جستجوی مقالات مرتبط با کلیدواژه "p53 protein" در نشریات گروه "پزشکی"

Apoptosis is regulated by a complex interplay of gene products that either activate or inhibit this process. This study aimed at assessing the combined impact of nanocurcumin supplementation and resistance training on TERF2 (Telomeric Repeat Binding Factor 2) gene expression and the p21-p53 axis in the muscle tissue of male rats.

In this experimental study, 24 male Wistar rats were randomly allocated into four groups: a healthy control group, a resistance training group, a nanocurcumin group, and a resistance training + nanocurcumin group. Resistance training was conducted over a 4-week period following a specific protocol. Concurrently, rats in the nanocurcumin groups received 80 mg of the supplement per kilogram of body weight. The expression levels of TERF2, p53, and p21 genes were assessed using the Real-Time PCR method.

The results showed significant differences in the expression levels of TERF2, p53, and p21 genes among the four groups (P<0.05). In the resistance training + nanocurcumin group, the expression of TERF2, p53, and p21 genes was significantly higher compared to the control group (P<0.05). Additionally, p53 gene expression in the resistance training group was significantly higher than in the nanocurcumin supplement group (P<0.05). The combined resistance training and nanocurcumin supplementation did not significantly affect the expression of the TERF2 gene in the muscle tissue of male rats compared to either training or supplementation alone (P<0.05). Furthermore, the synergistic effect of resistance training and supplementation significantly increased the expression of p21 and p53 genes (P<0.05).

Resistance training and nanocurcumin supplementation enhance TERF2 gene expression, potentially reducing telomere shortening and aging. Moreover, the upregulation of p53 and p21 gene expression during resistance training and nanocurcumin supplementation may induce cell cycle arrest and apoptosis.

Chronic hyperglycemia is associated with an increase in cellular damage due to oxidative stress and increases insulin resistance and also increases in p53 and p16 beta cells, leading to the induction of senescence in pancreatic insulin-secreting cells. The aim of this study was the effect of eight weeks of aerobic exercise on the expression of senescence proteins P53 and P16 in the pancreatic tissue of diabetic mice.

In this study, 15 NMRI mice (26.3 ±3.22 g) were divided into three groups randomly: healthy control, diabetic control and diabetic exercise. They were diabetic by HFD for 5 weeks and intraperitoneal injection of STZ. The aerobic training protocol (50-60% Vmax) was 5 days a week for 8 weeks. After anesthesia, blood and pancreatic tissue were removed. Insulin resistance, P53 and P16 protein concentrations in pancreatic beta cells were measured. Data were analyzed by ANOVA with a significance level of p <0.05.

According to the results of eight weeks of aerobic exercise by mice diabetic type 2, a significant decrease in insulin resistance (p = 0.005), protein concentrations of P53 (p = 0.002) and P16 (p = 0.010) in pancreatic tissue was observed.

Aerobic exercise may improve insulin sensitivity and delay cellular senescence due to diabetes by reducing cell senescence factors such as P53 and P16 in beta cells. Therefore, this type of exercise can be considered as a therapeutic approach to improve the condition of these patients.

P53 is a tumor suppressor protein with numerous missense mutations identified in its gene. These mutations are observed in a vast number of cancers. R213G is one of them which has a role in metastatic lung cancers. In this research, R213G was studied in comparison with the wild type via molecular dynamics simulation.

For the three-dimensional structure of the wild-type P53 protein, chain A was used from crystallographic structure with PDB ID: 1TSR.  For R213G mutation, residue 213 of this structure was changed to glycine. Molecular dynamics simulation was repeated twice for 15 ns using Gromacs 5.1.2 software package, AMBER99SB force field, and TIP3P as water model. RMSD, RMSF, radius of gyration, and potential energy analyses were performed on resulted trajectories.

RMSF analysis showed that the R213G mutation changes the flexibility of 11 residues including R-248. These residues are not near the mutated position, but all of them are located on 220-250 fragment of this domain or are residues in the neighbor of this fragment. The radius of gyration and potential energy results confirmed a reduction in stability of this protein as a result of this mutation.

RMSF analysis of R213G mutation beside the changes in stability and radius indicated that this mutation could greatly affect the P53 interactions with other macromolecules.