Last update 19 Sep 2024

SMOX

Last update 19 Sep 2024

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

MDL-72527

Target

PAOX x SMOX

Mechanism

PAOX inhibitors [+2]

Active Org.

Veterans Administration Outpatient Clinic [+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

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

100 Clinical Results associated with SMOX

100 Translational Medicine associated with SMOX

0 Patents (Medical) associated with SMOX

463

Literatures (Medical) associated with SMOX

01 Oct 2024·Clinics and Research in Hepatology and Gastroenterology

Targeting SMOX for the treatment of hepatocellular carcinoma?

Author: Cheng, Chunming ; Tao, Yulei

Dysregulation of the polyamine metabolism is common in different cancer types. SMOX is upregulated in hepatocellular carcinoma (HCC) but the relationship between SMOX and liver inflammation and fibrosis, remains unclear. In this issue of Clin Res Hepatol Gastroenterol, Hu and colleagues find targeting SMOX can alleviate liver cancer progression.

01 Aug 2024·Clinics and Research in Hepatology and Gastroenterology

Spermine oxidase regulates liver inflammation and fibrosis through β-catenin pathway

Article

Author: Hu, Tingting ; Sun, Xuecheng ; Hong, Wandong ; Huang, Qingke ; Tang, Wenqing ; Zhang, Jie ; Wu, Wenzhi

BACKGROUNDSpermine oxidase (SMOX), an inducible enzyme involved in the catabolic pathway of polyamine, was found to be upregulated in hepatocellular carcinoma and might be an important oncogene of it in our previous studies. This study attempted to further investigate its relationship with liver inflammation and fibrosis both in vitro and in vivo.METHODSThe effect of SMOX inhibition on LPS-induced inflammatory response in mouse liver cell line AML12 was validated by using small interfering RNA or SMOX inhibitor MDL72527. Western blotting and immunofluorescence were utilized to verify whether LPS could induce β-catenin to transfer into the nucleus and whether it could be reversed by interfering with the expression of SMOX or using SMOX inhibitor. Then, the SMOX inhibitor MDL72527 and SMOX knockout mice were used to verify the hypothesis above in vivo.RESULTSThe expression of SMOX could be induced by LPS in AML12 cells. The inhibition of SMOX could inhibit LPS-induced inflammatory response in AML12 cells. LPS could induce β-catenin transfer from cytoplasm to nucleus, while SMOX downregulation or inhibition could partially reverse this process. In vivo intervention with SMOX inhibitor MDL72527 or SMOX knockout mice could significantly improve the damage of liver function, reduce intrahepatic inflammation, inhibit the nuclear transfer of β-catenin in liver tissue, and alleviate carbon tetrachloride-induced liver fibrosis in mice.CONCLUSIONSMOX can promote the inflammatory response and fibrosis of hepatocytes. It provides a new therapeutic strategy for hepatitis and liver fibrosis, inhibiting early liver cancer.

01 Aug 2024·Biopreservation and Biobanking

Effect of Trehalose Supplementation in Egg-Yolk-Free Extender on Conventional Parameters and Gene Expression Related to Reactive Oxygen Species, Apoptosis, and Motility of Frozen Dog Spermatozoa

Article

Author: Jeon, Yubyeol ; Yu, Il-Jeoung ; Ibrahim, Saddah ; Talha, Nabeel Abdelbagi Hamad ; Shin, Sangmin

The present study was conducted to evaluate the effects of trehalose supplementation in egg-yolk (EY)-free tris extender on dog spermatozoa. Pooled spermatozoa were diluted with extender 1 (EY-free tris extender supplemented with 0, 10, 15, 20, or 30 mM trehalose) and cooled (2 × 10⁸ sperm/mL) for 1 hour at 4°C. After that, extender 2 (extender 1 containing 1 M glycerol) was added (v:v) to the diluted sperm, loaded in 0.5-mL straws (1 × 10⁸ sperm/mL), and incubated at 4°C for 30 minutes. The sperm straws were frozen over liquid nitrogen (LN₂) vapor for 20 minutes and then plunged directly into LN₂. After thawing at 37°C for 25 seconds, sperm progressive motility (CASA), viability (SYBR-14/PI), apoptosis (Annexin V/PI), and reactive oxygen species (ROS; H₂DCFDA/PI) were evaluated. Thereafter, the optimal concentrations of trehalose were selected, and the gene expression of BAX, BCL2, NOX5, SMOX, OGG1, and ROMO1 was evaluated after freeze-thawing. Supplementation with 20 and 30 mM trehalose significantly increased sperm progressive motility and viability compared to the control. However, trehalose had no significant effect on sperm ROS or phosphatidylserine translocation index. There were minor numerical increases and decreases in gene expression when the selected optimal concentrations of trehalose (20 and 30 mM) were compared to the control. However, there were no significant differences. We conclude that the addition of trehalose (20 and 30 mM) in EY-free extender could improve sperm motility and viability without significant effects on ROS, apoptosis, or gene expression.

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