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Last update 08 May 2025

SMOX

Last update 08 May 2025

Basic Info

Synonyms

C20orf16, dJ779E11.1, FLJ20746

+ [8]

Introduction

Flavoenzyme which catalyzes the oxidation of spermine to spermidine. Can also use N(1)-acetylspermine and spermidine as substrates, with different affinity depending on the isoform (isozyme) and on the experimental conditions. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs. May contribute to beta-alanine production via aldehyde dehydrogenase conversion of 3-amino-propanal.

Drugs associated with SMOX

C9-4

Target

SMOX

Mechanism

SMOX inhibitors

Active Org.

Nihon University

Originator Org.

Nihon University

Active Indication

Brain Ischemia

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

MDL-72527

Target

PAOX x SMOX

Mechanism

PAOX inhibitors [+2]

Active Org.

Johns Hopkins University School of Advanced International [+3]

Originator Org.

Aventis SA

Active Indication

Diabetic Retinopathy [+1]

Inactive Indication

Neoplasms

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

CN117964770

Patent Mining

Target

SMOX

Mechanism-

Active Org.

Guangdong Saier Biotechnology Co., Ltd. [+1]

Originator Org.

Bei Jing Chun Guan Li Ya Sheng Wu Ji Shu You Xian Gong Si [+1]

Active Indication

Brain Cancer

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with SMOX

100 Translational Medicine associated with SMOX

0 Patents (Medical) associated with SMOX

465

Literatures (Medical) associated with SMOX

01 Jun 2025·Cryobiology

BGP-15 improves quality of goat sperm by mitigating oxidative stress during cryopreservation

Article

Author: Wu, Caifeng ; Dai, Jianjun ; Zhu, Xing ; Xu, Jiehuan ; Liu, Fuqin ; Zhang, Shushan ; He, Mengqian ; Sun, Lingwei ; Gao, Jun

The objective of this study was to evaluate the effect of the addition of BGP-15 ((Z)-N'-(2-hydroxy-3-(piperidin-1-yl) propoxy) nicotinimidamide) on goat sperm during cryopreservation. The semen from six rams was diluted with a soybean lecithin-based extender containing different doses of BGP-15 (0, 50, 100, 150, and 200 μM). After the freeze-thawing process, sperm characteristics, plasma membrane integrity and functionality, acrosomal status, mitochondria activity, apoptosis status, and gene expression of post-thawed ram spermatozoa were assessed. Compared to fresh spermatozoa, the ultrastructure of frozen spermatozoa was damaged, and frozen spermatozoa had a reduced number of duplex microtubules with partially asymmetric distributions, localized disappearance of the central microtubule, and ambiguous submicrotubule structures. Moreover, the 100 μM BGP-15 treatment group had the highest percentage of viability, plasma membrane and acrosome integrities, and mitochondrial activity of frozen-thawed spermatozoa when compared to the control (P < 0.05). In the Computer-Assisted Semen Analyzer, sperm motility parameters were significantly increased in the BGP-15 treatment group against the control group (P < 0.05), except wobble. Similarly, BGP-15 treatment increased the levels of T-AOC, SOD, CAT, and GHS-Px and decreased the level of ROS which compared to controls (P < 0.05). Only the 100 μM BGP-15 treatment group had a higher MDA level than the control group (P < 0.05). In all BGP-15 treatment groups, the mRNA expressions of the ROMO1 gene were significantly reduced compared to controls (P < 0.05), and the mRNA expressions of the SMCP, MnSOD, and CuZnSOD genes were significantly increased (P < 0.05). While the difference in the mRNA expression of the SMOX gene between the 50 μM BGP-15 treatment group and the control group was not significant (P > 0.05). Moreover, the apoptosis rate of freeze-thawed spermatozoa significantly decreased in the 100 μM BGP-15 treatment group compared to the control (P < 0.05), while the MMP of freeze-thawed spermatozoa significantly enhanced in the 100 μM BGP-15 treatment group (P < 0.05). In conclusion, BGP-15 enhances cryo-protective effects on goat spermatozoa, and 100 μM BGP-15 addition to the extender during cryopreservation is beneficial to the goat breeding industry.

01 Jun 2025·Cellular Signalling

PUS1 facilitates cell migration in clear cell renal cell carcinoma through the promotion of mRNA pseudouridylation and the stabilization of the SMOX gene

Article

Author: Liu, Yuepeng ; Gu, Junfei ; Shi, Bei ; Zhu, Meng ; Chen, Yao ; Zhang, Bowei ; Cao, Yilong ; Zeng, Bowen ; Li, Jiehan ; Li, Xiaoling ; Lv, Jingwei ; Xu, Chao ; Sun, Qingyun ; Zhang, Sujing ; Dai, Shengtao

Clear cell renal cell carcinoma (ccRCC) is a highly aggressive malignancy characterized by its propensity for metastasis. Pseudouridine synthase 1 (PUS1), an enzyme involved in RNA modification, has been implicated in cancer progression, but its role in ccRCC remains unclear. This study investigates PUS1's role in ccRCC and evaluates its potential as a prognostic biomarker and therapeutic target. We assessed PUS1 expression in 541 ccRCC samples from The Cancer Genome Atlas (TCGA) and utilized Receiver Operating Characteristic (ROC) analyses to determine its prognostic value. High PUS1 levels were associated with reduced overall and disease-specific survival in ccRCC patients. Functional assays demonstrated that PUS1 promotes cell migration by stabilizing SMOX mRNA via pseudouridylation. The transcription factor USF1 regulates PUS1 expression by binding to its promoter region, enhancing its transcriptional activity. PUS1 silencing in ccRCC cell lines significantly reduced cell migration, while its overexpression had the opposite effect. These findings implicate the USF1-PUS1-SMOX signaling axis in regulating the migratory abilities of ccRCC cells. In conclusion, PUS1 plays a pivotal role in ccRCC progression and serves as an independent prognostic biomarker. Targeting PUS1 may offer promising therapeutic strategies for ccRCC patients. Further research is needed to explore its function in other cancers and to clarify its underlying molecular mechanisms.

02 Apr 2025·Antimicrobial Agents and Chemotherapy

Mutant prevention concentrations and phenotypic and genomic profiling of first-step resistance mechanisms to classical and novel β-lactams in Pseudomonas aeruginosa

Article

Author: Sastre-Femenia, Miquel Àngel ; Oliver, Antonio ; Gomis-Font, Maria Antonia

ABSTRACT A growing number of novel antipseudomonal β-lactams have been introduced in recent years, but the emergence of resistance is still a major concern in the treatment of Pseudomonas aeruginosa infections. Here, we compared the mutant prevention concentrations (MPCs) and the nature of first-step resistant mutants to classical and novel β-lactams in P. aeruginosa . MPCs were determined in duplicate experiments for ceftazidime, ceftazidime/avibactam, ceftolozane/tazobactam, imipenem, imipenem/relebactam, meropenem, meropenem/vaborbactam, aztreonam, aztreonam/avibactam, and cefiderocol in PAO1, PAOMS (Δ mutS ), and three extensively drug-resistant (XDR) clinical strains belonging to high-risk clones ST111, ST175, and ST235. Four mutants per strain and antibiotic, obtained from the highest concentration showing growth, were characterized through the determination of the susceptibility profiles and whole genome sequencing. Imipenem/relebactam presented the lowest MPC values, followed by ceftolozane/tazobactam. Overall, the MICs of the mutants were consistent with the antibiotic selection concentration, except for cefiderocol, which were much lower. MPCs were lower for ceftazidime/avibactam and imipenem/relebactam than those of the corresponding β-lactam alone. In contrast, MPCs of meropenem ± vaborbactam and aztreonam ± avibactam were identical in most strains. Ceftolozane/tazobactam and ceftazidime/avibactam derivatives presented mutations in ampC , galU , cpxRS, and/or in bla OXA-2 when present in the parent strain (ST235). Cefiderocol mutants were mainly defective in iron-uptake systems, particularly PiuA/DC. All carbapenems had oprD as the first-step mechanism. Imipenem/relebactam, meropenem ± vaborbactam, and aztreonam ± avibactam selected mutations frequently included efflux pumps and regulators. Imipenem ± relebactam also selected aroB mutations. This work first describes the MPCs and first-step resistance mechanisms for classical and novel β-lactams in P. aeruginosa . The identified shared and differential resistance development patterns between the available classical and novel β-lactams should be helpful to guide treatment strategies for XDR P. aeruginosa infections.

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