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Alpha Actinin 4

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Irina V. Ogneva – One of the best experts on this subject based on the ideXlab platform.

  • Relative contents of cytoskeletal proteins in the membrane (MF) and cytoplasmic (CF) fractions of cardiomyocytes with typical Western blot images.
    , 2018
    Co-Authors: Irina V. Ogneva, Sergey S. Loktev, Vladimir N. Sychev

    Abstract:

    (A) AlphaActinin-1. (B) AlphaActinin4. (C) Beta-actin. (D) Gamma-actin. (E) Beta-tubulin. (F) Desmin. “B”–basal control group, “V”–vivarium control group, “G”–ground control group (level marked by dotted line), “F”–flight group. *–p < 0.05 in comparison with group “G”. The values used to build graphs represented in the S1 Table. There were no changes in the cytoskeletal proteins contents in the membrane fraction of the cardiac tissue. In the cytoplasmic fraction, AlphaActinin-1 and AlphaActinin4 protein content decreased during space flight.

  • Relative contents of cytoskeletal proteins in the membrane (MF) and cytoplasmic (CF) fractions of lung cells with typical Western blot images.
    , 2018
    Co-Authors: Irina V. Ogneva, Sergey S. Loktev, Vladimir N. Sychev

    Abstract:

    (A) AlphaActinin-1. (B) AlphaActinin4. (C) Beta-actin. (D) Gamma-actin. (E) Beta-tubulin. (F) Desmin. “B”–basal control group, “V”–vivarium control group, “G”–ground control group (level marked by dotted line), “F”–flight group. The values used to build graphs represented in the S2 Table. There were no changes of cytoskeletal proteins contents in the membrane and cytoplasmic fractions of the lung tissue.

  • Possible role of non-muscle AlphaActinins in muscle cell mechanosensitivity.
    PloS one, 2014
    Co-Authors: Irina V. Ogneva, Nikolay S. Biryukov, Toomas A. Leinsoo, Irina M. Larina

    Abstract:

    The main hypothesis suggested that changes in the external mechanical load would lead to different deformations of the submembranous cytoskeleton and, as a result, dissociation of different proteins from its structure (induced by increased/decreased mechanical stress). The study subjects were fibers of the soleus muscle and cardiomyocytes of Wistar rats. Changes in external mechanical conditions were reconstructed by means of antiorthostatic suspension of the animals by their tails for 6, 12, 18, 24 and 72 hours. Transversal stiffness was measured by atomic force microscopy imaging; beta-, gamma-actin, AlphaActinin 1 and AlphaActinin 4 levels in membranous and cytoplasmic fractions were quantified by Western blot analysis; expression rates of the corresponding genes were studied using RT-PCR. Results: In 6 hours, AlphaActinin 1 and AlphaActinin 4 levels decreased in the membranous fraction of proteins of cardiomyocytes and soleus muscle fibers, respectively, but increased in the cytoplasmic fraction of the abovementioned cells. After 6–12 hours of suspension, the expression rates of beta-, gamma-actin, AlphaActinin 1 and AlphaActinin 4 were elevated in the soleus muscle fibers, but the AlphaActinin 1 expression rate returned to the reference level in 72 hours. After 18–24 hours, the expression rates of beta-actin and AlphaActinin 4 increased in cardiomyocytes, while the AlphaActinin 1 expression rate decreased in soleus muscle fibers. After 12 hours, the beta- and gamma-actin content dropped in the membranous fraction and increased in the cytoplasmic protein fractions from both cardiomyocytes and soleus muscle fibers. The stiffness of both cell types decreased after the same period of time. Further, during the unloading period the concentration of nonmuscle actin and different isoforms of AlphaActinins increased in the membranous fraction from cardiomyocytes. At the same time, the concentration of the abovementioned proteins decreased in the soleus muscle fibers.

Flaviu Bob – One of the best experts on this subject based on the ideXlab platform.

  • Urinary podocyte-associated mRNA levels correlate with proximal tubule dysfunction in early diabetic nephropathy of type 2 diabetes mellitus
    Diabetology & metabolic syndrome, 2017
    Co-Authors: Ligia Petrica, Sorin Ursoniu, Florica Gadalean, Adrian Vlad, Gheorghe Gluhovschi, Victor Dumitrascu, Daliborca Vlad, Cristina Gluhovschi, Silvia Velciov, Flaviu Bob

    Abstract:

    The study assessed mRNA expression of podocyte-associated molecules in urinary sediments of patients with type 2 diabetes mellitus (DM) in relation to urinary podocytes, biomarkers of podocyte injury and of proximal tubule (PT) dysfunction. A total of 76 patients with type 2 DM and 20 healthy subjects were enrolled in a cross-sectional study, and assessed concerning urinary podocytes, urinary mRNA of podocyte-associated genes, urinary biomarkers of podocyte damage and of PT dysfunction. We found significant differences between urinary mRNA of podocyte-associated molecules in relation with albuminuria stage. In multivariable regression analysis, urinary mRNA of nephrin, podocin, AlphaActinin4, CD2-associated protein, glomerular epithelial protein 1 (GLEPP1), ADAM 10, and NFκB correlated directly with urinary podocytes, albuminuria, urinary Alpha1-microglobulin, urinary kidney-injury molecule-1, nephrinuria, urinary vascular endothelial growth factor, urinary advanced glycation end-products (AGE), and indirectly with eGFR (p 

  • Urinary podocyte-associated mRNA levels correlate with proximal tubule dysfunction in early diabetic nephropathy of type 2 diabetes mellitus
    BMC, 2017
    Co-Authors: Ligia Petrica, Sorin Ursoniu, Florica Gadalean, Adrian Vlad, Gheorghe Gluhovschi, Victor Dumitrascu, Daliborca Vlad, Cristina Gluhovschi, Silvia Velciov, Flaviu Bob

    Abstract:

    Abstract Aim The study assessed mRNA expression of podocyte-associated molecules in urinary sediments of patients with type 2 diabetes mellitus (DM) in relation to urinary podocytes, biomarkers of podocyte injury and of proximal tubule (PT) dysfunction. Methods A total of 76 patients with type 2 DM and 20 healthy subjects were enrolled in a cross-sectional study, and assessed concerning urinary podocytes, urinary mRNA of podocyte-associated genes, urinary biomarkers of podocyte damage and of PT dysfunction. Results We found significant differences between urinary mRNA of podocyte-associated molecules in relation with albuminuria stage. In multivariable regression analysis, urinary mRNA of nephrin, podocin, AlphaActinin4, CD2-associated protein, glomerular epithelial protein 1 (GLEPP1), ADAM 10, and NFκB correlated directly with urinary podocytes, albuminuria, urinary Alpha1-microglobulin, urinary kidney-injury molecule-1, nephrinuria, urinary vascular endothelial growth factor, urinary advanced glycation end-products (AGE), and indirectly with eGFR (p 

Dmitri Tentler – One of the best experts on this subject based on the ideXlab platform.

  • Correction: Actin-binding protein AlphaActinin 4 (ACTN4) is a transcriptional co-activator of RelA/p65 sub-unit of NF-kB (vol 4, pg 362, 2013)
    Oncotarget, 2018
    Co-Authors: Vasilisa Aksenova, Karl-eric Magnusson, Mikhail Khotin, Eugene Tulchinsky, Gerry Melino, Nickolai A Barlev, Dmitri Tentler

    Abstract:

    [This corrects the article DOI: 10.18632/oncotarget.901.].

  • actin binding protein Alpha Actinin 4 actn4 is a transcriptional co activator of rela p65 sub unit of nf kb
    Oncotarget, 2013
    Co-Authors: Vasilisa Aksenova, G P Pinaev, Karl-eric Magnusson, L V Turoverova, Mikhail Khotin, Eugene Tulchinsky, Gerry Melino, Nickolai A Barlev, Dmitri Tentler

    Abstract:

    ACTN4 is an actin-binding protein that participates in cytoskeleton organisation. It resides both in the cytoplasm and nucleus and physically associates with various transcription factors. Here, we describe an effect of ACTN4 expression on transcriptional activity of the RelA/p65 subunit of NF-kB. We demonstrate that ACTN4 enhances RelA/p65-dependant expression of c-fos, MMP-3 and MMP-1 genes, but it does not affect TNC, ICAM1 and FN1 expression. Importantly, actin-binding domains of ACTN4 are not critical for the nuclear translocation and co-activation of RelA/p65- dependent transcription. Collectively, our data suggest that in the nucleus, ACTN4 functions as a selective transcriptional co-activator of RelA/p65.

  • actin binding protein Alpha Actinin 4 actn4 is a transcriptional co activator of rela p65 sub unit of nf kb
    Oncotarget, 2013
    Co-Authors: Vasilisa Aksenova, Karl-eric Magnusson, L V Turoverova, Mikhail Khotin, Eugene Tulchinsky, Gerry Melino, George P Pinaev, Nickolai A Barlev, Dmitri Tentler

    Abstract:

    // Vasilisa Aksenova 1,2 , Lidia Turoverova 1 , Mikhail Khotin 1 , Karl-Eric Magnusson 3 , Eugene Tulchinsky 4 , Gerry Melino 2,5 , George P. Pinaev 1 , Nickolai Barlev 1,2,6 , and Dmitri Tentler 1,2 1 Institute of Cytology, Russian Academy of Sciences, Tikhoretsky av., 4, St. Petersburg, Russia 2 Laboratory of Molecular Pharmacology, Saint-Petersburg Technological Institute, 26 Moskovsky Prospect, St. Petersburg, Russia 3 Division of Medical Microbiology, Department of Clinical and Experimental Medicine, Linkoping University, SE-581 85 Linkoping, Sweden 4 Department of Cancer Studies and Molecular Medicine, University of Leicester, RKCSB, LRI, Leicester, UK 5 MRC Toxicology Unit, Leicester, UK 6 Department of Biochemistry, University of Leicester, Lancaster Road, Leicester, UK Correspondence: Vasilisa Aksenova, email: // Dmitri Tentler, email: // Keywords : ACTN4, RelA/p65, transcription regulation, MMP Received : February 22, 2013 Accepted : February 26, 2013 Published : February 28, 2013 Abstract ACTN4 is an actin-binding protein that participates in cytoskeleton organisation. It resides both in the cytoplasm and nucleus and physically associates with various transcription factors. Here, we describe an effect of ACTN4 expression on transcriptional activity of the RelA/p65 subunit of NF-kB. We demonstrate that ACTN4 enhances RelA/p65-dependant expression of c- fos , MMP-3 and MMP-1 genes, but it does not affect TNC , ICAM1 and FN1 expression. Importantly, actin-binding domains of ACTN4 are not critical for the nuclear translocation and co-activation of RelA/p65-dependent transcription. Collectively, our data suggest that in the nucleus, ACTN4 functions as a selective transcriptional co-activator of RelA/p65.