ArticleMolecular biotechnology2012
Proteomic analysis of glycated proteins from streptozotocin-induced diabetic rat kidney.
Article in Molecular biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Protein modifications by advanced glycation end products (AGEs) in human clear cell renal cell carcinoma.Journal of translational medicine · 2025Article
- Proteomic Insight Reveals Elevated Levels of Albumin in Circulating Immune Complexes in Diabetic Plasma.Molecular & cellular proteomics : MCP · 2016Article
- Proteomics in India: the clinical aspect.Clinical proteomics · 2016Review
- Proteomic analysis of protease resistant proteins in the diabetic rat kidney.Molecular & cellular proteomics : MCP · 2013Article
- Proteomics and systems biology for understanding diabetic nephropathy.Journal of cardiovascular translational research · 2012Review
- Role of advanced glycation endproducts and glyoxalase I in diabetic peripheral sensory neuropathy.Translational research : the journal of laboratory and clinical medicine · 2012Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycation of proteins leading to formation of advanced glycation end products (AGEs) has been considered as one of the important causes of diabetic nephropathy. Therefore, in this study, glycated proteins were detected by anti-AGE antibodies from kidney of streptozotocin-induced diabetic rat showing nephropathic symptoms, by using two dimensional electrophoresis and western blot analysis. These glycated proteins were identified and characterized by using combination of peptide mass finger printing and tandem mass spectrometric approaches. Glycated proteins identified included proteins from metabolic pathways, oxidative stress, cell signaling, and transport. Several of the proteins modified by glycation were involved in glucose metabolism. The extent of glycation was higher in diabetes compared to control, in the glycated proteins that were common to both control and diabetic kidney. Two dimensional electrophoresis proteins profiling of glycated proteins suggest that four of the glycated proteins were significantly up regulated in diabetes.
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Registered trials
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