β-Catenin and its alteration in an experimental model of diabetic nephropathy

Se Jin Park, Eun Mi Ahn, Tae Sun Ha, Jaeil Shin

Research output: Contribution to journalArticle

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Abstract

Introduction. The aim of our study was to determine whether β-catenin, a subunit of the cadherin protein complex in the podocyte cytoskeleton, would be altered by hyperglycemia and advanced glycation endproducts (AGE) in glomerular epithelial cells and podocytes in vitro. Materials and Methods. Rat glomerular epithelial cells and mouse podocytes on bovine serum albumin-coated or AGE-coated plates with normal (5 mM) and high (30 mM) glucose doses were cultured and examined for the distribution of β-catenin using confocal microscopy and changes in β-catenin production by western blotting and reverse transcription-polymerase chain reaction, at 48 hours, 4 weeks, and 10 weeks. Results. Immunofluorescent staining revealed that β-catenin and α-actinin were colocalized around the cell membrane, and that β-catenin staining was most intense along the capillary loops, but moved internally toward the inner actin filaments in the presence of AGE and hyperglycemia. In western blot analysis, AGE and hyperglycemia significantly decreased the amount of β-catenin proteins by 31.5% at 48 hours, compared with normal control conditions (P <.01). The expression for β-catenin mRNA in AGE and hyperglycemia was also decreased by 59.6% at 24 hours, compared with that of normal glucose conditions (P <.01). No significant changes were seen in the osmotic controls. Conclusions. Our results suggest that AGE and hyperglycemia may induce the cytoplasmic redistribution of β-catenin and inhibit the production of β-catenin at the transcriptional and posttranslational levels, which may result in the development of kidney dysfunction in diabetic conditions.

Original languageEnglish
Pages (from-to)299-309
Number of pages11
JournalIranian Journal of Kidney Diseases
Volume8
Issue number4
Publication statusPublished - 2014 Jan 1

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Catenins
Diabetic Nephropathies
Theoretical Models
Hyperglycemia
Podocytes
Western Blotting
Epithelial Cells
Staining and Labeling
Actinin
Glucose
Protein Subunits
Cadherins
Bovine Serum Albumin
Cytoskeleton
Actin Cytoskeleton
Confocal Microscopy
Reverse Transcription
Cell Membrane
Kidney
Polymerase Chain Reaction

All Science Journal Classification (ASJC) codes

  • Nephrology

Cite this

Park, Se Jin ; Ahn, Eun Mi ; Ha, Tae Sun ; Shin, Jaeil. / β-Catenin and its alteration in an experimental model of diabetic nephropathy. In: Iranian Journal of Kidney Diseases. 2014 ; Vol. 8, No. 4. pp. 299-309.
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abstract = "Introduction. The aim of our study was to determine whether β-catenin, a subunit of the cadherin protein complex in the podocyte cytoskeleton, would be altered by hyperglycemia and advanced glycation endproducts (AGE) in glomerular epithelial cells and podocytes in vitro. Materials and Methods. Rat glomerular epithelial cells and mouse podocytes on bovine serum albumin-coated or AGE-coated plates with normal (5 mM) and high (30 mM) glucose doses were cultured and examined for the distribution of β-catenin using confocal microscopy and changes in β-catenin production by western blotting and reverse transcription-polymerase chain reaction, at 48 hours, 4 weeks, and 10 weeks. Results. Immunofluorescent staining revealed that β-catenin and α-actinin were colocalized around the cell membrane, and that β-catenin staining was most intense along the capillary loops, but moved internally toward the inner actin filaments in the presence of AGE and hyperglycemia. In western blot analysis, AGE and hyperglycemia significantly decreased the amount of β-catenin proteins by 31.5{\%} at 48 hours, compared with normal control conditions (P <.01). The expression for β-catenin mRNA in AGE and hyperglycemia was also decreased by 59.6{\%} at 24 hours, compared with that of normal glucose conditions (P <.01). No significant changes were seen in the osmotic controls. Conclusions. Our results suggest that AGE and hyperglycemia may induce the cytoplasmic redistribution of β-catenin and inhibit the production of β-catenin at the transcriptional and posttranslational levels, which may result in the development of kidney dysfunction in diabetic conditions.",
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β-Catenin and its alteration in an experimental model of diabetic nephropathy. / Park, Se Jin; Ahn, Eun Mi; Ha, Tae Sun; Shin, Jaeil.

In: Iranian Journal of Kidney Diseases, Vol. 8, No. 4, 01.01.2014, p. 299-309.

Research output: Contribution to journalArticle

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