DPP9: A Potential Drug Target and Biomarker (G91039)

Target Name: DPP9

NCBI ID: G91039

DPP9

DPP9: A Potential Drug Target and Biomarker

DPP9 (Dipeptidyl peptidase IX) is a protein that is expressed in various tissues of the body, including the brain, pancreas, and gastrointestinal tract. It is involved in the breakdown of a specific type of protein called dipeptide, which is a key component of proteins. This protein is a potential drug target and biomarker for various diseases, including cancer, diabetes, and neurological disorders.

The Role of DPP9 in Diabetes

DPP9 is a key enzyme in the breakdown of dipeptides, which is a key component of proteins. In the context of diabetes, the breakdown of dipeptides can contribute to the development and progression of the disease. DPP9 has been shown to be involved in the regulation of insulin sensitivity, and it has been suggested as a potential drug target for treating diabetes.

One of the mechanisms through which DPP9 may contribute to diabetes is by regulating the activity of the enzyme GLUT1. GLUT1 is a gene that is responsible for the absorption of glucose into the body's cells. In diabetes, the activity of GLUT1 is often impaired, leading to reduced insulin sensitivity and an increased risk of developing complications.

DPP9 has been shown to regulate GLUT1 activity by interacting with its active site. This interaction may be a potential target for drugs that can improve GLUT1 function and increase insulin sensitivity in diabetes.

The Potential Role of DPP9 in Cancer

DPP9 has also been shown to be involved in the regulation of the immune response, which is a critical aspect of cancer development. In cancer, the immune system is often impaired, leading to a lack of immune surveillance and a increased risk of tumor progression.

DPP9 has been shown to play a role in regulating the activity of the immune cell PD-L1. PD-L1 is a protein that is expressed in cancer cells and helps to suppress the immune response. DPP9 has been shown to interact with PD-L1 and regulate its activity, which may be a potential target for cancer treatments.

The Potential Role of DPP9 in Neurological Disorders

DPP9 is also involved in the regulation of the nervous system, and has been suggested as a potential drug target for treating neurological disorders. In neurological disorders, such as Alzheimer's disease and Parkinson's disease, the breakdown of dipeptides may contribute to the development and progression of the disease.

DPP9 has been shown to interact with the protein tau, which is a component of the neurodegenerative protein beta-amyloid. beta-amyloid is a hallmark of Alzheimer's disease, and its accumulation in the brain is thought to contribute to the development and progression of the disease. DPP9 has been shown to regulate tau activity by interacting with its active site, which may be a potential target for drugs that can reduce the accumulation of beta-amyloid in the brain.

Conclusion

DPP9 is a protein that is involved in the breakdown of dipeptides, which is a key component of proteins. In the context of diabetes, DPP9 has been shown to be involved in the regulation of insulin sensitivity and may be a potential drug target for treating the disease. It has also been suggested as a potential target for cancer treatments due to its involvement in the regulation of the immune response. Additionally, DPP9 has been shown to interact with the protein tau, which is a component of the neurodegenerative protein beta-amyloid. This suggests that DPP9 may also be involved in the regulation of the nervous system and may be a potential drug target for treating neurological disorders. Further research is needed to fully understand the role of DPP9 in these diseases

Protein Name: Dipeptidyl Peptidase 9

Functions: Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2 (PubMed:12662155, PubMed:16475979, PubMed:19667070, PubMed:29382749, PubMed:30291141, PubMed:33731929). Acts as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing activation of NLRP1 and CARD8 (PubMed:27820798, PubMed:29967349, PubMed:30291141, PubMed:31525884, PubMed:32796818, PubMed:36357533). Sequesters the cleaved C-terminal part of NLRP1 and CARD8, which respectively constitute the active part of the NLRP1 and CARD8 inflammasomes, in a ternary complex, thereby preventing their oligomerization and activation (PubMed:34019797, PubMed:33731929, PubMed:33731932). The dipeptidyl peptidase activity is required to suppress NLRP1 and CARD8; however, neither NLRP1 nor CARD8 are bona fide substrates of DPP9, suggesting the existence of substrate(s) required for NLRP1 and CARD8 inhibition (PubMed:33731929)

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