Unlocking the Potential of PEPD: A Promising Drug Target and Biomarker

Target Name: PEPD

NCBI ID: G5184

Unlocking the Potential of PEPD: A Promising Drug Target and Biomarker

Introduction

PEPD (Imidodipeptidase), a 26-kDa serine proteases enzyme, is a crucial enzyme in the degradation of imidodipeptides, a common peptide derived from amino-rich regions often found in therapeutic proteins. Imidodipeptides have been identified as potential drug targets in various diseases, including cancer, neurodegenerative disorders, and autoimmune diseases. The discovery of PEPD as a drug target and biomarker has significant implications for the development of new therapeutic approaches.

PEPD's Unique Characteristics

PEPD is an elongated single-chain serine proteases enzyme that catalyzes the hydrolysis of the imidodipeptide bond between the N-terminus and the C-terminus. It is highly specific for its substrate, showing only low levels of activity towards other types of peptides. This specificity is due to the unique structural features of its active site, which is composed of a short alkaline region, a hydrophobic middle region, and a long alkaline region. This creates a favorable environment for the formation of a stable, monophosphate salt, allowing for efficient proteolysis.

PEPD's Expression and Regulation

PEPD is highly expressed in various tissues, including pancreatic, spleen, heart, and liver, but its levels are generally low. Its expression is regulated by several factors, including tissue-specific suppressors, such as hypoxia, growth factors, and cytokines. Additionally , its levels are also regulated by its own degradation, which is driven by its own catalytic activity.

PEPD's Potential as a Drug Target

PEPD's unique properties and low expression levels make it an attractive drug target. Studies have shown that inhibition of PEPD can lead to significant improvements in the efficacy of various therapeutic proteins, including those for cancer, neurodegenerative diseases, and autoimmune diseases.

For example, in neurodegenerative diseases,PEPD has been shown to be involved in the progression of neurodegeneration. By inhibiting PEPD, researchers have been able to increase the lifespan of neurodegenerate disease model animals and improve cognitive function in animal models of Alzheimer's disease.

In addition, PEPD has also been shown to be a potential target for cancer. PEPD has been found to be overexpressed in various types of cancer, including breast, lung, and colorectal cancer. inhibition of PEPD has been shown to be an effective way to enhance the efficacy of cancer therapies.

PEPD's Potential as a Biomarker

PEPD's unique properties also make it an attractive biomarker for several diseases. Its low expression levels and stable activity make it a reliable marker for the diagnosis and monitoring of various diseases.

For example, in cancer, PEPD has been shown to be a potential biomarker for the diagnosis and prognosis of several types of cancer. Its expression has been found to be correlated with the severity of cancer and the response to chemotherapy. Additionally, its levels have has also been shown to be decreased in the serum of patients with cancer, making them a potential indicator of disease recurrence.

In addition, PEPD has also been shown to be a potential biomarker for neurodegenerative diseases. Its levels have been found to be decreased in the brain of individuals with neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. This suggests that PEPD may be an effective diagnostic tool for neurodegenerative diseases.

Conclusion

PEPD is a unique and highly specific enzyme with significant potential as a drug target and biomarker. Its low expression levels and stable activity make it an attractive target for the development of new therapeutic approaches for a variety of diseases. The results of recent studies suggest that inhibition of PEPD may be an effective way to improve the

Protein Name: Peptidase D

Functions: Dipeptidase that catalyzes the hydrolysis of dipeptides with a prolyl (Xaa-Pro) or hydroxyprolyl residue in the C-terminal position (PubMed:17081196, PubMed:35165443). The preferred dipeptide substrate is Gly-Pro, but other Xaa-Pro dipeptides, such as Ala-Pro, Met-Pro, Phe-Pro, Val-Pro and Leu-Pro, can be cleaved (PubMed:17081196). Plays an important role in collagen metabolism because the high level of iminoacids in collagen (PubMed:2925654)

More Common Targets