ArticleClinical proteomics2011
Morphological changes in diabetic kidney are associated with increased O-GlcNAcylation of cytoskeletal proteins including α-actinin 4.
Article in Clinical proteomics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 39 citations in OpenAlex.
- Post‑translational modifications in diabetic kidney disease (Review).International journal of molecular medicine · 2026Review
- The multifaceted modulations by dapagliflozin in preventing hyperglycemia-induced diabetic nephropathy through glucose transporters and PPARα.Journal of diabetes and metabolic disorders · 2025Article
- Glycosylation in kidney diseases.Precision clinical medicine · 2025Review
- Immunohistochemical Study onActa histochemica et cytochemica · 2025Review
- O-linked β-N-acetylglucosamine (O-GlcNAc) modification: Emerging pathogenesis and a therapeutic target of diabetic nephropathy.Diabetic medicine : a journal of the British Diabetic Association · 2025Review
- ER Stress-Perturbed Intracellular Protein O-GlcNAcylation Aggravates Podocyte Injury in Diabetes Nephropathy.International journal of molecular sciences · 2023Article
- O-GlcNAcylation: an important post-translational modification and a potential therapeutic target for cancer therapy.Molecular medicine (Cambridge, Mass.) · 2022Review
- Article
- Vitamin D suppresses cellular pathways of diabetes complication in liver.Iranian journal of basic medical sciences · 2019Article
- Protein O-GlcNAcylation Is Essential for the Maintenance of Renal Energy Homeostasis and FunctionJournal of the American Society of Nephrology : JASN · 2019Article
- Nutrient regulation of signaling and transcription.The Journal of biological chemistry · 2019Review
- High glucose reduces megalin-mediated albumin endocytosis in renal proximal tubule cells through protein kinase BThe Journal of biological chemistry · 2018Article
- Investigation of post-translational modifications in type 2 diabetes.Clinical proteomics · 2018Review
- Avocado oil induces long-term alleviation of oxidative damage in kidney mitochondria from type 2 diabetic rats by improving glutathione status.Journal of bioenergetics and biomembranes · 2017Article
- Podocyte-specific VEGF-a gain of function induces nodular glomerulosclerosis in eNOS null mice.Journal of the American Society of Nephrology : JASN · 2014Article
- Post-translational modification and regulation of actin.Current opinion in cell biology · 2013Review
- Effects on high cholesterol-fed to liver, retina, hippocampus, and Harderian gland in Goto-Kakizaki rat.International journal of clinical and experimental pathology · 2013Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
purposeThe objective of the present study is to identify proteins that change in the extent of the modification with O-linked N-acetylglucosamine (O-GlcNAcylation) in the kidney from diabetic model Goto-Kakizaki (GK) rats, and to discuss the relation between O-GlcNAcylation and the pathological condition in diabetes.
methodsO-GlcNAcylated proteins were identified by two-dimensional gel electrophoresis, immunoblotting and peptide mass fingerprinting. The level of O-GlcNAcylation of these proteins was examined by immunoprecipitation, immunoblotting and in situ Proximity Ligation Assay (PLA).
resultsO-GlcNAcylated proteins that changed significantly in the degree of O-GlcNAcylation were identified as cytoskeletal proteins (α-actin, α-tubulin, α-actinin 4, myosin) and mitochondrial proteins (ATP synthase β, pyruvate carboxylase). The extent of O-GlcNAcylation of the above proteins increased in the diabetic kidney. Immunofluorescence and in situ PLA studies revealed that the levels of O-GlcNAcylation of actin, α-actinin 4 and myosin were significantly increased in the glomerulus and the proximal tubule of the diabetic kidney. Immunoelectron microscopy revealed that immunolabeling of α-actinin 4 is disturbed and increased in the foot process of podocytes of glomerulus and in the microvilli of proximal tubules.
conclusionThese results suggest that changes in the O-GlcNAcylation of cytoskeletal proteins are closely associated with the morphological changes in the podocyte foot processes in the glomerulus and in microvilli of proximal tubules in the diabetic kidney. This is the first report to show that α-actinin 4 is O-GlcNAcylated. α-Actinin 4 will be a good marker protein to examine the relation between O-GlcNAcylation and diabetic nephropathy.
Identifiers
What Socratic holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.