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miR (zeige MLXIP Proteine)-185 was significantly downregulated in RCC (zeige XRCC1 Proteine) tissues and cell lines. SENP1 was a direct target of miR (zeige MLXIP Proteine)-186, and SENP1 mRNA expression was reversely correlated with miR (zeige MLXIP Proteine)-186 in RCC (zeige XRCC1 Proteine) tissues.
Treatment of cells with streptonigrin resulted in increased global SUMOylation levels and reduced level of hypoxia inducible factor alpha (HIF1alpha (zeige HIF1A Proteine)). These findings inform both the design of SENP1 targeting strategy and the modification of streptonigrin to improve its efficacy for possible future clinical use.
SENP1 promotes cell proliferation and disease progression in clear cell renal cell carcinoma (zeige MOK Proteine), possibly through deSUMOylating and stabilizing HIF-1alpha (zeige HIF1A Proteine), leading to increased expression of key glycolytic enzymes and enhanced glycolytic flux.
Molecular dynamics simulations showed that binding of the beta-grasp domain of SUMO1 (zeige SUMO1 Proteine) 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.
GATA1 (zeige GATA1 Proteine) is an essential downstream target of SENP1 and that the differential expression and response of GATA1 (zeige GATA1 Proteine) and Bcl-xL (zeige BCL2L1 Proteine) are a key mechanism underlying chronic mountain sickness pathology.
miRNA1236 regulates hypoxia-induced epithelial-mesenchymal transformation and metastasis by repressing HDAC3 (zeige HDAC3 Proteine) and SENP1 expression.
SENP1 deSUMOylated SMAD4 (zeige SMAD4 Proteine) to promote EMT (zeige ITK Proteine) via up-regulating E-cadherin (zeige CDH1 Proteine) in prostate cancer cells. Therefore, SENP1 is a potential target for treatment of advanced prostate cancer.
The variability of the SENP1 and SENP2 genes may play a role in breast cancer occurrence.
this study elucidated that SENP1 is essential for triple-negative breast cancer cell proliferation and migration in vitro, as well as tumor formation and metastasis in vivo
Hepatocellular carcinoma cells express a high level of Senp1 which is induced by HGF/c-Met signals. Senp1 silencing reduces the HGF (zeige HGF Proteine)-induced proliferation and migration of HCC (zeige FAM126A Proteine) cells, induces HCC (zeige FAM126A Proteine) cell apoptosis and growth arrest, and epithelial-to-mesenchymal transition, with increase of E-cadherin (zeige CDH1 Proteine) and ZO-1 (zeige TJP1 Proteine) expression, decrease of fibronectin (zeige FN1 Proteine) and N-cadherin (zeige CDH2 Proteine) expression.
knockdown of SENP1 augments the ability of Shh (zeige SHH Proteine) to sustain the proliferation of cerebellar granule cell precursors, demonstrating the physiological significance of the negative regulation of Shh (zeige SHH Proteine) signaling by SENP1.
SUMO1 (zeige SUMO1 Proteine) conjugation of RB and Lamin A/C (zeige LMNA Proteine) is modulated by the SUMO protease SENP1 and that sumoylation of both proteins is required for their interaction.
SENP1 plays a neuroprotective role in ischemia/reperfusion injury.
a novel negative feedback loop mediated by STAT3 (zeige STAT3 Proteine)-SOCS3 (zeige SOCS3 Proteine), which is tightly controlled by SENP1 via de-SUMOylation of protein tyrosine phosphatase 1B (PTP1B (zeige PTPN1 Proteine)), in IFN-gamma (zeige IFNG Proteine) signaling, is reported.
SENP1 deletion in adipocytes causes Type 1 diabetes mellitus via enhanced SUMOylation of NEMO (zeige IKBKG Proteine), leading to increased NF-kappaB (zeige NFKB1 Proteine) activity, cytokine production and pancreatic inflammation.
results of the present study are of both theoretical and therapeutic significance to explore the potential roles of SENP1 under IH condition and elucidated the mechanisms underlying microglial survival and activation
A role for islet SENP1 as a regulator of in vivo glucose homeostasis was demonstrated by the tissue-selective and inducible knockout of this enzyme.
SENP1 up-regulation in diseased heart is mediated via calcineurin-NFAT/MEF2C-PGC-1alpha pathway.
SENP1 deficiency exacerbates ischemia-reperfusion injury in cardiomyocytes via a HIF1alpha (zeige HIF1A Proteine)-dependent pathway.
SENP1 enhances adipogenesis through de-SUMOylation of Sharp-1 (zeige BHLHE41 Proteine), which then releases Sharp-1 (zeige BHLHE41 Proteine) repression of PPARgamma (zeige PPARG Proteine) expression and adipocyte differentiation. These results reveal SENP1 as a novel regulator in adipogenesis.
XSENP1a and XSENP1b are sumo-specific proteases that inhibit normal head formation by inhibiting Wnt (zeige WNT2 Proteine)/beta-catenin (zeige CTNNB1 Proteine) signaling.
This gene encodes a cysteine protease that specifically targets members of the small ubiquitin-like modifier (SUMO) protein family. This protease regulates SUMO pathways by deconjugating sumoylated proteins. This protease also functions to process the precursor SUMO proteins into their mature form. Alternate splicing results in multiple transcript variants.
SUMO1/sentrin specific protease 1
, sentrin-specific protease 1
, sentrin/SUMO-specific protease SENP1
, SUMO-1 protease 2
, Sumo1/sentrin/SMT3 specific peptidase 1
, SUMO-specific protease U1p1
, sentrin specific protease 1a
, SUMO1/sentrin specific peptidase 1
, sentrin/SUMO-specific protease 1
, similar to Sentrin-specific protease 1 (Sentrin/SUMO-specific protease SENP1)
, sentrin specific protease 1b