PLoS ONE · 2014 · 24 citations · 38 references
Life SciencesCell BiologyNeuroscienceCellular NeuroscienceMolecular NeurobiologyMolecular NeuroscienceNeural DevelopmentNeuronal Cell BiologyNeuronal DifferentiationNeuronal Gene ExpressionImmunohistochemical DetectionImmunohistochemical MarkersImmunohistochemical StainingNeuron-specific EnolasePodocyte BiologyPodocyte Foot Process EffacementSmall Interfering Rna ModificationsUbiquitin System
Growing evidence suggests that there are many common cell biological features shared by neurons and podocytes; however, the mechanism of podocyte foot process formation remains unclear. Comparing the mechanisms of process formation between two cell types should provide useful guidance from the progress of neuron research. Studies have shown that some mature proteins of podocytes, such as podocin, nephrin, and synaptopodin, were also expressed in neurons. In this study, using cell biological experiments and immunohistochemical techniques, we showed that some neuronal iconic molecules, such as Neuron-specific enolase, nestin and Neuron-specific nuclear protein, were also expressed in podocytes. We further inhibited the expression of Neuron-specific enolase, nestin, synaptopodin and Ubiquitin carboxy terminal hydrolase-1 by Small interfering RNA in cultured mouse podocytes and observed the significant morphological changes in treated podocytes. When podocytes were treated with Adriamycin, the protein expression of Neuron-specific enolase, nestin, synaptopodin and Ubiquitin carboxy terminal hydrolase-1 decreased over time. Meanwhile, the morphological changes in the podocytes were consistent with results of the Small interfering RNA treatment of these proteins. The data demonstrated that neuronal iconic proteins play important roles in maintaining and regulating the formation and function of podocyte processes.
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Peter Mündel, Jochen Reiser, Aimée Zúñiga et al. · Experimental Cell Research · 1997 · 879 citations
The Neuron-Specific Protein PGP 9.5 Is a Ubiquitin Carboxyl-Terminal Hydrolase
Keith D. Wilkinson, Keunmyoung Lee, Seema S. Deshpande et al. · Science · 1989 · 873 citations