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1.
Fig 7

Fig 7. From: Nucleophosmin, a Critical Bax Cofactor in Ischemia-Induced Cell Death.

(A and B) Effect of NPM siRNA on NPM expression and cell survival after metabolic stress. (A) Effect of NPM or control (CTL) NPM siRNA versus no siRNA (None) on NPM expression in primary renal cells. β-Actin was used as a loading control. (B) Cell survival after metabolic stress. *, P < 0.05 versus CTL or no siRNA; n = 3 to 4 separate experiments.

Zhiyong Wang, et al. Mol Cell Biol. 2013 May;33(10):1916-1924.
2.
Fig 3

Fig 3. From: Nucleophosmin, a Critical Bax Cofactor in Ischemia-Induced Cell Death.

(A and B) NPM mutant expression. (A) Diagram of Flag-NPM constructs cloned into lentiviral vectors. The diagram indicates key sites that regulate intracellular NPM localization. Deletion of the NLS prevents nuclear NPM entry, and deletion of the NES prevents NPM from exiting nuclei. A single-amino-acid substitution at lysine 263 (K263R) prevents NPM sumoylation, which is required for nuclear NPM export. (B) Expression of wild-type NPM and mutants was confirmed by immunoblot analysis using an anti-Flag antibody.

Zhiyong Wang, et al. Mol Cell Biol. 2013 May;33(10):1916-1924.
3.
Fig 10

Fig 10. From: Nucleophosmin, a Critical Bax Cofactor in Ischemia-Induced Cell Death.

Effect of a Bax blocking peptide on kidney function after renal ischemia in vivo. Shown is the effect of a cell-permeable NPM-Bax blocking peptide (NPM-Bax peptide), versus a nonspecific (control) peptide, on kidney function (BUN) on days 1 to 4 after 25 min of ischemia; 100 μg/g peptide was administered 30 min before and again 30 min after ischemia; n = 6 mice per group; *, P < 0.05 versus control peptide.

Zhiyong Wang, et al. Mol Cell Biol. 2013 May;33(10):1916-1924.
4.
Fig 9

Fig 9. From: Nucleophosmin, a Critical Bax Cofactor in Ischemia-Induced Cell Death.

(A and B) Effect of renal ischemia in vivo on cytosolic NPM translocation. (A) NPM content in the cytosolic fraction of renal cortex at baseline (Base), immediately after 30 min of ischemia (Isch), and after 15 min of reperfusion (Reperf). GAPDH was used as a loading control. (B) Densitometric analysis of 3 to 4 separate immunoblot studies performed as described for panel A.

Zhiyong Wang, et al. Mol Cell Biol. 2013 May;33(10):1916-1924.
5.
Fig 2

Fig 2. From: Nucleophosmin, a Critical Bax Cofactor in Ischemia-Induced Cell Death.

Effect of metabolic stress on NPM-Bax interaction. Immunoprecipitates (IP) were harvested from cells using an antibody directed against Bax at baseline (Base), immediately after 60 min of ATP depletion (ATP Depl), and after 30 or 60 min of recovery (Recovery) and then probed for Bax (upper) or NPM (lower) content. Immunoglobulin G (IgG) is shown as a control. Studies were performed on 400-μg cell lysate samples. IB, immunoblot.

Zhiyong Wang, et al. Mol Cell Biol. 2013 May;33(10):1916-1924.
6.
Fig 6

Fig 6. From: Nucleophosmin, a Critical Bax Cofactor in Ischemia-Induced Cell Death.

(A and B) Effect of Bax siRNA on Bax expression and survival after metabolic stress in cells that express NPM lacking the nuclear localizing sequence. (A) Percent survival after metabolic stress in cells that express the toxic NPM mutant (NPM-ΔNLS) in the presence and absence of specific (Bax siRNA +) or control (Bax siRNA −) siRNA. *, P < 0.05 versus the wild type; †, P < 0.05 versus NPM-ΔNLS. (B) Bax content in the lysates of cells exposed to Bax siRNA. Trials 1 to 3 represent three separate siRNA experiments.

Zhiyong Wang, et al. Mol Cell Biol. 2013 May;33(10):1916-1924.
7.
Fig 4

Fig 4. From: Nucleophosmin, a Critical Bax Cofactor in Ischemia-Induced Cell Death.

(A and B) Distribution of wild-type NPM and mutants in stressed and nonstressed cells. (A) NPM distribution in intact primary cells that express wild-type (WT) NPM or mutants lacking either the NLS (ΔNLS), the sumoylation site (K263R), or the NES (ΔNES) before (Baseline) or after (ATP Depl) stress; cells were stained with anti-Flag, antirhodamine secondary antibody. (B) Effect of wild-type NPM and mutant expression on the percentage of cell survival after metabolic stress compared to the baseline using the MTT assay (see Materials and Methods). n = 3 to 4 separate experiments; *, P < 0.05 compared to the wild-type baseline. NS, survival not significantly different from that of the wild type (P > 0.05).

Zhiyong Wang, et al. Mol Cell Biol. 2013 May;33(10):1916-1924.
8.
Fig 1

Fig 1. From: Nucleophosmin, a Critical Bax Cofactor in Ischemia-Induced Cell Death.

(A to C) Effect of metabolic stress on intracellular NPM distribution. (A) At baseline, intact cells stained with NPM antibody show prominent nucleolar staining (open arrow). In many cells, stress (ATP Deplete) induces NPM redistribution into the cytosol (closed arrow), whereas in other cells, nucleolar to nuclear NPM redistribution is detected (open arrow). During recovery, NPM reaccumulates in nucleoli (open arrow). (B) NPM redistribution into the cytosolic fraction in cells permeabilized with low-dose digitonin (upper) (see Materials and Methods) and total NPM (lower), measured by immunoblot analysis. GAPDH and β-actin were used as loading controls. (C) Densitometric analysis of four separate immunoblot studies. *, P < 0.05 versus the baseline; n = 5 separate studies. CTL, control.

Zhiyong Wang, et al. Mol Cell Biol. 2013 May;33(10):1916-1924.
9.
Fig 8

Fig 8. From: Nucleophosmin, a Critical Bax Cofactor in Ischemia-Induced Cell Death.

(A and B) Effect of an NPM-Bax blocking peptide on cell survival after metabolic stress. (A) Effect of a cell-permeable NPM-Bax peptide added to the medium 1 h before, during, or after subjecting proximal tubule cells to 60 min of ATP depletion on cell survival versus no peptide or a control (CTL) peptide. *, P = 0.08 versus CTL or no siRNA peptide; n = 3 to 4 separate experiments. (B) Immunoblot analyses of cytochrome c leakage (Cytosolic cyto c), active Bax content (Bax 6A7), and active caspase 3 (active Casp 3) after stress. GAPDH and β-actin were used as loading controls.

Zhiyong Wang, et al. Mol Cell Biol. 2013 May;33(10):1916-1924.
10.
Fig 5

Fig 5. From: Nucleophosmin, a Critical Bax Cofactor in Ischemia-Induced Cell Death.

(A to E) Effect of wild-type NPM or NPM mutant expression on stress-induced mitochondrial NPM and Bax accumulation and outer mitochondrial membrane injury. (A) Immunoblot analysis of NPM (upper) and Bax (lower) accumulation in the mitochondrial fraction of cells expressing either empty vector (EV), NPM lacking the nuclear localizing sequence (NPM-ΔNLS), or wild-type NPM (NPM-WT) at baseline (Base), after 60 min of ATP depletion (ATP), or after 20 min of recovery (Rec). F1F0-ATPase, an intrinsic outer membrane protein, was used as the loading control. (B) Nonmitochondrial AIF and cytochrome c (Cyto-C) in cells before and after stress (assessed in the presence of high-dose digitonin; see Materials and Methods), with GAPDH as a loading control. (C) Densitometric analysis of 3 to 4 separate immunoblot studies performed as described for panel B. (D) Immunoblot analysis of active caspase 3 (17- and 19-kDa bands) in lysates harvested from cells that express either empty vector (EV), NPM lacking the nuclear localizing sequence (NPM-ΔNLS), or wild-type NPM (NPM-WT) at baseline (Base), immediately after 60 min of ATP depletion (ATP), and after 60 min of recovery (Rec). (E) Densitometric analysis of 3 to 4 separate immunoblot studies performed as described for panel D.

Zhiyong Wang, et al. Mol Cell Biol. 2013 May;33(10):1916-1924.

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