Recombinant human DPP3 protein

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The protein DPP3 short for Dipeptidyl Peptidase 3 is an enzyme with a mass of approximately 82 kDa. It belongs to the M49 family of metallopeptidases and is widely expressed in human tissues including kidney heart liver and brain. This enzyme has the function of cleaving dipeptides from the N-terminus of polypeptides. Alternative names for DPP3 include DPP III and dipeptidyl peptidase III. By breaking down peptides DPP3 plays an important role in proteolysis.

Biological function summary

DPP3 influences several physiological processes. It is reported to participate in the degradation of enkephalins which are neuropeptides involved in regulating pain. DPP3 does not form part of a larger complex but operates independently within cells to execute its functions. By degrading its substrates DPP3 helps modulate peptide signaling pathways and maintain cellular homeostasis.

Pathways

DPP3 has significant involvement in the enkephalin degradation pathway which is essential in pain modulation and stress responses. It also plays a part in the ubiquitin-proteasome pathway facilitating the degradation of damaged or misfolded proteins. DPP3 interacts with proteins such as the ubiquitin-conjugating enzyme influencing protein turnover processes.

DPP3 links closely to cardiovascular diseases and cancer. Elevated levels of DPP3 are observed in heart failure where it may disrupt normal peptide balance and contribute to disease progression. Additionally its relationship with proteins such as angiotensin-converting enzyme (ACE) may affect blood pressure regulation. In certain cancers DPP3 expression changes can influence tumor growth by altering peptide-mediated signaling pathways with its interactions suggesting potential as a therapeutic target.