RhoA/ROCK downregulates FPR2-mediated NADPH oxidase activation in mouse bone marrow granulocytes

Filina, Julia; Gabdoulkhakova, Aida; Safronova, V. G.

doi:10.1016/j.cellsig.2014.05.017

Cited by 24 publications

(14 citation statements)

References 80 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The role of RhoA signaling cascades was further investigated using the cell permeable Rho inhibitor, CT04. CT04 is powerful for efficient inactivation of Rho GTPase in a variety of cultured cells (25). In the present study, PA-induced activation of RhoA was prevented by CT04.…”

Section: Discussionsupporting

confidence: 51%

c-Maf inducing protein inhibits cofilin-1 activity and alters podocyte cytoskeleton organization

Liu

et al. 2017

Molecular Medicine Reports

View full text Add to dashboard Cite

The glomerular visceral epithelial cells, also termed podocytes, are key in maintaining the normal renal filtration barrier. Although it has been demonstrated that stimulation of c‑Maf inducing protein (CMIP) expression is involved in podocyte damage, the molecular events during this process remain unclear. In the current study, CMIP‑induced proximal signaling was investigated by focusing on its effect on cofilin‑1 activity in puromycin aminonucleoside (PA)‑damaged podocytes. An obvious elevation of CMIP expression and phosphorylated (p) cofilin‑1 levels was detected in cultured podocytes treated with PA and in glomeruli isolated from PA‑induced nephropathy rats. Stable knockdown of CMIP prevented upregulation of p‑cofilin‑1 and reorganization of actin cytoskeleton in PA‑treated podocytes. The activity of the Src family kinase Fyn was reduced, whereas small GTPase Ras homolog gene family, member A (RhoA) activity was increased in PA‑treated podocytes. Stimulation of CMIP expression inhibited Fyn activation and decreased the expression level of p‑p190RhoGAP, a negative regulator of RhoA activity. The level of p‑LIM domain kinase 1 (LIMK1), a downstream effector of RhoA, increased significantly in PA‑treated podocytes. Notably, the applications of RhoA inhibitor or knockdown of LIMK prevented increase of the p‑cofilin‑1 level in PA‑treated podocytes. Thus, the current data provided evidence that the CMIP/Fyn/RhoA/cofilin‑1 signaling pathway may be associated with actin disorganization and podocyte foot process spreading following podocyte injury.

show abstract

Section: Discussionsupporting

confidence: 51%

c-Maf inducing protein inhibits cofilin-1 activity and alters podocyte cytoskeleton organization

Liu

et al. 2017

Molecular Medicine Reports

View full text Add to dashboard Cite

show abstract

“…RhoGTPases are interesting candidates to explain the structural cellular changes in microgravity 29 . As demonstrated in bone marrow polymorphonuclear leukocytes, RhoA activity not only responds within seconds upon stimulation, but is also associated with NADPH oxidase activation and oxidative burst reaction in time frames less than one minute 30 . In a previous study, repression of RhoA activation in bovine brain microvascular endothelial cells was observed after 72 h simulated microgravity (3D clinorotation), following down regulation of Rho-activating LARG (leukemia-associated Rho guanine nucleotide exchange factor) expression 31 .…”

Section: Discussionmentioning

confidence: 90%

Rapid adaptation to microgravity in mammalian macrophage cells

Thiel

Zélicourt

Tauber

et al. 2017

Sci Rep

View full text Add to dashboard Cite

Despite the observed severe effects of microgravity on mammalian cells, many astronauts have completed long term stays in space without suffering from severe health problems. This raises questions about the cellular capacity for adaptation to a new gravitational environment. The International Space Station (ISS) experiment TRIPLE LUX A, performed in the BIOLAB laboratory of the ISS COLUMBUS module, allowed for the first time the direct measurement of a cellular function in real time and on orbit. We measured the oxidative burst reaction in mammalian macrophages (NR8383 rat alveolar macrophages) exposed to a centrifuge regime of internal 0 g and 1 g controls and step-wise increase or decrease of the gravitational force in four independent experiments. Surprisingly, we found that these macrophages adapted to microgravity in an ultra-fast manner within seconds, after an immediate inhibitory effect on the oxidative burst reaction. For the first time, we provided direct evidence of cellular sensitivity to gravity, through real-time on orbit measurements and by using an experimental system, in which all factors except gravity were constant. The surprisingly ultra-fast adaptation to microgravity indicates that mammalian macrophages are equipped with a highly efficient adaptation potential to a low gravity environment. This opens new avenues for the exploration of adaptation of mammalian cells to gravitational changes.

show abstract

“…Previous research has shown that RhoGDIs can inactivate RHOA, resulting in the passive localization of RHOA to the cytoplasm, where it is sequestered and its activation or interaction with effectors are prevented 23 , 24 . To further prove whether CLOCK and BMAL1 can regulate the interaction between GDI and RHOA, Co-IP assays were employed, and the results revealed that CLOCK and BMAL1 reduced the interaction between RHOA and RhoGDI (Fig.…”

Section: Resultsmentioning

confidence: 99%

CLOCK and BMAL1 stabilize and activate RHOA to promote F-actin formation in cancer cells

Zhang

et al. 2018

Exp Mol Med

View full text Add to dashboard Cite

Circadian genes control most of the physiological functions in cancer cells, including cell proliferation, migration, and invasion. The CLOCK and BMAL1 complex plays a central role in circadian rhythms. Previous studies have shown that circadian genes may act as oncogenes or tumor-suppressor genes. In addition, F-actin, regulated by RHOA, has been shown to participate in tumor progression. However, the roles of the CLOCK and BMAL1 genes in the regulation of tumor progression via the RHOA-ROCK-CFL pathway remain largely unclear. Here we first indicate that the rearrangement of F-actin is regulated by CLOCK and BMAL1. We found that CLOCK and BMAL1 can upregulate RHOA expression by inhibiting CUL3-mediated ubiquitination and activate RHOA by reducing the interaction between RHOA and RhoGDI. Consequently, CLOCK and BMAL1 control the expression of the components of the RHOA-ROCK-CFL pathway, which alters the dynamics of F-actin/G-actin turnover and promotes cancer cell proliferation, migration, and invasion. In conclusion, our research proposes a novel insight into the role of CLOCK and BMAL1 in tumor cells.

show abstract

RhoA/ROCK downregulates FPR2-mediated NADPH oxidase activation in mouse bone marrow granulocytes

Cited by 24 publications

References 80 publications

c-Maf inducing protein inhibits cofilin-1 activity and alters podocyte cytoskeleton organization

c-Maf inducing protein inhibits cofilin-1 activity and alters podocyte cytoskeleton organization

Rapid adaptation to microgravity in mammalian macrophage cells

CLOCK and BMAL1 stabilize and activate RHOA to promote F-actin formation in cancer cells

Contact Info

Product

Resources

About