Target Name: DPP4
NCBI ID: G1803
Other Name(s): Dipeptidyl peptidase IV | CD26 | adenosine deaminase complexing protein 2 | Dipeptidyl peptidase IV membrane form | Dipeptidyl peptidase 4 | Dipeptidyl peptidase 4 soluble form | dipeptidylpeptidase 4 | Dipeptidyl peptidase 4 membrane form | DPP IV | dipeptidyl peptidase IV | ADABP | Dipeptidyl peptidase 4, transcript variant 1 | DPP4_HUMAN | Post-proline dipeptidyl aminopeptidase IV | Dipeptidyl peptidase IV soluble form | ADCP2 | Adenosine deaminase complexing protein 2 | TP103 | Gly-Pro naphthylamidase | Dipeptidyl peptidase 4 (isoform 1) | dipeptidylpeptidase IV (CD26, adenosine deaminase complexing protein 2) | dipeptidyl peptidase 4 | Xaa-Pro-dipeptidylaminopeptidase | T-cell activation antigen CD26 | ADCP-2 | DPP4 variant 1 | DPPIV

DPP4: A Drug Target / Disease Biomarker

DPP4 (DNA-protein phosphatase 4) is a protein that is expressed in various tissues and cells throughout the body. It plays a crucial role in the regulation of DNA replication, repair, and aging. Discovered in 1999, DPP4 has since been shown to be involved in a wide range of physiological processes, including cell growth, apoptosis, angiogenesis, and inflammation. As a result, DPP4 has gained significant interest as a potential drug target or biomarker.

DPP4 functions as a critical enzyme in the DNA damage repair pathway. During DNA replication, DPP4 is involved in the repair of DNA double-strand breaks and single-strand breaks. In addition, DPP4 is involved in the regulation of DNA replication efficiency, which is critical for maintaining accurate genetic information in the cell.

DPP4 has also been shown to play a key role in the regulation of cell apoptosis. When cells are exposed to DNA damage or other stressors, DPP4 triggers the production of reactive oxygen species (ROS) that can cause cell death. This is essential for understanding the mechanisms underlying cellular stress and aging, as well as the potential therapeutic applications of DPP4 as a drug target.

DPP4 has also been shown to be involved in the regulation of angiogenesis, the process by which new blood vessels are formed in the body. Angiogenesis is a critical process for maintaining blood flow and oxygenation in the body, and it is often disrupted in diseases such as cancer and cardiovascular disease. The role of DPP4 in this process suggests that it may be a useful target for new therapies aimed at preventing or treating these diseases.

DPP4 has also been shown to be involved in the regulation of inflammation. Inflammation is a critical immune response that helps the body to heal from injuries and illnesses. However, chronic inflammation can lead to a host of diseases, including heart disease and cancer. The role of DPP4 in the regulation of inflammation suggests that it may be a useful target for new therapies aimed at preventing or treating these diseases.

In conclusion, DPP4 is a protein that is involved in a wide range of physiological processes in the body. Its role in DNA replication, apoptosis, angiogenesis, and inflammation makes it a potential drug target or biomarker. Further research is needed to fully understand the mechanisms underlying the functions of DPP4, as well as its potential therapeutic applications.

Protein Name: Dipeptidyl Peptidase 4

Functions: Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation (PubMed:10951221, PubMed:10900005, PubMed:11772392, PubMed:17287217). Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC (PubMed:10951221, PubMed:10900005, PubMed:11772392, PubMed:14691230). Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (PubMed:17287217). Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion (PubMed:11772392). In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM (PubMed:16651416, PubMed:10593948). May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation (PubMed:18708048). When overexpressed, enhanced cell proliferation, a process inhibited by GPC3 (PubMed:17549790). Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones such as brain natriuretic peptide 32 (PubMed:16254193, PubMed:10570924). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline (PubMed:10593948)

More Common Targets

DPP6 | DPP7 | DPP8 | DPP9 | DPP9-AS1 | DPPA2 | DPPA2P3 | DPPA3 | DPPA3P1 | DPPA3P2 | DPPA4 | DPPA4P3 | DPPA5 | DPPA5P4 | DPRX | DPRXP2 | DPRXP4 | DPT | DPY19L1 | DPY19L1P1 | DPY19L2 | DPY19L2P1 | DPY19L2P2 | DPY19L2P3 | DPY19L2P4 | DPY19L3 | DPY19L3-DT | DPY19L4 | DPY30 | DPYD | DPYD-AS1 | DPYS | DPYSL2 | DPYSL3 | DPYSL4 | DPYSL5 | DQX1 | DR1 | DRAIC | DRAM1 | DRAM2 | DRAP1 | DRAXIN | DRB sensitivity-inducing factor complex | DRC1 | DRC3 | DRC7 | DRD1 | DRD2 | DRD3 | DRD4 | DRD5 | DRD5P1 | DRD5P2 | DRG1 | DRG2 | DRGX | DRICH1 | DROSHA | DRP2 | DSC1 | DSC2 | DSC3 | DSCAM | DSCAM-AS1 | DSCAML1 | DSCC1 | DSCR10 | DSCR4 | DSCR8 | DSCR9 | DSE | DSEL | DSEL-AS1 | DSG1 | DSG1-AS1 | DSG2 | DSG3 | DSG4 | DSN1 | DSP | DSP-AS1 | DSPP | DST | DST-AS1 | DSTN | DSTNP2 | DSTYK | DTD1 | DTD1-AS1 | DTD2 | DTHD1 | DTL | DTNA | DTNB | DTNB-AS1 | DTNBP1 | DTWD1 | DTWD2 | DTX1