Partial colocalization of glucocorticoid and mineralocorticoid receptors in discrete compartments in nuclei of rat hippocampus neurons

Steensel, Bas van; Binnendijk, E.P. van; Hornsby, C. D.; Voort, H. T. M. van der; Krozowski, Zygmunt; Kloet, E. R. de; Driel, Roel van

doi:10.1242/jcs.109.4.787

Cited by 321 publications

(54 citation statements)

References 24 publications

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“…The results showed that Manders' coefficients had a higher overlap of S1R on AQP (M2): 0.458 ± 0.046 (AQP8) > 0.411 ± 0.04 (AQP3) > 0.307 ± 0.109 (AQP11) (Figure 8D-F). The cross-correlation analysis [52] showed bell-shaped curves (Figure S2) with the following CCF maxima values: 0.562 ± 0.129 (AQP11) > 0.453 ± 0.212 (AQP3) > 0.355 ± 0.021 (AQP8) (Figure 8D-F). Taken together, the results suggest at least a partial colocalization of S1R and AQPs, confirming that the herein used cellular model is suitable for studying the effect of S1R modulators on AQP-mediated antioxidant effect.…”

Section: Resultsmentioning

confidence: 98%

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Sigma-1 Receptor Agonists Acting on Aquaporin-Mediated H2O2 Permeability: New Tools for Counteracting Oxidative Stress

Pellavio

Rossino

Gastaldi

et al. 2021

IJMS

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Sigma1 Receptor (S1R) is involved in oxidative stress, since its activation is triggered by oxidative or endoplasmic reticulum stress. Since specific aquaporins (AQP), called peroxiporins, play a relevant role in controlling H2O2 permeability and ensure reactive oxygen species wasted during oxidative stress, we studied the effect of S1R modulators on AQP-dependent water and hydrogen peroxide permeability in the presence and in the absence of oxidative stress. Applying stopped-flow light scattering and fluorescent probe methods, water and hydrogen peroxide permeability in HeLa cells have been studied. Results evidenced that S1R agonists can restore water permeability in heat-stressed cells and the co-administration with a S1R antagonist totally counteracted the ability to restore the water permeability. Moreover, compounds were able to counteract the oxidative stress of HeLa cells specifically knocked down for S1R. Taken together these results support the hypothesis that the antioxidant mechanism is mediated by both S1R and AQP-mediated H2O2 permeability. The finding that small molecules can act on both S1R and AQP-mediated H2O2 permeability opens a new direction toward the identification of innovative drugs able to regulate cell survival during oxidative stress in pathologic conditions, such as cancer and degenerative diseases.

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Section: Resultsmentioning

confidence: 98%

“…To evaluate the colocalization, we used JACoP (just another Colocalization Plugin) from Fiji to quantify the Pearson's correlation coefficient r, Manders' colocalization coefficient (M1 and M2) and Van Steensel's Cross-correlation Function (CCF) of 3D images [50][51][52].…”

Section: Immunofluorescence Staining Confocal Microscopy and Colocalization Analysismentioning

confidence: 99%

Sigma-1 Receptor Agonists Acting on Aquaporin-Mediated H2O2 Permeability: New Tools for Counteracting Oxidative Stress

Pellavio

Rossino

Gastaldi

et al. 2021

IJMS

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“…5 , first column, merged image and line profile). To quantitatively evaluate the colocalization, we employed a cross-correlation function (CCF) analysis, which measures Pearson’s correlations by shifting the image of one fluorescence channel to the x-direction ( van Steensel et al, 1996 ; Fig. 5 , bottom row).…”

Section: Resultsmentioning

confidence: 99%

Live imaging of transcription sites using an elongating RNA polymerase II–specific probe

Uchino

Ito

Sato

et al. 2021

Journal of Cell Biology

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In eukaryotic nuclei, most genes are transcribed by RNA polymerase II (RNAP2), whose regulation is a key to understanding the genome and cell function. RNAP2 has a long heptapeptide repeat (Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7), and Ser2 is phosphorylated on an elongation form. To detect RNAP2 Ser2 phosphorylation (RNAP2 Ser2ph) in living cells, we developed a genetically encoded modification-specific intracellular antibody (mintbody) probe. The RNAP2 Ser2ph-mintbody exhibited numerous foci, possibly representing transcription “factories,” and foci were diminished during mitosis and in a Ser2 kinase inhibitor. An in vitro binding assay using phosphopeptides confirmed the mintbody’s specificity. RNAP2 Ser2ph-mintbody foci were colocalized with proteins associated with elongating RNAP2 compared with factors involved in the initiation. These results support the view that mintbody localization represents the sites of RNAP2 Ser2ph in living cells. RNAP2 Ser2ph-mintbody foci showed constrained diffusional motion like chromatin, but they were more mobile than DNA replication domains and p300-enriched foci, suggesting that the elongating RNAP2 complexes are separated from more confined chromatin domains.

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“…IRIF size was measured with a 2D Crosscorrelation plugin for ImageJ as described by Reindl et al 16 . It is based on the approach introduced by Van Steensel et al 45 using the Pearson correlation coefficient with the gray values for the i-th pixel in image A and image B, respectively, and the respective mean gray values. For size measurement, image B is a duplicate of image A, and the cross-correlation function is called the autocorrelation function (ACF).…”

Section: Methodsmentioning

confidence: 99%

Dosimetry of heavy ion exposure to human cells using nanoscopic imaging of double strand break repair protein clusters

Reindl

Kundrát

Girst

et al. 2022

Sci Rep

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The human body is constantly exposed to ionizing radiation of different qualities. Especially the exposure to high-LET (linear energy transfer) particles increases due to new tumor therapy methods using e.g. carbon ions. Furthermore, upon radiation accidents, a mixture of radiation of different quality is adding up to human radiation exposure. Finally, long-term space missions such as the mission to mars pose great challenges to the dose assessment an astronaut was exposed to. Currently, DSB counting using γH2AX foci is used as an exact dosimetric measure for individuals. Due to the size of the γH2AX IRIF of ~ 0.6 µm, it is only possible to count DSB when they are separated by this distance. For high-LET particle exposure, the distance of the DSB is too small to be separated and the dose will be underestimated. In this study, we developed a method where it is possible to count DSB which are separated by a distance of ~ 140 nm. We counted the number of ionizing radiation-induced pDNA-PKcs (DNA-PKcs phosphorylated at T2609) foci (size = 140 nm ± 20 nm) in human HeLa cells using STED super-resolution microscopy that has an intrinsic resolution of 100 nm. Irradiation was performed at the ion microprobe SNAKE using high-LET 20 MeV lithium (LET = 116 keV/µm) and 27 MeV carbon ions (LET = 500 keV/µm). pDNA-PKcs foci label all DSB as proven by counterstaining with 53BP1 after low-LET γ-irradiation where separation of individual DSB is in most cases larger than the 53BP1 gross size of about 0.6 µm. Lithium ions produce (1.5 ± 0.1) IRIF/µm track length, for carbon ions (2.2 ± 0.2) IRIF/µm are counted. These values are enhanced by a factor of 2–3 compared to conventional foci counting of high-LET tracks. Comparison of the measurements to PARTRAC simulation data proof the consistency of results. We used these data to develop a measure for dosimetry of high-LET or mixed particle radiation exposure directly in the biological sample. We show that proper dosimetry for radiation up to a LET of 240 keV/µm is possible.

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Partial colocalization of glucocorticoid and mineralocorticoid receptors in discrete compartments in nuclei of rat hippocampus neurons

Cited by 321 publications

References 24 publications

Sigma-1 Receptor Agonists Acting on Aquaporin-Mediated H2O2 Permeability: New Tools for Counteracting Oxidative Stress

Sigma-1 Receptor Agonists Acting on Aquaporin-Mediated H2O2 Permeability: New Tools for Counteracting Oxidative Stress

Live imaging of transcription sites using an elongating RNA polymerase II–specific probe

Dosimetry of heavy ion exposure to human cells using nanoscopic imaging of double strand break repair protein clusters

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