Mechanisms of angiotensin II signaling on cytoskeleton of podocytes

Hsu, Hsiang-Hao; Hoffmann, Sigrid; Endlich, Nicole; Velić, Ana; Schwab, Albrecht; Weide, Thomas; Schlatter, Eberhard; Pavenstädt, Hermann

doi:10.1007/s00109-008-0399-y

Cited by 131 publications

(137 citation statements)

References 79 publications

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“…To further validate our findings, another podocyte cell culture injury model was used that utilized Ang II as the injuryinducing agent (36). Untransduced or transduced podocytes with TAT-Neph1CD were subjected to Ang II (100 nM) treatment in a time-dependent fashion (Fig.…”

Section: Transduction Of Tat-neph1cd Protects Podocytes From Panand Amentioning

confidence: 68%

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Slit Diaphragm Protein Neph1 and Its Signaling

Arif

Rathore

Kumari

et al. 2014

Journal of Biological Chemistry

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Background: Neph1 is a podocyte protein that is critical for maintaining renal function. Results: Inhibiting Neph1 signaling preserves podocyte structure and function in response to glomerular injury-inducing agents. Conclusion: Maintaining a robust expression of Neph1 at the podocyte cell membrane protects podocytes from renal injury. Significance: This is the first report demonstrating that Neph1 signaling is a therapeutic target for preventing podocyte damage.

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Section: Transduction Of Tat-neph1cd Protects Podocytes From Panand Amentioning

confidence: 68%

“…Angiotensin II (Ang II) Treatment-The culture human podocytes (at 90% confluency) were treated with Ang II (100 nM) for a period of 48 h to induce injury (36). After treatment, the podocytes were fixed with 4% PFA and labeled with the desired antibodies and analyzed by immunofluorescence.…”

Section: Methodsmentioning

confidence: 99%

Slit Diaphragm Protein Neph1 and Its Signaling

Arif

Rathore

Kumari

et al. 2014

Journal of Biological Chemistry

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“…Moreover, AngII induces a shift of the podocyte phenotype from a dynamically stable type to an adaptively migratory type. This is conferred among others via the influence on the actin cytoskeleton (12).…”

Section: Discussionmentioning

confidence: 99%

“…Upon receptor activation via AngII stimulation, the intracellular C terminus of AT1R couples to G proteins, such as G q/11 , G i , G 12 , and G 13 , thereby inducing various second messenger pathways, such as PLC/inositol trisphosphate, reactive oxygen species, calcium, and protein kinase signaling (10,11). It has also been shown that AngII has direct effects on the actin cytoskeleton rearrangement of podocytes.…”

mentioning

confidence: 99%

“…It has also been shown that AngII has direct effects on the actin cytoskeleton rearrangement of podocytes. The integrity of the actin cytoskeleton is important for the physiologic function of podocytes, and actin cytoskeleton deregulation may result in podocyte disease (12); however, the molecular details of AngII-dependent signaling cascades in podocytes are not yet fully understood. In this study, we focused on AT1R-mediated protein kinase signaling and investigated which phosphorylation sites were regulated during short-term treatment with AngII in AT1R-expressing human podocytes.…”

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confidence: 99%

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Angiotensin II regulates phosphorylation of actin‐associated proteins in human podocytes

et al. 2017

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Within the kidney, angiotensin II (AngII) targets different cell types in the vasculature, tubuli, and glomeruli. An important part of the renal filtration barrier is composed of podocytes with their actin-rich foot processes. In this study, we used stable isotope labeling with amino acids in cell culture coupled to mass spectrometry to characterize relative changes in the phosphoproteome of human podocytes in response to short-term treatment with AngII. In 4 replicates, we identified a total of 17,956 peptides that were traceable to 2081 distinct proteins. Bioinformatic analyses revealed that among the increasingly phosphorylated peptides are predominantly peptides that are related to actin filaments, cytoskeleton, lamellipodia, mammalian target of rapamycin, and MAPK signaling. Among others, this screening approach highlighted the increased phosphorylation of actin-bundling protein, L-plastin (LCP1). AngII-dependent phosphorylation of LCP1 in cultured podocytes was mediated by the kinases ERK, p90 ribosomal S6 kinase, PKA, or PKC. LCP1 phosphorylation increased filopodia formation. In addition, treatment with AngII led to LCP1 redistribution to the cell margins, membrane ruffling, and formation of lamellipodia. Our data highlight the importance of AngII-triggered actin cytoskeleton-associated signal transduction in

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Hydrogen peroxide induces dimerization of protein kinase G type Iα subunits and increases albumin permeability in cultured rat podocytes

Piwkowska

Rogacka

Jankowski

et al. 2011

Journal Cellular Physiology

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Podocytes help regulate filtration barrier permeability in the kidneys. They express contractile proteins that are characteristic of smooth muscle cells as well as receptors for vasoactive factors such as angiotensin II and atrial natriuretic peptide (ANP). The later one generates intracellular cGMP, with subsequent activation of cGMP-dependent protein kinase; PKG (isoform PKGIα and PKGIβ). In this study, we asked whether hydrogen peroxide (H(2)O(2)), a physiological vasorelaxing factor, affected podocyte permeability and the podoctye PKGIα signaling pathway. Expression of PKGIα was confirmed in cultured rat podocytes using RT-PCR, immunofluorescence, and Western blotting. Exposure of podocytes to exogenous H(2)O(2) (100 µM) in non-reducing conditions increased the formation of PKGIα interprotein disulfide bonds, affected the phosphorylation of PKG target proteins, namely MYPT1 (maximal increase of about 57% at 30 min) and MLC (maximal decrease of about 62% at 10 min). Furthermore, H(2)O(2) increased the permeability of a layer of podocytes to albumin: Transmembrane flux for albumin increased five-fold (106.6 ± 5.2 µg/ml vs. 20.2 ± 2.5 µg/ml, P < 0.05, n = 5), and the PKG inhibitor Rp-8-Br-cGMPS (100 µM) prevented the flux increase. These data suggest that oxidative modulation of PKGIα in podocytes plays an important

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Mechanisms of angiotensin II signaling on cytoskeleton of podocytes

Cited by 131 publications

References 79 publications

Slit Diaphragm Protein Neph1 and Its Signaling

Slit Diaphragm Protein Neph1 and Its Signaling

Angiotensin II regulates phosphorylation of actin‐associated proteins in human podocytes

Hydrogen peroxide induces dimerization of protein kinase G type Iα subunits and increases albumin permeability in cultured rat podocytes

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