Intermediate vimentin filaments and their role in intracellular organelle distribution

Минин, А. А.; Moldaver, M. V.

doi:10.1134/s0006297908130063

Cited by 54 publications

(40 citation statements)

References 128 publications

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“…18 To assess HTM cell viability, we stained transduced HTM cells with trypan blue, and we counted only cells excluding the dye by using a disposable hemocytometer. We observed a significant decrease in the number of cells transduced with p.Cys268Phe and p.Glu373Ala ( Figure 4C).…”

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confidence: 99%

Mutations in DDX58, which Encodes RIG-I, Cause Atypical Singleton-Merten Syndrome

Jang

Kim

Now

et al. 2015

The American Journal of Human Genetics

188

165

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Singleton-Merten syndrome (SMS) is an autosomal-dominant multi-system disorder characterized by dental dysplasia, aortic calcification, skeletal abnormalities, glaucoma, psoriasis, and other conditions. Despite an apparent autosomal-dominant pattern of inheritance, the genetic background of SMS and information about its phenotypic heterogeneity remain unknown. Recently, we found a family affected by glaucoma, aortic calcification, and skeletal abnormalities. Unlike subjects with classic SMS, affected individuals showed normal dentition, suggesting atypical SMS. To identify genetic causes of the disease, we performed exome sequencing in this family and identified a variant (c.1118A>C [p.Glu373Ala]) of DDX58, whose protein product is also known as RIG-I. Further analysis of DDX58 in 100 individuals with congenital glaucoma identified another variant (c.803G>T [p.Cys268Phe]) in a family who harbored neither dental anomalies nor aortic calcification but who suffered from glaucoma and skeletal abnormalities. Cys268 and Glu373 residues of DDX58 belong to ATP-binding motifs I and II, respectively, and these residues are predicted to be located closer to the ADP and RNA molecules than other nonpathogenic missense variants by protein structure analysis. Functional assays revealed that DDX58 alterations confer constitutive activation and thus lead to increased interferon (IFN) activity and IFN-stimulated gene expression. In addition, when we transduced primary human trabecular meshwork cells with c.803G>T (p.Cys268Phe) and c.1118A>C (p.Glu373Ala) mutants, cytopathic effects and a significant decrease in cell number were observed. Taken together, our results demonstrate that DDX58 mutations cause atypical SMS manifesting with variable expression of glaucoma, aortic calcification, and skeletal abnormalities without dental anomalies.

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confidence: 99%

Mutations in DDX58, which Encodes RIG-I, Cause Atypical Singleton-Merten Syndrome

Jang

Kim

Now

et al. 2015

The American Journal of Human Genetics

188

165

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“…Molecular interaction studies demonstrated that purified synemin interacts with desmin, vimentin and ␣ -actinin. Transfection studies indicate that synemin requires the presence of another IF, such as vimentin, to assemble into an IF [Minin and Moldaver, 2008]. The transient co-localisation of synemin and vimentin within the area of the Balbiani body of quail oocytes supports this idea.…”

Section: Discussionmentioning

confidence: 85%

“…Recent studies demonstrated that interactions with vimentin filaments affect the motility, distribution and anchorage of mitochondria within the cytoplasm [Minin and Moldaver, 2008]. In cells lacking vimentin filaments, the normal distribution of mitochondria within the cytoplasm becomes disrupted, and the intracellular motility of mitochondria appears increased relative to control cells that express a normal vimentin network.…”

Section: Discussionmentioning

confidence: 99%

Expression of Intermediate Filaments in the Balbiani Body and Ovarian Follicular Wall of the Japanese Quail <b><i>(Coturnix japonica)</i></b>

Rodler¹,

Sinowatz²

2013

Cells Tissues Organs

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In the present study, we examined the distribution of 6 groups of intermediate filaments (IFs; cytokeratins, CKs, vimentin, synemin, desmin, glial fibrillary acidic protein and lamins) in oocytes and follicular walls of the Japanese quail (Coturnix japonica) during their development using immunohistochemical and ultrastructural techniques. A distinctly vimentin- and synemin-positive Balbiani body, which is a transient accumulation of organelles (mitochondria, Golgi complex and endoplasmic reticulum) that occurs in the oocytes of all vertebrates including birds, could be detected in the oocytes of primordial and early pre-vitellogenic follicles. In larger pre-vitellogenic follicles, the Balbiani body has dispersed and the positivity of the granulosa cells appeared to concentrate in the basal portion of their cytoplasm. Our ultrastructural data demonstrated that the matrix of the Bal-biani body consists of fine IFs, which may play a role in the formation and dispersion of the Balbiani body. Of the CKs studied (panCK, CK5, CK7, CK8, CK14, CK15, CK18 and CK19), only CK5 showed a slight positive staining in both the theca externa and the Balbiani bodies of pre-vitellogenic oocytes. In conclusion, our data, which describe the changes in avian IF protein expression during folliculogenesis, suggest that the functions of the IFs (vimentin and synemin) of oocytes and follicular walls are not primarily mechanical but may be involved in the transient tethering of mitochondria in the area of the Balbiani body and in the gain of endocrine competence during the differentiation of granulosa cells.

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“…Consequently, the hGSTO1-induced Prx2 expression in response to the oxidative stress requires further study. Vimentin is the most widely expressed intermediate filament protein (Minin and Moldaver 2008). Vimentin is involved in cell migration, cell contact, scaffolding as well as regulation of signal transduction pathways including the MAP kinase ERK pathway (Chernoivanenko et al 2013).…”

Section: A B Discussionmentioning

confidence: 99%

Proteomic analysis of human glutathione transferase omega (hGSTO1) stable transfection in a 6-hydroxydopamine-induced neuronal cells

Wongtrakul

Saisawang²,

Kumrapich³

et al. 2018

gpb

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Abstract.Parkinson's disease is the second most common neurodegenerative disorder after Alzheimer's disease. The disease is associated with dopaminergic neuron losses in the substantia nigra area of the brain and the formation of cytoplasmic inclusion bodies. Human glutathione transferase omega 1 (hGSTO1) appears to have a role in modulating stress response. The study was aimed to elucidate differentially expressed proteins caused by oxidative stress induced by 6-hydroxydopamine (6-OHDA). Human neuronal cells SH-SY5Y overexpressing hGSTO1 were used to investigate protein glutathionylation and the modulation of cellular protein expression. Therefore SH-SY5Y/hGSTO1 and SH-SY5Y/control lysate proteins were separated by 2D-gel electrophoresis compared with untreated conditions in both standard and non-reducing conditions. In standard conditions, the analysis of protein profiles demonstrated 25 differentially expressed spots and 10 spots were chosen for further protein identification by LC-MS analysis. Several proteins were later identified as vimentin, galectin-1, high mobility group protein B2, clathrin, tropomyosin, heterogenous nuclear ribonucleoprotein and peroxiredoxin-2. Search Tool for Interactions of Chemicals (STITCH) analysis suggested that oxidative stress induced by 6-OHDA involved carbohydrate metabolism in SH-SY5Y via a lactose metabolic pathway. Our results raise the possibility that hGSTO1 modulates the functions of many proteins that play a role in the degenerative cell response of a Parkinson's model.

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Intermediate vimentin filaments and their role in intracellular organelle distribution

Cited by 54 publications

References 128 publications

Mutations in DDX58, which Encodes RIG-I, Cause Atypical Singleton-Merten Syndrome

Mutations in DDX58, which Encodes RIG-I, Cause Atypical Singleton-Merten Syndrome

Expression of Intermediate Filaments in the Balbiani Body and Ovarian Follicular Wall of the Japanese Quail <b><i>(Coturnix japonica)</i></b>

Proteomic analysis of human glutathione transferase omega (hGSTO1) stable transfection in a 6-hydroxydopamine-induced neuronal cells

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