AGK is a key metabolic enzyme, mainly present in the muscles, hearts and brain tissues of vertebrates. It catalyzes the reversible reaction between creatine and adenosine triphosphate (ATP), generating creatine phosphate and adenosine diphosphate (ADP), thereby rapidly providing energy reserves for cellular activities, especially playing a significant role during intense exercise or high energy consumption. AGK was first isolated in the mid-20th century. The study of its structure and function provides an important basis for the regulation of energy metabolism, muscle physiology and the diagnosis of related diseases (such as myocardial infarction). As a core molecule in metabolic pathways, the efficient reaction mechanism and tissue-specific distribution of AGK make it one of the research hotspots in biochemistry and clinical medicine.
AGK is a key metabolic enzyme with a molecular weight of approximately 24-26 kDa. Its specific size may vary slightly depending on the species and post-translational modifications (such as phosphorylation).
| Species | Human | Mouse | Rats | Bovine |
| Molecular Weight (kDa) | 25.5 | 25.3 | 25.4 | 25.6 |
| Primary Structural Differences | Conserved catalytic domain | Highly homologous and functionally similar | Highly similar to human AGK | Similar role in lipid metabolism |
AGK catalyzes the phosphorylation of acylglycerol (such as monoacylglycerol) through the conserved phosphorylation site of its active center, participating in lipid signal transduction and energy metabolism regulation. Its structural stability depends on the hydrophobic core and key disulfide bonds, ensuring that it still maintains functional activity under cellular stress conditions.
Fig. 1 AGK deficiency enhances the anti-tumor immune function of TAMs through the cGAS-STING-I interferon pathway.1
Key structural properties of AGK:
AGK is a key metabolic enzyme, mainly involved in lipid metabolism and energy homeostasis regulation, and plays an important role in various physiological processes at the same time.
| Function | Description |
| Lipid phosphorylation | Catalyze the phosphorylation of monoacylglycerol (MAG) and diacylglycerol (DAG), generating lysophosphatidic acid (LPA) and phosphatidic acid (PA), and regulate lipid signaling. |
| Regulation of energy metabolism | By generating phosphatidic acid involved in three acylglycerol (TAG) synthesis and mitochondria beta oxidation, affecting cell energy supply. |
| Maintenance of mitochondrial function | Some subtypes are located in mitochondria, participate in cardiolipin metabolism, and affect the stability of mitochondrial membranes and the efficiency of electron transport chains. |
| Cell signal transduction | Its product LPA can act as a signaling molecule to activate G protein-coupled receptors (GPCRs), regulating cell proliferation, migration and inflammatory responses. |
| Disease association | Abnormal expression of AGK is associated with metabolic syndrome, cardiovascular diseases and certain cancers, and may become a potential therapeutic target. |
The enzymatic activity of AGK is regulated by ATP/ADP levels, phosphorylation modification and subcellular localization. Its substrate preferences (such as selectivity for MAG vs DAG) may vary in different tissues.
1. Huang, Shanshan, et al. "Up-regulated acylglycerol kinase (AGK) expression associates with gastric cancer progression through the formation of a novel YAP1-AGK–positive loop." Journal of Cellular and Molecular Medicine 24.19 (2020): 11133-11145. https://doi.org/10.1111/jcmm.15613
This article indicates that the research on AGK antibodies has found that AGK is highly expressed in gastric cancer and is associated with a poor prognosis. AGK promotes tumor proliferation and metastasis by activating the YAP1/TEAD signaling pathway. Meanwhile, YAP1 can trans-activate the expression of AGK, forming a positive feedback loop. AGK antibodies can be used as potential research tools.
2. Zhu, Qian, et al. "Acylglycerol kinase promotes tumour growth and metastasis via activating the PI3K/AKT/GSK3β signalling pathway in renal cell carcinoma." Journal of hematology & oncology 13 (2020): 1-16. https://doi.org/10.1186/s13045-019-0840-4
This article indicates that AGK, as a novel lipid kinase, may play a pro-cancer role in metastatic renal cell carcinoma. Its expression characteristics are related to the poor prognosis of patients and may become a new therapeutic target.
3. Du, Qiuyang, et al. "Acylglycerol kinase inhibits macrophage anti-tumor activity via limiting mtDNA release and cGAS-STING-type I IFN response." Theranostics 15.4 (2025): 1304. https://www.thno.org/v15p1304.htm
Studies have found that AGK deficiency in macrophages activates the cGAS-STING-I interferon pathway by inducing mitochondrial damage and mtDNA release, thereby enhancing the anti-tumor immunity of CD8+T cells (based on experimental evidence from the B16/LLC mouse model).
4. Sun, Fei, et al. "Acylglycerol kinase promotes ovarian cancer progression and regulates mitochondria function by interacting with ribosomal protein L39." Journal of Experimental & Clinical Cancer Research 41.1 (2022): 238. https://doi.org/10.1186/s13046-022-02448-5
Studies have found that AGK is highly expressed in ovarian cancer. It maintains mitochondrial function by binding to RPL39, promotes the characteristics of tumor stem cells and cisplatin resistance (based on clinical samples and in vivo and in vitro experimental evidence).
5. Zhang, Zhibo, et al. "Netupitant Inhibits the Proliferation of Breast Cancer Cells by Targeting AGK." Cancers 16.22 (2024): 3807. https://doi.org/10.3390/cancers16223807
Studies have found that the anti-tumor drug Netupitant inhibits the kinase activity of AGK by targeting it and blocks the PI3K/AKT/mTOR pathway, thereby suppressing the proliferation of breast cancer cells and inducing apoptosis (based on in vitro and nude mouse experimental evidence).
Creative Biolabs specializes in the production of high-quality AGK antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Western Blot, Flow Cytometry, Immunohistochemistry, and other diagnostic methodologies.
For more details on our AGK antibodies, custom preparations, or technical support, contact us at info@creative-biolabs.com.
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