intraneuronal alterations--also affecting the metabolism of beta-actin--can develop...
November 30, 2012: Ideggyógyászati Szemle
Lise N Munsie, Ray Truant
The cofilin-actin rod stress response is an actin cytoskeletal dynamic arrest that occurs in cells under a variety of stress conditions. Upon stress, the rapidly activated cofilin saturates actin filaments causing them to bundle into rod structures in either the nucleus or cytoplasm, halting actin polymerization and thus freeing ATP. Importantly, these rods dissociate quickly following relief of the transient stress. The rods form inappropriately in neurons involved in the progression of Alzheimer disease (AD) and we have linked dysfunctional dynamics of the nuclear rod response to Huntington disease (HD)...
November 2012: Bioarchitecture
Ben Chen, Min Jiang, Mi Zhou, Lulan Chen, Xu Liu, Xin Wang, Yun Wang
Cofilin is the major actin-depolymerizing factor in the CNS for the regulation of actin dynamics. Neurodegenerative stimuli can induce the formation of cofilin rod, a pathological structure composed of cofilin and actin. The formation of cofilin rod was found to disrupt synapse function and cause neurite loss. The aim of the present study is to study the whole process of cofilin rod formation pattern in cultured hippocampal neurons under excitotoxic stimulation and to explore its underlying pharmacological mechanism...
November 27, 2012: Brain Research
Shuai Ren, Dong-Yun Ouyang, Mark Saltis, Li-Hui Xu, Qing-Bing Zha, Ji-Ye Cai, Xian-Hui He
PURPOSE: The cucurbitacins are a class of triterpenoid molecules that possess cytotoxic characteristics for plant defense against herbivore feeding. 23,24-dihydrocucurbitacin F (DHCF), a derivative of the cucurbitacin family, has been isolated as an active component from the root of Hemsleya amabilis (Cucurbitaceae), an ancient Chinese remedy for bacillary dysentery, gastroenteritis, and cancers. While the toxicity of other cucurbitacins has been explored in several cancers, little data exist on the effect of DHCF on human cancers, including prostate cancer (PCa)...
September 2012: Cancer Chemotherapy and Pharmacology
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