Diagnostic enzyme White Glutamate Dehydrogenase Assay CAS NO 9029-12-3

The CAS number of Glutamate Dehydrogenase (GDH) is 9029-12-3. It is a mitochondrial enzyme that is commonly found in animals, plants, and microorganisms. It belongs to the amino acid dehydrogenase superfamily and plays a key role in the metabolism of nitrogen and carbon in organisms. In general, this enzyme catalyzes the reversible oxidation and deamination of L-glutamate using NAD+and/or NADP+as coenzymes, producing α - ketoglutarate, which participates in the tricarboxylic acid cycle (TCA cycle), signal transduction, regulation of nitrogen and carbon metabolism, and other physiological activities. It plays an important role in energy regulation and maintaining cellular homeostasis.

Many studies have shown that although glutamine can be synthesized in most tissues, its demand often exceeds supply. Glutamine is usually an essential nutrient for cell proliferation. More and more studies have shown that glutamine metabolism plays an important role in tumor growth, proliferation, and metastasis. In many cancer cells, glutamine is the main mitochondrial substrate, and glutamate dehydrogenase is one of the key enzymes in the glutamine metabolic pathway. Therefore, glutamate dehydrogenase is also very important for tumor cells.

Some studies have found that human breast cancer cells assimilate ammonia mainly through glutamic acid dehydrogenase catalytic reduction of amine, thus accelerating the proliferation of breast cancer cells. Ryu et al. found through experiments that the expression level of glutamate dehydrogenase also increased to some extent in canine breast tumor cells. Therefore, specifically inhibiting the expression level and activity of glutamate dehydrogenase in breast cancer cells may have the potential to inhibit the proliferation and proliferation of breast cancer cells.

In patients with liver disease, the activity of glutamate dehydrogenase in liver cancer cells is significantly lower than that in adjacent normal or cirrhotic liver cells. In addition, the overall glutamate dehydrogenase activity of all tumor cells is 30% lower than that of normal and cirrhotic liver cells. After liver cell necrosis and mitochondrial disintegration, GDH will escape from cells and enter the bloodstream. The increase in plasma GDH in liver cancer patients is most significant. Therefore, measuring the activity and content of GDH in serum can be used as an indicator for the diagnosis of mitochondrial damage and liver cell lesions.

Colorectal cancer is the third most common new type of cancer, and its mortality rate ranks third among all cancers, making it one of the cancers with higher mortality rates. According to relevant reports, the 5-year survival rate for patients diagnosed with local colorectal cancer is 90%, which decreases to 68% after local spread and sharply drops to 10% after distant spread. Liu et al. found that the expression level of GDH in colorectal cancer cells is higher than that in corresponding non tumor cells. Overexpression of GDH is related to the migration ability and tumor size of colorectal cancer. The higher the expression level of GDH, the stronger the tumor migration ability and the larger the tumor size. When shRNA is used to inhibit the gene encoding GDH, the proliferation and migration ability of colorectal cancer cells significantly decrease.

From this, it can be seen that glutamate dehydrogenase is of great significance for the examination of tumors and cancers. More and more evidence shows that GDH is closely related to the proliferation, migration, invasion and other activities of tumor cells, and there is an abnormal increase in expression in many tumor cells. GDH is gradually becoming a potential target for cancer treatment, and the screening of GDH inhibitors may gradually become a research hotspot.

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