PPIAP19: A Potential Drug Target and Biomarker for Peptidylprolyl Isomerase A (Cyclophilin A)

Target Name: PPIAP19

NCBI ID: G390006

PPIAP19

Other Name(s): Peptidylprolyl isomerase A (cyclophilin A) pseudogene 19 | peptidylprolyl isomerase A pseudogene 19 | bA108K1.2

PPIAP19: A Potential Drug Target and Biomarker for Peptidylprolyl Isomerase A (Cyclophilin A)

Peptidylprolyl isomerase A (Cyclophilin A) is a key enzyme in the regulation of protein synthesis and degradation, which is essential for various cellular processes, including cell growth, apoptosis, and inflammation. PPIAP19, also known as PPIAP19 gene or PPIAP19 protein, is a pseudogene that encodes for a protein involved in the regulation of protein synthesis and degradation. The identification and characterization of PPIAP19 as a potential drug target and biomarker have significant implications for the development of new therapeutics for various diseases.

Molecular Background

PPIAP19 is a member of the PPIAP family, which includes several structurally similar proteins involved in protein synthesis and degradation. These proteins belong to the P-type ATPase subfamily and share a conserved catalytic core, which consists of a catalytic domain and a nucleotide-binding domain (NBD). PPIAP19 is characterized by a unique N-terminus, which includes a 24 amino acid residue known as PPIAP19- specific domain (PSD). The PSD is responsible for the N-terminal signaling of the protein and plays a crucial role in its function.

Expression and Localization

PPIAP19 is expressed in various tissues and cells, including the liver, muscle, heart, kidney, and brain. It is primarily localized to the cytoplasm and is present in a cytosol-associated protein (CAP) structure. The level of PPIAP19 expression varies depending on the cell type and the specific context. For example, high levels of PPIAP19 have been observed in cancer cells, which may contribute to their enhanced protein synthesis and metastatic potential.

Function and regulation

PPIAP19 is involved in the regulation of protein synthesis and degradation by activating and inhibiting the activity of several factors. Firstly, it activates the activity of cyclophilins, which are negative regulators of protein synthesis and degradation. Cyclophilins inhibit the activity of PPIAP19 by a process called phosphorylation, which leads to the dissociation of the protein from its nucleotide-binding domain and subsequent release into the cytoplasm.

Secondly, PPIAP19 inhibits the activity of several enzymes involved in protein synthesis and degradation, including the translation factors that initiate the process. This inhibition is critical for maintaining the cytoplasmic environment conducive to the translocation of new proteins into the cytoplasm, which is necessary for protein synthesis and degradation.

Discovery and Potential Therapeutic Applications

The identification of PPIAP19 as a potential drug target and biomarker has significant implications for the development of new therapeutics for various diseases. The potential therapeutic applications of PPIAP19 are summarized in Table 1.

Table 1: Potential Therapeutic Applications of PPIAP19

In summary, PPIAP19 is a pseudogene that encodes for a protein involved in the regulation of protein synthesis and degradation. Its unique N-terminus and involvement in the regulation of cyclophilins make it an attractive target for new therapeutics for various diseases. Further research is necessary to fully understand its function and develop effective therapies based on its potential as a drug target.

Protein Name: Peptidylprolyl Isomerase A Pseudogene 19

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•   general information;
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•   the target screening and validation;
•   expression level;
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•   related combination drugs;
•   pharmacochemistry experiments;
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•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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