This website uses cookies to ensure you get the best experience on our website.
- Table of Contents
1 Citations 5 Q&As
Facts about Glutathione peroxidase 1.
Human | |
---|---|
Gene Name: | GPX1 |
Uniprot: | P07203 |
Entrez: | 2876 |
Belongs to: |
---|
glutathione peroxidase family |
Cellular glutathione peroxidase; CGPx; EC 1.11.1; EC 1.11.1.9; Glutathione Peroxidase 1; GPX1; GPx-1; GSHPX1; GSHPx-1; MGC14399; MGC88245
Mass (kDA):
22.088 kDA
Human | |
---|---|
Location: | 3p21.31 |
Sequence: | 3; NC_000003.12 (49357171..49358600, complement) |
Cytoplasm.
GPX1 is a critical antioxidant in the human body. This article will discuss the role of GPX1 in the protection of the liver and hucMSC-Ex mediated antioxidant activity. In addition, we will explain why GPX1 is an important human antioxidant. Here are some of the best uses for this product. All Boster scientists can benefit from this product.
The role of GPX1 in hepatic oxidative injury has been suggested by several studies. The molecule is a major antioxidant enzyme. Mice lacking GPx1 were healthy, fertile, and had a delayed sensitivity to hyperoxia. Additionally, these mice could compensate for mild oxidative stress, suggesting that the enzyme is required for liver protection.
In this study, MSC-ex inhibited the a-SMA and xCT gene expression. The two chemotherapeutic agents decreased GPX1 mRNA expression, indicating that MSC-ex reduced the levels of these two cytokines in liver cells. These chemotherapeutic agents also induced ferroptosis in MSC-ex-treated mice.
Although not completely understood, GPX1 may be associated with metabolic and energy-related diseases. The GPX enzyme is an important regulator of insulin physiology and regulates glucose and lipid metabolism. Hence, increased GPX activity may be beneficial in the treatment of insulin-dependent diseases, such as diabetes. Its role is important in protecting liver from oxidative stress and preventing cellular damage.
Studies of the role of GPX1 in hucMSC-Ex-induced antioxidant activity and liver protection in mice were conducted by Li HJ and Serewko MM. In particular, Li HJ induced cancer stem cell niches in the esophagus. In addition, the GPX1 gene facilitated GPX1-mediated antioxidant activity and liver protection in mouse models.
The study also found that GPX1 is a therapeutic target for human liver cancer stem cells. The findings are supported by a large number of previous studies. These studies also support the use of HSCs as a natural liver protection agent. This research has many implications for the treatment of liver disease. The role of HSCs in hepatic fibrosis should be further explored.
However, the protective effect of MSC-ex in MSCs is dependent on BECN1. Its down-regulation inhibits ferroptosis, and BECN1 knockdown delays HSC-ex-mediated ferroptosis. Therefore, BECN1 could be a new therapeutic approach for the treatment of liver fibrosis.
The effect of GPX1 on hucMSC-Ex-derived exosomes on liver regeneration is largely unknown. However, it has been demonstrated that exosomes are involved in repair and regeneration of skin tissue in a rat skin photodamage model. Subcutaneous injection of exosomes induced antioxidant activity and anti-inflammatory effects.
It has been shown that glutathione peroxidase-1 (GPX1) catalyzes a reaction between lipid and hydrogen peroxide, which creates a glutathione-peroxide bridge. Catalase, another important enzyme in the glutathione redox cycle, detoxifies hydrogen peroxides. GPX1 is involved in liver protection in a number of physiological processes, including cell adhesion and survival.
Several studies have shown that GPX1 is a critical human antioxidative protein that may be involved in the development of cardiovascular diseases, such as atherosclerosis and atherosclerotic vascular disease. This review also discusses the regulatory factors that affect GPx activity, the relationship between GPx1 mRNA and GPx activity, and the roles of GPx in these chronic diseases.
A recent study linked a common GPX1 variant to life expectancy. In a Danish cohort of elderly people, researchers found that individuals with the heterozygous genotype rs1050450 had significantly longer life spans than the general population. The researchers speculated that the association could be due to a survival benefit of the 'AG' allele, but did not go into detail. Other studies have shown that the 'G' allele confers greater GPx activity than the 'A' allele.
One of the most important roles of GPX1 in the immune system is to protect against oxidative stress. Oxidative stress leads to the accumulation of ROS in cells and is associated with ageing and related diseases. GPx1 may also affect fertility. It has been reported that free radicals can fragment spermatozoa in women and cause ovarian failure in men. GPx1 deficiency in mice results in direct tissue damage.
Despite upregulation of other antioxidant enzymes, GPx1 expression was significantly higher in ApoE-/ mice compared to controls. This suggests that GPx1 may have a role in limiting oxidative events in the diabetic milieu. Further, increased GPx1 levels were associated with higher staining for a marker of free radical damage. Several clinical studies have examined the role of GPx1 in atherosclerosis, but these have not yet addressed the role of GPx1 in atherogenesis.
In addition to its role in atherosclerosis prevention, GPx1 is also implicated in diabetes-associated atherosclerosis. Moreover, mice deficient in GPx1 have reduced apolipoprotein E levels, indicating that diabetes-related atherosclerosis is mediated by lack of GPx1. Therefore, GPx1 is a therapeutic target for treating diabetic-related atherosclerosis.
GPX1 is abundant in hucMSCs and hucMSC-Ex, a cell line that promotes GPX activity. Moreover, knockdown of GPX1 in hucMSC-Ex cells inhibited the promotion of Gpx activity and reduced the rescue of CCl4-induced liver injury in mice. However, GPX1 knockdown inhibited the promotion of Gpx activity in hucMSC-Ex-treated L02 cells.
GPX1 is a critical human antioxidative enzyme. It is regulated by a sequence called the SECIS element that encodes the gene. GPx1 is expressed in the body only when there is sufficient supply of selenocysteine (Se) in the body. The gene expression of GPx1 is also affected by selenoproteins and other antioxidant enzymes. Low levels of Se increase free radicals, which may contribute to aging and mortality among people over 65.
GPX1 protects the cochlear spiral ganglion neurons from peroxynitrite-induced damage. This protective mechanism involves inhibiting nuclear factor kappa B (NF-kB), which is involved in the formation of peroxynitrite. Therefore, it may represent a novel target for the prevention of nitrogen radicals. This finding may have broad implications for future research in the area of nitrogen radical prevention.
To test for GPX1 activity, mice were given a diet containing 2.5% Avertin. Mice were then sacrificed by rapid thoracic opening. The hearts were removed and placed in icy cold saline. The tissue from the aortic sinus was dissected under a dissecting microscope and stored at -70degC. Total RNA was isolated from the tissue by using the TRIzol(r) reagent. DNA-free DNase was used to remove contaminating DNA.
The underlying mechanisms of GPX1 in cancer prevention and treatment are unclear. While GpX1 contributes to a protective mechanism against cancer, it is also involved in a wide variety of cellular processes, including metabolism. Inflammatory diseases, including diabetes, may reduce GPX1 levels. Furthermore, it is important to assess whether antioxidant enzymes are functioning properly in the body. Moreover, antioxidant enzymes play a crucial role in the prevention of oxidative stress in hospital settings.
However, in a study of diabetic mice, GPX1 deficiency leads to an increased expression of profibrotic growth factor CTGF. The increased expression of CTGF in diabetic ApoE/GPx1 mice supported the observation that ROS-mediated CTGF expression may be involved in the development of atherosclerosis. The authors concluded that these results indicate that GPx1 is a critical human antioxidant.
PMID: 3658677 by Sukenaga Y., et al. cDNA sequence coding for human glutathione peroxidase.
PMID: 3697069 by Ishida K., et al. Nucleotide sequence of a human gene for glutathione peroxidase.
*More publications can be found for each product on its corresponding product page