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miR (show MLXIP Proteins)-185 was significantly downregulated in RCC (show XRCC1 Proteins) tissues and cell lines. SENP1 was a direct target of miR (show MLXIP Proteins)-186, and SENP1 mRNA expression was reversely correlated with miR (show MLXIP Proteins)-186 in RCC (show XRCC1 Proteins) tissues.
Treatment of cells with streptonigrin resulted in increased global SUMOylation levels and reduced level of hypoxia inducible factor alpha (HIF1alpha (show HIF1A Proteins)). 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 (show MOK Proteins), possibly through deSUMOylating and stabilizing HIF-1alpha (show HIF1A Proteins), 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 (show SUMO1 Proteins) 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 (show GATA1 Proteins) is an essential downstream target of SENP1 and that the differential expression and response of GATA1 (show GATA1 Proteins) and Bcl-xL (show BCL2L1 Proteins) are a key mechanism underlying chronic mountain sickness pathology.
miRNA1236 regulates hypoxia-induced epithelial-mesenchymal transformation and metastasis by repressing HDAC3 (show HDAC3 Proteins) and SENP1 expression.
SENP1 deSUMOylated SMAD4 (show SMAD4 Proteins) to promote EMT (show ITK Proteins) via up-regulating E-cadherin (show CDH1 Proteins) 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 (show HGF Proteins)-induced proliferation and migration of HCC (show FAM126A Proteins) cells, induces HCC (show FAM126A Proteins) cell apoptosis and growth arrest, and epithelial-to-mesenchymal transition, with increase of E-cadherin (show CDH1 Proteins) and ZO-1 (show TJP1 Proteins) expression, decrease of fibronectin (show FN1 Proteins) and N-cadherin (show CDH2 Proteins) expression.
knockdown of SENP1 augments the ability of Shh (show SHH Proteins) to sustain the proliferation of cerebellar granule cell precursors, demonstrating the physiological significance of the negative regulation of Shh (show SHH Proteins) signaling by SENP1.
SUMO1 (show SUMO1 Proteins) conjugation of RB and Lamin A/C (show LMNA Proteins) 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 (show STAT3 Proteins)-SOCS3 (show SOCS3 Proteins), which is tightly controlled by SENP1 via de-SUMOylation of protein tyrosine phosphatase 1B (PTP1B (show PTPN1 Proteins)), in IFN-gamma (show IFNG Proteins) signaling, is reported.
SENP1 deletion in adipocytes causes Type 1 diabetes mellitus via enhanced SUMOylation of NEMO (show IKBKG Proteins), leading to increased NF-kappaB (show NFKB1 Proteins) 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 (show HIF1A Proteins)-dependent pathway.
SENP1 enhances adipogenesis through de-SUMOylation of Sharp-1 (show BHLHE41 Proteins), which then releases Sharp-1 (show BHLHE41 Proteins) repression of PPARgamma (show PPARG Proteins) 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 (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) 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