Journal: Acta Pharmaceutica Sinica. B

Article Title: A new perspective of triptolide-associated hepatotoxicity: the relevance of NF- κ B and NF- κ B-mediated cellular FLICE-inhibitory protein

doi: 10.1016/j.apsb.2020.02.009

Figure Lengend Snippet: Possible role of NF- κ B and NF- κ B-mediated pro-survival signals in TP/LPS-induced hepatotoxicity. (A) Experimental design to detect the time-dependent changes of NF- κ B and its related pro-survival factors. (B)–(G) Relative mRNA levels of NF- κ B target genes, including Ciap1 , Ciap2 , Flip L , Xiap , Tnfaip3 , and Nfkbia , were detected by qPCR with tubulin as the internal control ( n = 6). (H)–(L) Representative Western blots and relative intensity of protein bands of FLIP L , CIAP1, XIAP, and I κ B- α after the treatment of TP and LPS with tubulin as the loading control ( n = 4–6). (M) Representative photomicrographs of liver sections by IHC for P65 1 h after LPS application (200 × ). Scale bar = 50 μm. Results were expressed as mean ± SEM and statistical analysis was performed using Two-way ANOVA following by Tukey's multiple comparison test. *, # , $ P <0.05, **, ## , $$ P <0.01, ***, ### , $$$ P <0.001; ns, no statistical difference.

Article Snippet: Antibody against RIPK1 (17519-1-AP), mixed lineage kinase domain like pseudokinase (MLKL, 66675-1-Ig), myeloperoxidase (MPO, 22225-1-AP), and CIAP1 (10022-1-AP) were purchased from Proteintech (Chicago, IL, USA).

Techniques: Control, Western Blot, Comparison

Journal: Acta Pharmaceutica Sinica. B

Article Title: A new perspective of triptolide-associated hepatotoxicity: the relevance of NF- κ B and NF- κ B-mediated cellular FLICE-inhibitory protein

doi: 10.1016/j.apsb.2020.02.009

Figure Lengend Snippet: The primer sequences used for qPCR assay in mice.

Article Snippet: Antibody against RIPK1 (17519-1-AP), mixed lineage kinase domain like pseudokinase (MLKL, 66675-1-Ig), myeloperoxidase (MPO, 22225-1-AP), and CIAP1 (10022-1-AP) were purchased from Proteintech (Chicago, IL, USA).

Techniques:

Journal: Circulation Research

Article Title: Integrin-Mediated Transcriptional Activation of Inhibitor of Apoptosis Proteins Protects Smooth Muscle Cells Against Apoptosis Induced by Degraded Collagen

doi: 10.1161/01.res.0000229267.77982.0d

Figure Lengend Snippet: Figure 5. Degraded collagen fragments induce IAPs in an NF-B–dependent manner. A, Whole cell extracts prepared from cells incubated with degraded collagen fragments for the indicated times were immunoblotted with antibodies against xIAP, c-IAP2, and survivin. -Actin was used as loading control. Induction of IAP expression after 24 hours of treatment was quantified using NIH Image. Results are presented as meanSD from 5 independent experiments. *P0.05 vs control. B, SMC were infected with control PURO vector or IBSer32,36/Ala and treated as described in Figure 2C. Protein levels of xIAP and c-IAP2 were determined by immunoblotting. -Actin was used as loading control. Shown is a representative experiment of 3.

Article Snippet: The following antibodies were used for immunoblotting: xIAP, poly(ADP-ribosyl) polymerase (PARP) (BD Biosciences), c-IAP2, I B (Santa Cruz Biotechnology); p-I , cleaved caspase-3, cleaved lamin A (New England Biolabs); survivin (Novus Biologicals); caspase-3 (R&D Systems); - and -actin (Sigma-Aldrich); and GAPDH (HyTest Ltd).

Techniques: Incubation, Control, Expressing, Infection, Plasmid Preparation, Western Blot

Journal: Circulation Research

Article Title: Integrin-Mediated Transcriptional Activation of Inhibitor of Apoptosis Proteins Protects Smooth Muscle Cells Against Apoptosis Induced by Degraded Collagen

doi: 10.1161/01.res.0000229267.77982.0d

Figure Lengend Snippet: Figure 6. Collagen fragments induce apoptosis after siRNA treatment against IAPs. A, SMC were transfected with specific siRNA against xIAP, c-IAP2, or nonsilencing control siRNA, and IAP expression was analyzed by Western blotting 48 and 72 hours later. Shown is a representative experiment of 4. B, SMC were treated with siRNAs as in A and exposed to collagen frag- ments for 18 hours. Apoptosis was determined by immunoblot- ting with antibodies against cleaved lamin A/C, PARP, and active caspase-3. -Actin was used as loading control. Shown is a representative experiment of 3.

Article Snippet: The following antibodies were used for immunoblotting: xIAP, poly(ADP-ribosyl) polymerase (PARP) (BD Biosciences), c-IAP2, I B (Santa Cruz Biotechnology); p-I , cleaved caspase-3, cleaved lamin A (New England Biolabs); survivin (Novus Biologicals); caspase-3 (R&D Systems); - and -actin (Sigma-Aldrich); and GAPDH (HyTest Ltd).

Techniques: Transfection, Control, Expressing, Western Blot

Journal: Molecular and Cellular Biochemistry

Article Title: TOR1 AIP1 interacts with p53 to enhance cell cycle dysregulation in prostate cancer progression

doi: 10.1007/s11010-025-05276-1

Figure Lengend Snippet: The expression of TOR1 AIP1 was downregulated in prostate cancer samples. A The expression of TOR1 AIP1 in 499 tumor tissues and 52 normal tissues was analyzed by TCGA. B The expression level of TOR1 AIP1 was validated by qPCR using clinical samples ( n = 5). C The protein level of TOR1 AIP1 in human prostate tumor specimens was determined by WB ( n = 3). D The expression of TOR1 AIP1 in prostate cancer was examined by IHC ( n = 3). Normal group: Non-cancerous tissue adjacent to the tumor, Tumor group: neoplastic tissue. Compared with the indicated group, * P < 0.05, ** P < 0.01, and *** P < 0.001

Article Snippet: To further confirm that the p53 expression might serve as the molecular mechanism of TOR1 AIP1 involved in the development of PRAD, we used pifithrin-α (MedChemExpress, Shanghai, China), an inhibitor of p53 protein, to determine if it resulted in rescuing the effect of TOR1 AIP1 on tumor progression.

Techniques: Expressing

Journal: Molecular and Cellular Biochemistry

Article Title: TOR1 AIP1 interacts with p53 to enhance cell cycle dysregulation in prostate cancer progression

doi: 10.1007/s11010-025-05276-1

Figure Lengend Snippet: The prognostic value of TOR1 AIP1 in prostate cancer patients. A The prognostic value of mRNA Level of TOR1 AIP1 in prostate cancer patients (Kaplan–Meier Plotter). B – E Lower TOR1 AIP1 expression was associated with age, N stage, T stage, and M stage. F ROC curve analysis of TOR1 AIP1. Compared with the indicated group, * P < 0.05, ** P < 0.01, and *** P < 0.001

Article Snippet: To further confirm that the p53 expression might serve as the molecular mechanism of TOR1 AIP1 involved in the development of PRAD, we used pifithrin-α (MedChemExpress, Shanghai, China), an inhibitor of p53 protein, to determine if it resulted in rescuing the effect of TOR1 AIP1 on tumor progression.

Techniques: Expressing

Journal: Molecular and Cellular Biochemistry

Article Title: TOR1 AIP1 interacts with p53 to enhance cell cycle dysregulation in prostate cancer progression

doi: 10.1007/s11010-025-05276-1

Figure Lengend Snippet: TOR1 AIP1 inhibited the proliferation and invasion of the DU145 and PC3M cells. TOR1 AIP1 stably overexpression DU145 cells and PC3M cells using lentivirus were generated. A and B The viability of DU145 and PC3M cells were measured by CCK8 assay at the indicated times. C and D Colony formation assays were performed in DU145 cells and PC3M cells transfected with indicated lentivirus. E – G The penetrability in Transwell chambers was measured to verify the invasive capability of DU145 cells and PC3M cells. Data represent mean ± SD ( n = 3). NC: Control virus-transfected cells, TOR1 AIP1 OVE: TOR1 AIP1-overexpressing cells. Compared with the indicated group, * P < 0.05, ** P < 0.01, and *** P < 0.001

Article Snippet: To further confirm that the p53 expression might serve as the molecular mechanism of TOR1 AIP1 involved in the development of PRAD, we used pifithrin-α (MedChemExpress, Shanghai, China), an inhibitor of p53 protein, to determine if it resulted in rescuing the effect of TOR1 AIP1 on tumor progression.

Techniques: Stable Transfection, Over Expression, Generated, CCK-8 Assay, Transfection, Control, Virus

Journal: Molecular and Cellular Biochemistry

Article Title: TOR1 AIP1 interacts with p53 to enhance cell cycle dysregulation in prostate cancer progression

doi: 10.1007/s11010-025-05276-1

Figure Lengend Snippet: shRNA-mediated silencing of TOR1 AIP1 increased the proliferation, migration, and invasion of PRAD cells. TOR1 AIP1 stably knockdown 22RV1 and C4 - 2 cell lines using lentivirus were generated. A and B The viability of 22RV1 and C4 - 2 cells were measured by CCK8 assay at the indicated times. C and D Colony formation assays were performed in 22RV1 and C4 - 2 cells transfected with indicated lentivirus. E – G Transwell assays were used to detect the migration and invasion ability of 22RV1 and C4 - 2 cells. NC: Control virus-transfected cells, sh#1 and sh#2: TOR1 AIP1 knockdown cells. Data represent mean ± SD ( n = 3). By comparison with vehicle control group, * P < 0.05 and *** P < 0.001

Article Snippet: To further confirm that the p53 expression might serve as the molecular mechanism of TOR1 AIP1 involved in the development of PRAD, we used pifithrin-α (MedChemExpress, Shanghai, China), an inhibitor of p53 protein, to determine if it resulted in rescuing the effect of TOR1 AIP1 on tumor progression.

Techniques: shRNA, Migration, Stable Transfection, Knockdown, Generated, CCK-8 Assay, Transfection, Control, Virus, Comparison

Journal: Molecular and Cellular Biochemistry

Article Title: TOR1 AIP1 interacts with p53 to enhance cell cycle dysregulation in prostate cancer progression

doi: 10.1007/s11010-025-05276-1

Figure Lengend Snippet: TOR1 AIP1 overexpression suppressed the progression of PRAD in vivo. We generated TOR1 AIP1 stably overexpressed DU145 cells and PC3M cells (TOR1 AIP1 OVE) or TOR1 AIP1 stably knockdown 22RV1 cells and C4 - 2 cells (sh#1 and sh#2) and control cells (shNC) and injected them subcutaneously into the right axils of nude mice. A and B Xenograft tumor images of DU145 cells and PC3M cells stably transfected with NC or TOR1 AIP1 overexpression. C and D Tumor Weight of DU145 cells and PC3M cells stably transfected with NC or TOR1 AIP1 overexpression ( n = 5). E and F The growth curve of DU145 cells and PC3M cells stably transfected with NC or TOR1 AIP1 overexpression in nude mice ( n = 5). G and H Xenograft tumor images of 22RV1 cells and C4 - 2 cells stably transfected with shNC or TOR1 AIP1 sh#1 and sh#2 ( n = 4). I and J Tumor weight of shNC and TOR1 AIP1 sh#1 and sh#2 ( n = 4). K and L The growth curve of different groups ( n = 4). NC and shNC: Nude mice inoculated with control virus-transfected cells, OVE: Nude mice injected with TOR1 AIP1-overexpressing cells, sh#1 and sh#2: Nude mice injected with TOR1 AIP1 knockdown cells. Data represent mean ± SD. Compared with the indicated group, *** P < 0.001

Article Snippet: To further confirm that the p53 expression might serve as the molecular mechanism of TOR1 AIP1 involved in the development of PRAD, we used pifithrin-α (MedChemExpress, Shanghai, China), an inhibitor of p53 protein, to determine if it resulted in rescuing the effect of TOR1 AIP1 on tumor progression.

Techniques: Over Expression, In Vivo, Generated, Stable Transfection, Knockdown, Control, Injection, Transfection, Virus

Journal: Molecular and Cellular Biochemistry

Article Title: TOR1 AIP1 interacts with p53 to enhance cell cycle dysregulation in prostate cancer progression

doi: 10.1007/s11010-025-05276-1

Figure Lengend Snippet: TOR1 AIP1 interacts with p53 to inhibit the tumor progression in vitro. A – C Cell cycle analysis was performed using flow cytometry. D and E The expressions of p53 protein in DU145 and PC3M cells with stably transfected with NC or TOR1 AIP1 overexpression were determined by western blot. F and G The interaction between TOR1 AIP1 and p53 in DU145 and PC3M cells was determined by CO-IP. H and I The viability of TOR1 AIP1 stably overexpression DU145 cells and PC3M cells with or without pifithrin-α treatment were measured by CCK8 assay. J and K Colony formation assays were performed in TOR1 AIP1 stably overexpression DU145 cells and PC3M cells with or without pifithrin-α treatment. L – N Transwell assay was used to detect the effect of pifithrin-α on migration and invasion of TOR1 AIP1 stably overexpression DU145 cells and PC3M cells. Data represent mean ± SD ( n = 3). NC: Control virus-transfected cells, TOR1 AIP1 OVE: TOR1 AIP1-overexpressing cells. Compared with the indicated group, *** P < 0.001, n.s, no significant difference

Article Snippet: To further confirm that the p53 expression might serve as the molecular mechanism of TOR1 AIP1 involved in the development of PRAD, we used pifithrin-α (MedChemExpress, Shanghai, China), an inhibitor of p53 protein, to determine if it resulted in rescuing the effect of TOR1 AIP1 on tumor progression.

Techniques: In Vitro, Cell Cycle Assay, Flow Cytometry, Stable Transfection, Transfection, Over Expression, Western Blot, Co-Immunoprecipitation Assay, CCK-8 Assay, Transwell Assay, Migration, Control, Virus

Journal: Molecular and Cellular Biochemistry

Article Title: TOR1 AIP1 interacts with p53 to enhance cell cycle dysregulation in prostate cancer progression

doi: 10.1007/s11010-025-05276-1

Figure Lengend Snippet: p53-mediated the anti-tumor effect of TOR1 AIP1 in vivo. We injected subcutaneously TOR1 AIP1 stably overexpression cells, with or without pifithrin-α intratumoral treatment for nude mice. A – F Tumor images ( A , B ), tumor weights ( C , D ), and tumor growth curve ( E , F ) of different groups. Data represent mean ± SD ( n = 5). NC: Nude mice inoculated with control virus-transfected cells, OVE: Nude mice injected with TOR1 AIP1-overexpressing cells. Compared with the indicated group, ** P < 0.01 and *** P < 0.001

Article Snippet: To further confirm that the p53 expression might serve as the molecular mechanism of TOR1 AIP1 involved in the development of PRAD, we used pifithrin-α (MedChemExpress, Shanghai, China), an inhibitor of p53 protein, to determine if it resulted in rescuing the effect of TOR1 AIP1 on tumor progression.

Techniques: In Vivo, Injection, Stable Transfection, Over Expression, Control, Virus, Transfection