Background[1-3]
Fructokinase 6 phosphate 1 antibody is an immune protein isolated from the serum of germ-free animals after systemic immunization with fructokinase 6 phosphate 1. Fructokinase 6 phosphate 1 antibody can specifically bind to fructokinase 6 phosphate 1 and can be used as an antibody in the fructokinase 6 phosphate 1 ELSA kit.
Detection of 6-phosphofructokinase1 (PFK1) in the glycolysis pathway, which catalyzes fructose 6-phosphate to generate fructose 1,6-bisphosphate (Fructosel, 6bisphosphate, F-1, 6-BP) , which is the second phosphorylation reaction of the glycolysis pathway and requires the participation of ATP and Mg2+. 6-Phosphofructokinase 1 is the main rate-limiting enzyme in the glycolysis process and the main regulatory point in the glycolysis process. During glycolysis, fructose 6-phosphate generates fructosel, 6bisphosphate, F-1, 6-BP. The enzyme that catalyzes this reaction is 6-phosphofructokinase1 (PFK1). ), this is the second phosphorylation reaction of the glycolysis pathway, requiring the participation of ATP and Mg2+, ΔG”0=-14.2KJ/mol, the reaction is irreversible. During the glycolysis process, fructose-6-phosphate generates 1,6- Fructose diphosphate, the enzyme that catalyzes this reaction is 6-phosphofructokinase1 (PFK1), which is the second phosphorylation reaction of the glycolysis pathway and requires the participation of ATP and Mg2+, ΔG”0=-14.2 KJ/mol, the reaction is irreversible. 6-Phosphofructokinase 1 is the main rate-limiting enzyme in glycolysis and the main regulatory point in glycolysis. At this point, glycolysis has completed the first stage of metabolism.
Apply[4][5]
For research on the correlation between phenotypic differences of phosphofructokinase 1 and human breast cancer photoinitiators and glycolysis levels in adjacent tissue
From the perspective of energy metabolism, we compared the glycolysis levels and the phenotypic differences of the glycolytic metabolism rate-limiting enzyme phosphofructokinase 1 in human breast cancer and paracancerous tissues, trying to find out the effects of glycolytic metabolism in breast cancer. possible mechanisms to find new targets for breast cancer treatment. Enzymatic analysis is used to detect lactate content and lactate dehydrogenase activity in different stages of breast cancer and adjacent tissues, reflecting the differences in levels of glycolysis metabolism; and at the same time, it detects glycolysis metabolism rate-limiting enzymes, hexokinase, and phosphate The activities of fructokinase 1 and pyruvate kinase were used to initially explore the possible reasons for the differences in glycolysis levels of pearlescent pigments.
Use Western-Blot technology to detect the expression and phenotypic differences of phosphofructokinase 1 in breast cancer and paracancerous tissues, analyze its impact on phosphofructokinase 1 activity, and further explore the possible reasons for the difference in glycolysis levels . Western-Blot results were analyzed using Quantity One gel quantification software for grayscale analysis, and measurement data were expressed as mean ± standard deviation. The means of the two groups were compared using the t test and the count data using the χ2 test. Linear regression analysis was used to explore the correlation between the phenotypic differences of phosphofructokinase 1 and its activity. SPSS13.0 statistical software was used to analyze the experimental data. P<0.05 was considered significant. Statistical difference.
The proportion of P subtype in breast cancer tissue increases with the increase of pathological stage, and the proportion of M and L subtype decreases with the increase of pathological stage. Further correlation analysis showed that the expression of P isoform was positively correlated with the activity of phosphofructokinase 1, and the correlation was statistically significant (R2=0.9982, p=0.032); the expression of M isoform was positively correlated with the activity of phosphofructokinase 1 The activity was negatively correlated, but not statistically significant (R2=0.9694, p=0.107); the expression of L isoform was also negatively correlated with activity, but not statistically significant (R2=0.9274, p=0.178). In paracancerous tissue, the proportions of phosphofructokinase 1M, L and P isoforms in stages I, II and III were 8%: 70%: 22%, 3%: 71%: 26% and 12% respectively. : 64%: 24%, there is no obvious phenotypic difference in the expression of phosphofructokinase 1 between each pathological stage.
