ArticleJournal of ginseng research2014
Ginseng total saponin modulates the changes of α-actinin-4 in podocytes induced by diabetic conditions.
Article in Journal of ginseng research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Drying features of microwave and far-infrared combination drying on white ginseng slices.Food science and biotechnology · 2019Article
- Kidney-derived c-kitScientific reports · 2018Article
- Dissipation and residues of the diamide insecticide chlorantraniliprole in ginseng ecosystems under different cultivation environments.Environmental monitoring and assessment · 2017Article
- Montelukast improves the changes of cytoskeletal and adaptor proteins of human podocytes by interleukin-13.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2017Article
- Drying characteristics and quality of red ginseng using far-infrared rays.Journal of ginseng research · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe actin cytoskeleton in podocytes is essential for the maintenance of its normal structure and function. Its disruption is a feature of podocyte foot-process effacement and is associated with proteinuria. α-Actinin-4 in podocytes serves as a linker protein binding the actin filaments of the cytoskeleton.
methodsTo investigate the effect of ginseng total saponin (GTS) on the pathological changes of podocyte α-actinin-4 induced by diabetic conditions, we cultured mouse podocytes under normal glucose (5mM) or high glucose (HG, 30mM) conditions, with or without the addition of advanced glycosylation end products (AGE), and treated with GTS.
resultsIn confocal imaging, α-actinin-4 colocalized with the ends of F-actin fibers in cytoplasm, but diabetic conditions disrupted F-actin fibers and concentrated α-actinin-4 molecules at the peripheral cytoplasm. GTS upregulated α-actinin protein in a time- and dose-dependent manner, and suppressed the receptor for AGE levels in western blotting. Diabetic conditions, including HG, AGE, and both together, decreased cellular α-actinin-4 protein levels at 24 h and 48 h. Such quantitative and qualitative changes of α-actinin-4 protein induced by diabetic conditions were mitigated by GTS.
conclusionThese findings imply that both HG and AGE have an influence on the distribution and amount of α-actinin-4 in podocytes that can be recovered by GTS.
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