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https://www.readbyqxmd.com/read/27895727/deficiency-of-sumo-specific-protease-1-induces-arsenic-trioxide-mediated-apoptosis-by-regulating-xbp1-activity-in-human-acute-promyelocytic-leukemia
#1
Fei-Fei Wang, Ming-Zhu Liu, Yi Sui, Qing Cao, Bo Yan, Mei-Ling Jin, Xi Mo
Small ubiquitin-like modifier (SUMO)/sentrin-specific protease 1 (SENP1), a member of the SENP family, is highly expressed in several neoplastic tissues. However, the effect of SENP1 in acute promyelocytic leukemia (APL) has not been elucidated. In the present study, it was observed that SENP1 deficiency had no effect on the spontaneous apoptosis or differentiation of NB4 cells. Arsenic trioxide (As2O3) could induce the upregulation of endoplasmic reticulum (ER) stress, resulting in the apoptosis of NB4 cells...
November 2016: Oncology Letters
https://www.readbyqxmd.com/read/27882949/sumo-specific-protease-1-protects-neurons-from-apoptotic-death-during-transient-brain-ischemia-reperfusion
#2
Huijun Zhang, Yan Wang, Aoxue Zhu, Dehua Huang, Shining Deng, Jinke Cheng, Michael X Zhu, Yong Li
SUMO-specific protease 1 (SENP1) deconjugates SUMO from modified proteins. Although post-ischemic activation of SUMO conjugation was suggested to be neuroprotective against ischemia/reperfusion (I/R) injury, the function of SENP1 in this process remained unclear. Here we show that transient middle cerebral artery occlusion in mice followed by 6, 12 and 24 h reperfusion significantly enhanced SENP1 levels in the affected brain area, independent of transcription. Consistent with the increase in SENP1, the levels of SUMO1-conjugated proteins were decreased by I/R in cortical neurons of control littermate mice, but unchanged in that of animals with conditional ablation of SENP1 gene from adult principal neurons, the SENP1(flox/flox):CamKIIα-Cre (SENP1 cKO) mice...
November 24, 2016: Cell Death & Disease
https://www.readbyqxmd.com/read/27852060/senp1-regulates-pten-stability-to-dictate-prostate-cancer-development
#3
Tasneem Bawa-Khalfe, Feng-Ming Yang, Joan Ritho, Hui-Kuan Lin, Jinke Cheng, Edward T H Yeh
SUMO protease SENP1 is elevated in multiple carcinomas including prostate cancer (PCa). SENP1 exhibits carcinogenic properties; it promotes androgen receptor-dependent and -independent cell proliferation, stabilizes HIF1α, increases VEGF, and supports angiogenesis. However, mice expressing an androgen-responsive promoter driven SENP1-transgene (SENP1-Tg) develop high-grade prostatic intraepithelial neoplasia, but not carcinoma. We now show that tumor suppressive PTEN signaling is induced in SENP1-Tg to enhance prostate epithelial cell apoptosis...
November 10, 2016: Oncotarget
https://www.readbyqxmd.com/read/27821551/senp1-drives-hypoxia-induced-polycythemia-via-gata1-and-bcl-xl-in-subjects-with-monge-s-disease
#4
Priti Azad, Huiwen W Zhao, Pedro J Cabrales, Roy Ronen, Dan Zhou, Orit Poulsen, Otto Appenzeller, Yu Hsin Hsiao, Vineet Bafna, Gabriel G Haddad
In this study, because excessive polycythemia is a predominant trait in some high-altitude dwellers (chronic mountain sickness [CMS] or Monge's disease) but not others living at the same altitude in the Andes, we took advantage of this human experiment of nature and used a combination of induced pluripotent stem cell technology, genomics, and molecular biology in this unique population to understand the molecular basis for hypoxia-induced excessive polycythemia. As compared with sea-level controls and non-CMS subjects who responded to hypoxia by increasing their RBCs modestly or not at all, respectively, CMS cells increased theirs remarkably (up to 60-fold)...
November 14, 2016: Journal of Experimental Medicine
https://www.readbyqxmd.com/read/27741516/senp1-promotes-proliferation-of-clear-cell-renal-cell-carcinoma-through-activation-of-glycolysis
#5
Baijun Dong, Yujing Gao, Xunlei Kang, Hongchang Gao, Jin Zhang, Hua Guo, Mingjian J You, Wei Xue, Jinke Cheng, Yiran Huang
Metabolic shift toward aerobic glycolysis is a fundamental element contributing to the development and progression of clear cell renal cell carcinoma (ccRCC). We and others previously observed enhanced glycolysis and diminished tricarboxylic acid (TCA) cycle activity in ccRCC tissue. Here, by integrated gene expression and metabolomic analyses of 36 matched pairs of tumor and adjacent normal tissues, we showed that expression of Sentrin/SUMO-specific protease 1 (SENP1) is positively associated with glycolysis levels in ccRCC...
October 12, 2016: Oncotarget
https://www.readbyqxmd.com/read/27703003/sumo-modification-reverses-inhibitory-effects-of-smad-nuclear-interacting-protein-1-in-tgf-%C3%AE-responses
#6
Sisi Liu, Jianyin Long, Bo Yuan, Mingjie Zheng, Mu Xiao, Jianming Xu, Xia Lin, Xin-Hua Feng
SNIP1 (Smad nuclear interacting protein 1) is a transcription repressor for the TGF-β and NF-κB signaling pathways through disrupting the recruitment of co-activator p300. However, it is unclear how the functions of SNIP1 in the TGF-β signaling pathway are controlled. Our present studies show that SNIP1 is covalently modified by small ubiquitin-like modifier (SUMO) in vitro and in vivo at three lysine sites: Lys(5), Lys(30), and Lys(108), with Lys(30) being the major SUMO modification site. SUMOylation of SNIP1 is enhanced by SUMO E3 ligase PIAS proteins and inhibited by SUMO proteases SENP1/2...
November 18, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27702761/senp1-regulates-ifn-%C3%AE-stat1-signaling-through-stat3-socs3-negative-feedback-loop
#7
Tingting Yu, Yong Zuo, Rong Cai, Xian Huang, Shuai Wu, Chenxi Zhang, Y Eugene Chin, Dongdong Li, Zhenning Zhang, Nansong Xia, Qi Wang, Hao Shen, Xuebiao Yao, Zhong-Yin Zhang, Song Xue, Lei Shen, Jinke Cheng
Interferon-γ (IFN-γ) triggers macrophage for inflammation response by activating the intracellular JAK-STAT1 signaling. SOCS1 and protein tyrosine phosphatases can negatively modulate IFN-γ signaling. Here we identify a novel negative feedback loop mediated by STAT3-SOCS3, which is tightly controlled by SENP1 via de-SUMOylation of protein tyrosine phosphatase 1B (PTP1B), in IFN-γ signaling. SENP1-deficient macrophages show defects in IFN-γ signaling and M1 macrophage activation. PTP1B in SENP1-deficient macrophages is highly SUMOylated, which reduces PTP1B-induced de-phosphorylation of STAT3...
October 4, 2016: Journal of Molecular Cell Biology
https://www.readbyqxmd.com/read/27693211/inhibition-of-sumo-specific-protease-1-induces-apoptosis-of-astroglioma-cells-by-regulating-nf-%C3%AE%C2%BAb-akt-pathways
#8
Wenrong Xia, Hongwei Tian, Xin Cai, HaiBo Kong, Wenliang Fu, Weiwei Xing, Yuanyuan Wang, Minji Zou, Yuhua Hu, Donggang Xu
SUMO-specific protease 1 (SENP1) is an important regulation protease in the protein desumoylation, which was shown to have a prooncogenicrole in many types of cancer. However, the mechanism of action for SENP1 in astrocytoma is not yet clear. Astrocytoma is the most frequent one among various neurogliomas, of which a subtype known as glioblastoma multiforme (GBM) is the most malignant brain glioma and seriously influences the life quality of the patients. In this study, the expression of SENP1 was detected in 28 cases of various grades of astrocytoma and 6 cases of normal human tissues...
September 28, 2016: Gene
https://www.readbyqxmd.com/read/27659494/senp1-is-a-crucial-regulator-for-cell-senescence-through-desumoylation-of-bmi1
#9
Nansong Xia, Juan Cai, Feifei Wang, Baijun Dong, Song Liu, Fengling Chen, Jinke Cheng, Yong Zuo
Cell senescence can limit proliferative potential and prevent tumorigenesis. Bmi1 is a key regulator in cell senescence by suppressing the Ink4a/Arf locus. However, how to regulate Bmi1 activity in cell senescence is largely unknown. Here, we show that SENP1 plays an important role in cell senescence by regulating Bmi1 SUMOylation. Senp1(-/-) primary MEF cells show resistance to cell senescence induced by passaging or other senescence inducing signals. SENP1 deficiency also reduces oncogene H-Ras(V12)-induced senescence, and enhances H-Ras(V12)-induced cell transformation...
September 23, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27644314/senp2-expression-was-induced-by-chronic-glucose-stimulation-in-ins1-cells-and-it-was-required-for-the-associated-induction-of-ccnd1-and-mafa
#10
Hye Seung Jung, Yu Mi Kang, Ho Seon Park, Byung Yong Ahn, Hakmo Lee, Min Joo Kim, Jin Young Jang, Sun-Whe Kim
Post-translational modification by bonding of small ubiquitin-like modifier (SUMO) peptides influences various cellular functions, and is regulated by SUMO-specific proteases (SENPs). Several proteins have been suggested to have diverse impact on insulin synthesis and secretion through SUMO modification in beta cells. However, the role of SUMO modification in beta cell mass has not been established. Here, we examined the changes in expression of Senp in INS1 cells and pancreatic islets under diabetes-relevant stress conditions and associated changes in beta cell mass...
September 20, 2016: Islets
https://www.readbyqxmd.com/read/27631804/in-situ-sumoylation-and-desumoylation-assays-fluorescent-methods-to-visualize-sumoylation-and-desumoylation-in-permeabilized-cells
#11
Eri Yuasa, Hisato Saitoh
This chapter deals with the fluorescence detection of SUMOylation and deSUMOylation in semi-intact cultured human cells, the so-called "in situ SUMOylation assay" and the "in situ deSUMOylation assay," respectively. In the in situ SUMOylation assay, the recombinant green-fluorescence protein fused to the SUMO1 (GFP-SUMO1) protein is used to visualize the nuclear rim, nucleolus, and nuclear bodies. These GFP signals represent cellular regions where SUMOylation efficiently takes place. If the recombinant SUMO-specific protease SENP1-catalytic domain is added after in situ SUMOylation, GFP signals can be erased...
2016: Methods in Molecular Biology
https://www.readbyqxmd.com/read/27626674/sumo-signaling-by-hypoxic-inactivation-of-sumo-specific-isopeptidases
#12
Kathrin Kunz, Kristina Wagner, Luca Mendler, Soraya Hölper, Nathalie Dehne, Stefan Müller
Post-translational modification of proteins with ubiquitin-like SUMO modifiers is a tightly regulated and highly dynamic process. The SENP family of SUMO-specific isopeptidases comprises six cysteine proteases. They are instrumental in counterbalancing SUMO conjugation, but their regulation is not well understood. We demonstrate that in hypoxic cell extracts, the catalytic activity of SENP family members, in particular SENP1 and SENP3, is inhibited in a rapid and fully reversible process. Comparative mass spectrometry from normoxic and hypoxic cells defines a subset of hypoxia-induced SUMO1 targets, including SUMO ligases RanBP2 and PIAS2, glucose transporter 1, and transcriptional regulators...
September 13, 2016: Cell Reports
https://www.readbyqxmd.com/read/27617172/the-role-of-adipose-derived-inflammatory-cytokines-in-type-1-diabetes
#13
REVIEW
Lan Shao, Boya Feng, Yuying Zhang, Huanjiao Zhou, Weidong Ji, Wang Min
Adipose tissue dysfunction correlates with the development of diabetes. Mice with an adipocyte-specific deletion of the SUMO-specific protease SENP1 develop symptoms of type-1 diabetes mellitus (T1DM). Peri-pancreatic adipocytes (PATs) exert both systemic and paracrine effects on pancreases function. Our recent studies report that PATs of SENP1-deficient mice have increased proinflammatory cytokine production compared with other adipose depots. Proinflammatory cytokines produced from PATs not only have direct cytotoxic effects on pancreatic islets, but also increase CCL5 expression in adjacent pancreatic islets, which induces persistent inflammation in pancreases by acquisition of Th1 and Th17 effector T cell subsets...
July 2016: Adipocyte
https://www.readbyqxmd.com/read/27604867/sumoylation-regulates-the-intracellular-fate-of-zo-2
#14
Franziska Wetzel, Sonnhild Mittag, Misael Cano-Cortina, Tobias Wagner, Oliver H Krämer, Rainer Niedenthal, Lorenza Gonzalez-Mariscal, Otmar Huber
The zonula occludens (ZO)-2 protein links tight junctional transmembrane proteins to the actin cytoskeleton and associates with splicing and transcription factors in the nucleus. Multiple posttranslational modifications control the intracellular distribution of ZO-2. Here, we report that ZO-2 is a target of the SUMOylation machinery and provide evidence on how this modification may affect its cellular distribution and function. We show that ZO-2 associates with the E2 SUMO-conjugating enzyme Ubc9 and with SUMO-deconjugating proteases SENP1 and SENP3...
September 7, 2016: Cellular and Molecular Life Sciences: CMLS
https://www.readbyqxmd.com/read/27576863/allosteric-activation-of-senp1-by-sumo1-%C3%AE-grasp-domain-involves-a-dock-and-coalesce-mechanism
#15
Jingjing Guo, Huan-Xiang Zhou
Small ubiquitin-related modifiers (SUMOs) are conjugated to proteins to regulate a variety of cellular processes. SENPs are cysteine proteases with a catalytic center located within a channel between two subdomains that catalyzes SUMO C-terminal cleavage for processing of SUMO precursors and de-SUMOylation of target proteins. The β-grasp domain of SUMOs binds to an exosite cleft, and allosterically activates SENPs via an unknown mechanism. Our molecular dynamics simulations showed that binding of the β-grasp domain induces significant conformational and dynamic changes in SENP1, including widening of the exosite cleft and quenching of nanosecond dynamics in all but a distal region...
2016: ELife
https://www.readbyqxmd.com/read/27573572/depletion-of-senp1-suppresses-the-proliferation-and-invasion-of-triple-negative-breast-cancer-cells
#16
Zhonghua Wang, Jia Jin, Jian Zhang, Leiping Wang, Jun Cao
To investigate the roles of SUMO-specific protease 1 (SENP1) in triple-negative breast cancer (TNBC), we detected the expression level of SENP1 in the clinical samples of TNBC and non‑TNBC patients by using immunohistochemical staining, qRT‑PCR, and western blotting. We found that SENP1 was highly expressed in the TNBC tissues compared with the normal breast tissues, as well as non‑TNBC tissues. Next, we constructed the si‑SENP1‑transfected TNBC cell lines for further biological function investigation...
October 2016: Oncology Reports
https://www.readbyqxmd.com/read/27507651/comment-on-sumo-deconjugation-is-required-for-arsenic-triggered-ubiquitylation-of-pml
#17
Omar Ferhi, Laurent Pérès, Sarah Tessier, Hugues de Thé, Valérie Lallemand-Breitenbach
Fasci et al proposed that a SENP1-mediated switch from SUMO2 to SUMO1 conjugation on Lys(65) in promyelocytic leukemia protein (PML) is required for arsenic-induced PML degradation, the basis for the antileukemic activity of arsenic. We found that PML or PML/RARA (retinoic acid receptor α) mutants that cannot be SUMO-conjugated on this specific site nevertheless underwent immediate arsenic-triggered SUMO modification. Moreover, these mutants were efficiently degraded in cells and even in vivo, demonstrating that SUMOylation of Lys(65) was dispensable for arsenic response...
2016: Science Signaling
https://www.readbyqxmd.com/read/27491710/vialinin-a-and-thelephantin-g-potent-inhibitors-of-tumor-necrosis-factor-%C3%AE-production-inhibit-sentrin-sumo-specific-protease-1-enzymatic-activity
#18
Yasukiyo Yoshioka, Daisuke Namiki, Mao Makiuchi, Kouichi Sugaya, Jun-Ichi Onose, Hitoshi Ashida, Naoki Abe
Several p-terphenyl compounds have been isolated from the edible Chinese mushroom Thelephora vialis. Vialinin A, a p-terphenyl compound, strongly inhibits tumor necrosis factor-α production and release. Vialinin A inhibits the enzymatic activity of ubiquitin-specific peptidase 5, one of the target molecules in RBL-2H3 cells. Here we examined the inhibitory effect of p-terphenyl compounds, including vialinin A, against sentrin/SUMO-specific protease 1 (SENP1) enzymatic activity. The half maximal inhibitory concentration values of vialinin A and thelephantin G against full-length SENP1 were 1...
September 1, 2016: Bioorganic & Medicinal Chemistry Letters
https://www.readbyqxmd.com/read/27449295/momordin-ic-a-new-natural-senp1-inhibitor-inhibits-prostate-cancer-cell-proliferation
#19
Jingjing Wu, Hu Lei, Jinfu Zhang, Xiangyun Chen, Caixia Tang, Weiwei Wang, Hanzhang Xu, Weilie Xiao, Wenli Gu, Yingli Wu
SUMO-specific protease 1 (SENP1), a member of the de-SUMOylation protease family, is elevated in prostate cancer (PCa) cells and is involved in PCa pathogenesis. Momordin Ιc (Mc), a natural pentacyclic triterpenoid, inhibited SENP1 in vitro, as reflected by reduced SENP1C-induced cleavage of SUMO2-ΔRanGAP1. Mc also altered the thermal stability of SENP1 in a newly developed cellular thermal shift assay, indicating that Mc directly interacts with SENP1 in PCa cells. Consistent with SENP1 inhibition, Mc increased SUMOylated protein levels, which was further confirmed by the accumulation of two known SUMOylated proteins, hypoxia inducible factor-1a and nucleus accumbens associated protein 1 in PC3 cells...
July 16, 2016: Oncotarget
https://www.readbyqxmd.com/read/27347128/downregulation-of-senp1-inhibits-cell-proliferation-migration-and-promotes-apoptosis-in-human-glioma-cells
#20
Qiu-Sheng Zhang, Meng Zhang, Xian-Jian Huang, Xiao-Jia Liu, Wei-Ping Li
Small ubiquitin-related modifier protein (SUMO) is an evolutionarily conserved protein in a broad range of eukaryotic organisms. De-SUMOylation, the reverse reaction of SUMOylation, is regulated by a family of SUMO-specific proteases (SENPs). SENP1 is a member of the de-SUMOylation protease family involved in the de-SUMOylation of a variety of SUMOylated proteins. The present study demonstrates that small hairpin RNA (shRNA)-mediated downregulation of SENP1 inhibits cell proliferation and migration, and promotes apoptosis in human glioma cells...
July 2016: Oncology Letters
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