PM20D1: A Promising Drug Target and Biomarker for Carboxypeptidase PM20D1-Positive Chronic Pain

Target Name: PM20D1

NCBI ID: G148811

PM20D1

PM20D1: A Promising Drug Target and Biomarker for Carboxypeptidase PM20D1-Positive Chronic Pain

Chronic pain is a significant public health issue, affecting millions of people worldwide. The persistent nature of pain, its impact on quality of life, and the limitations in available treatments have led to a growing interest in identifying new targets for pain modulation. One promising candidate for drug development is PM20D1, a carboxypeptidase (CPS) enzyme with unique functions in the regulation of protein synthesis and degradation. In this article, we will discuss the potential of PM20D1 as a drug target and biomarker for the treatment of chronic pain.

PM20D1: The Enigma of Carboxypeptidase PM20D1

Carboxypeptidase PM20D1 is an enzyme involved in the regulation of protein synthesis and degradation. This enzyme catalyzes the conversion of carboxy-amino acids to carboxy-peptides, thereby providing a critical link in the regulation of protein structure and function. PM20D1 is a single-chain protein with 20 distinct amino acid residues. It has a unique catalytic mechanism, where it uses a specific substrate-induced conformational change to activate its catalytic activity. This conformational change allows PM20D1 to form a stable transition state, which is critical for efficient protein synthesis and degradation.

PM20D1's functions extend beyond its role in protein regulation. It has been shown to play a significant role in the regulation of cellular processes such as cell adhesion, migration, and invasion. PM20D1 has also been implicated in the regulation of inflammation and pain signaling. These functions make PM20D1 an attractive target for the development of new drugs with novel therapeutic effects.

Drug Development Strategies for PM20D1

1. Blockade of PM20D1: One approach to drug development against PM20D1 is to block its catalytic activity by binding to the active site. This can lead to a decrease in protein synthesis and potentially lead to therapeutic effects. Small molecules such as inhibitors of PM20D1's active site, or antibodies targeting PM20D1's active site have been shown to be effective in animal models of chronic pain.
2. modulation of PM20D1 expression: Another approach to drug development against PM20D1 is to modulate its expression levels. This can be achieved by small molecules, sirens, or RNA interference. Modulation of PM20D1 expression levels can lead to changes in cellular processes that are relevant to chronic pain.
3. Interaction with PM20D1: Another approach to drug development against PM20D1 is to target its interactions with other proteins. PM20D1 has been shown to interact with several proteins, including heat shock protein (HSP) 70, which plays a critical role in the regulation of protein synthesis and degradation. Targeting these interactions can lead to therapeutic effects.

Conclusion

PM20D1 is a unique carboxypeptidase enzyme with functions in protein regulation and other cellular processes. Its role in the regulation of chronic pain makes it an attractive target for drug development. The development of new therapeutic approaches for PM20D1-positive chronic pain will require a combination of structural, biochemical, and clinical studies to fully understand its potential as a drug target.

Protein Name: Peptidase M20 Domain Containing 1

Functions: Secreted enzyme that regulates the endogenous N-fatty acyl amino acid (NAAs) tissue and circulating levels by functioning as a bidirectional NAA synthase/hydrolase (PubMed:27374330). It condenses free fatty acids and free amino acids to generate NAAs and bidirectionally catalyzes the reverse hydrolysis reaction (PubMed:27374330). Some of these NAAs stimulate oxidative metabolism via mitochondrial uncoupling, increasing energy expenditure in a UPC1-independent manner. Thereby, this secreted protein may indirectly regulate whole body energy expenditure. PM20D1 circulates in tight association with both low- and high-density (LDL and HDL,respectively) lipoprotein particles (By similarity)

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