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Irina V. Ogneva - One of the best experts on this subject based on the ideXlab platform.
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Relative contents of cytoskeletal proteins in the membrane (MF) and cytoplasmic (CF) fractions of cardiomyocytes with typical Western blot images.
2018Co-Authors: Irina V. Ogneva, Sergey S. Loktev, Vladimir N. SychevAbstract:(A) Alpha-Actinin-1. (B) Alpha-Actinin-4. (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, Alpha-Actinin-1 and Alpha-Actinin-4 protein content decreased during space flight.
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Relative contents of cytoskeletal proteins in the membrane (MF) and cytoplasmic (CF) fractions of lung cells with typical Western blot images.
2018Co-Authors: Irina V. Ogneva, Sergey S. Loktev, Vladimir N. SychevAbstract:(A) Alpha-Actinin-1. (B) Alpha-Actinin-4. (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.
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Possible role of non-muscle Alpha-Actinins in muscle cell mechanosensitivity.
PloS one, 2014Co-Authors: Irina V. Ogneva, Nikolay S. Biryukov, Toomas A. Leinsoo, Irina M. LarinaAbstract: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, Alpha-Actinin 1 and Alpha-Actinin 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, Alpha-Actinin 1 and Alpha-Actinin 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, Alpha-Actinin 1 and Alpha-Actinin 4 were elevated in the soleus muscle fibers, but the Alpha-Actinin 1 expression rate returned to the reference level in 72 hours. After 18–24 hours, the expression rates of beta-actin and Alpha-Actinin 4 increased in cardiomyocytes, while the Alpha-Actinin 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 Alpha-Actinins increased in the membranous fraction from cardiomyocytes. At the same time, the concentration of the abovementioned proteins decreased in the soleus muscle fibers.
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Structure and functional characteristics of rat's left ventricle cardiomyocytes under antiorthostatic suspension of various duration and subsequent reloading.
Journal of biomedicine & biotechnology, 2012Co-Authors: Irina V. Ogneva, Nikolay S. Biryukov, T. M. Mirzoev, O. M. Veselova, Irina M. LarinaAbstract:The goal of the research was to identify the structural and functional characteristics of the rat's left ventricle under antiorthostatic suspension within 1, 3, 7 and 14 days, and subsequent 3 and 7-day reloading after a 14-day suspension. The transversal stiffness of the cardiomyocyte has been determined by the atomic force microscopy, cell respiration—by polarography and proteins content—by Western blotting. Stiffness of the cortical cytoskeleton increases as soon as one day after the suspension and increases up to the 14th day, and starts decreasing during reloading, reaching the control level after 7 days. The stiffness of the contractile apparatus and the intensity of cell respiration also increases. The content of non-muscle isoforms of actin in the cytoplasmic fraction of proteins does not change during the whole experiment, as does not the beta-actin content in the membrane fraction. The content of gamma-actin in the membrane fraction correlates with the change in the transversal stiffness of the cortical cytoskeleton. Increased content of Alpha-Actinin-1 and Alpha-Actinin-4 in the membrane fraction of proteins during the suspension is consistent with increased gamma-actin content there. The opposite direction of change of Alpha-Actinin-1 and Alpha-Actinin-4 content suggests their involvement into the signal pathways.
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Transversal stiffness and beta-actin and Alpha-Actinin-4 content of the M. soleus fibers in the conditions of a 3-day reloading after 14-day gravitational unloading.
Journal of biomedicine & biotechnology, 2011Co-Authors: Irina V. OgnevaAbstract:The aim of the work was to analyze the structural changes in different parts of the sarcolemma and contractile apparatus of muscle fibers by measuring their transversal stiffness by atomic force microscopy in a three-day reloading after a 14-day gravity disuse, which was carried out by hind-limbs suspension. The object of the study was the soleus muscle of the Wistar rat. It was shown that after 14 days of disuse, there was a reduction of transversal stiffness of all points of the sarcolemma and contractile apparatus. Readaptation for 3 days leads to complete recovery of the values of the transversal stiffness of the sarcolemma and to partial value recovery of the contractile apparatus. The changes in transversal stiffness of sarcolemma correlate with beta-actin and Alpha-Actinin-4 in membrane protein fractions.
Flaviu Bob - One of the best experts on this subject based on the ideXlab platform.
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Urinary podocyte-associated mRNA levels correlate with proximal tubule dysfunction in early diabetic nephropathy of type 2 diabetes mellitus
Diabetology & metabolic syndrome, 2017Co-Authors: Ligia Petrica, Sorin Ursoniu, Florica Gadalean, Adrian Vlad, Gheorghe Gluhovschi, Victor Dumitrascu, Daliborca Vlad, Cristina Gluhovschi, Silvia Velciov, Flaviu BobAbstract: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, Alpha-Actinin-4, 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
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Urinary podocyte-associated mRNA levels correlate with proximal tubule dysfunction in early diabetic nephropathy of type 2 diabetes mellitus
BMC, 2017Co-Authors: Ligia Petrica, Sorin Ursoniu, Florica Gadalean, Adrian Vlad, Gheorghe Gluhovschi, Victor Dumitrascu, Daliborca Vlad, Cristina Gluhovschi, Silvia Velciov, Flaviu BobAbstract: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, Alpha-Actinin-4, 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.
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Correction: Actin-binding protein Alpha-Actinin 4 (ACTN4) is a transcriptional co-activator of RelA/p65 sub-unit of NF-kB (vol 4, pg 362, 2013)
Oncotarget, 2018Co-Authors: Vasilisa Aksenova, Karl-eric Magnusson, Mikhail Khotin, Eugene Tulchinsky, Gerry Melino, Nickolai A Barlev, Dmitri TentlerAbstract:[This corrects the article DOI: 10.18632/oncotarget.901.].
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actin binding protein Alpha Actinin 4 actn4 is a transcriptional co activator of rela p65 sub unit of nf kb
Oncotarget, 2013Co-Authors: Vasilisa Aksenova, Karl-eric Magnusson, L V Turoverova, Mikhail Khotin, Eugene Tulchinsky, Gerry Melino, George P Pinaev, Nickolai A Barlev, Dmitri TentlerAbstract:// 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.
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Actin-binding protein Alpha-Actinin 4 (ACTN4) is a transcriptional co-activator of RelA/p65 sub-unit of NF-kB.
Oncotarget, 2013Co-Authors: Vasilisa Aksenova, Karl-eric Magnusson, Mikhail Khotin, Eugene Tulchinsky, Gerry Melino, Nickolai A Barlev, Dmitri TentlerAbstract:// 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.
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actin binding protein Alpha Actinin 4 actn4 is a transcriptional co activator of rela p65 sub unit of nf kb
Oncotarget, 2013Co-Authors: Vasilisa Aksenova, G P Pinaev, Karl-eric Magnusson, L V Turoverova, Mikhail Khotin, Eugene Tulchinsky, Gerry Melino, Nickolai A Barlev, Dmitri TentlerAbstract: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.
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Proteomic analysis of ACTN4-interacting proteins reveals it's a putative involvement in mRNA metabolism.
Biochemical and biophysical research communications, 2010Co-Authors: Mikhail Khotin, Karl-eric Magnusson, Vasilisa Aksenova, N A Barlev, Veronika Borutinskaite, Alexander V. Vener, Olga Bajenova, Dmitri TentlerAbstract:Alpha-Actinin 4 (ACTN4) is an actin-binding protein. In the cytoplasm, ACTN4 participates in structural organisation of the cytoskeleton via cross-linking of actin filaments. Nuclear localisation of ACTN4 has also been reported, but no clear role in the nucleus has been established. In this report, we describe the identification of proteins associated with ACTN4 in the nucleus. A combination of two-dimensional gel electrophoresis (2D-GE) and MALDI-TOF mass-spectrometry revealed a large number of ACTN4-bound proteins that are involved in various aspects of mRNA processing and transport. The association of ACTN4 with different ribonucleoproteins suggests that a major function of nuclear ACTN4 may be regulation of mRNA metabolism and signaling.
Irina M. Larina - One of the best experts on this subject based on the ideXlab platform.
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Possible role of non-muscle Alpha-Actinins in muscle cell mechanosensitivity.
PloS one, 2014Co-Authors: Irina V. Ogneva, Nikolay S. Biryukov, Toomas A. Leinsoo, Irina M. LarinaAbstract: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, Alpha-Actinin 1 and Alpha-Actinin 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, Alpha-Actinin 1 and Alpha-Actinin 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, Alpha-Actinin 1 and Alpha-Actinin 4 were elevated in the soleus muscle fibers, but the Alpha-Actinin 1 expression rate returned to the reference level in 72 hours. After 18–24 hours, the expression rates of beta-actin and Alpha-Actinin 4 increased in cardiomyocytes, while the Alpha-Actinin 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 Alpha-Actinins increased in the membranous fraction from cardiomyocytes. At the same time, the concentration of the abovementioned proteins decreased in the soleus muscle fibers.
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Structure of the cortical cytoskeleton of the left cardiac ventricle hystiocytes and of soleus muscle fibers in rats following short-time suspension
Aviakosmicheskaia i ekologicheskaia meditsina = Aerospace and environmental medicine, 2014Co-Authors: Ogneva, Irina M. LarinaAbstract:Purpose of the investigation was to examine structural rearrangements in the cortical cytoskeleton as a result of changes in external mechanic conditions. Objects of the investigation were Wistar rat's m. soleus fibers and left ventricle hystiocytes. Suspension for 6, 12, 18, 24 and 72 hours was performed according to the Ilyin-Novikov procedure modified by Morey-Holton. Cell stiffness, non-muscle actin and actin-binding proteins in the protein membrane and cytoplasmic fractions, and respective gene expression were evaluated. In addition, corticosterone levels were measured in blood serum. After 6 hours of suspension, actin-binding proteins went down in the membrane fraction, i.e. Alpha-Actinin-1 decreased in hystiocytes and Alpha-Actinin-4 in m. soleus fibers. On the contrary, their content in the cytoplasmatic fraction increased. Expression of genes coding beta- and gamma-actin, Alpha-Actinin-1 and Alpha-Actinin-4 in m. soleus fibers showed a decrease. However, the apha-Actinin-1 gene regained its baseline expression rate in 72 hours. Following 18 to 24 hours of suspension, expression of the beta-actin and Alpha-Actinin-4 genes in hystiocytes grew in comparison with baseline values, while expression of Alpha-Actinin-1 gene decreased. After 12 hours of suspension, beta- and gamma-actin levels were reduced in membrane proteins and increased in cytoplasmatic proteins in hystiocytes and m. soleus fibers. Stiffness showed a decline in each type of cell. Further into suspension, membrane proteins of hystiocytes increased levels of non-muscle actin and actin-binding proteins, and stiffness of these cells. Levels of these proteins decreased in m. soleus fibers, as also did cell stiffness. Serum corticosterone hardly altered but was slightly increased after 6 hours of suspension.
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Structure and functional characteristics of rat's left ventricle cardiomyocytes under antiorthostatic suspension of various duration and subsequent reloading.
Journal of biomedicine & biotechnology, 2012Co-Authors: Irina V. Ogneva, Nikolay S. Biryukov, T. M. Mirzoev, O. M. Veselova, Irina M. LarinaAbstract:The goal of the research was to identify the structural and functional characteristics of the rat's left ventricle under antiorthostatic suspension within 1, 3, 7 and 14 days, and subsequent 3 and 7-day reloading after a 14-day suspension. The transversal stiffness of the cardiomyocyte has been determined by the atomic force microscopy, cell respiration—by polarography and proteins content—by Western blotting. Stiffness of the cortical cytoskeleton increases as soon as one day after the suspension and increases up to the 14th day, and starts decreasing during reloading, reaching the control level after 7 days. The stiffness of the contractile apparatus and the intensity of cell respiration also increases. The content of non-muscle isoforms of actin in the cytoplasmic fraction of proteins does not change during the whole experiment, as does not the beta-actin content in the membrane fraction. The content of gamma-actin in the membrane fraction correlates with the change in the transversal stiffness of the cortical cytoskeleton. Increased content of Alpha-Actinin-1 and Alpha-Actinin-4 in the membrane fraction of proteins during the suspension is consistent with increased gamma-actin content there. The opposite direction of change of Alpha-Actinin-1 and Alpha-Actinin-4 content suggests their involvement into the signal pathways.
Ligia Petrica - One of the best experts on this subject based on the ideXlab platform.
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Urinary podocyte-associated mRNA levels correlate with proximal tubule dysfunction in early diabetic nephropathy of type 2 diabetes mellitus
Diabetology & metabolic syndrome, 2017Co-Authors: Ligia Petrica, Sorin Ursoniu, Florica Gadalean, Adrian Vlad, Gheorghe Gluhovschi, Victor Dumitrascu, Daliborca Vlad, Cristina Gluhovschi, Silvia Velciov, Flaviu BobAbstract: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, Alpha-Actinin-4, 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
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Urinary podocyte-associated mRNA levels correlate with proximal tubule dysfunction in early diabetic nephropathy of type 2 diabetes mellitus
BMC, 2017Co-Authors: Ligia Petrica, Sorin Ursoniu, Florica Gadalean, Adrian Vlad, Gheorghe Gluhovschi, Victor Dumitrascu, Daliborca Vlad, Cristina Gluhovschi, Silvia Velciov, Flaviu BobAbstract: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, Alpha-Actinin-4, 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
