PPIAP22: A Potential Drug Target and Biomarker for Peptidyl Prolyl Isomerase A

Target Name: PPIAP22

NCBI ID: G653214

PPIAP22

Other Name(s): peptidylprolyl isomerase A pseudogene 22 | PPIAL3 | Peptidylprolyl isomerase A (cyclophilin A) pseudogene 22 | PPIA3L

PPIAP22: A Potential Drug Target and Biomarker for Peptidyl Prolyl Isomerase A

Peptidyl prolyl isomerase (PPI) is an enzyme involved in the regulation of protein levels and post-translational modifications, which plays a crucial role in various cellular processes, including cell growth, apoptosis, and inflammation. PPI has four isoforms, A, B, C, and D, which differ in their catalytic efficiency and substrate specificity. PPIAP22 is a pseudogene that encodes the protein sequence responsible for the function of PPI. In this article, we will discuss the potential implications of PPIAP22 as a drug target and biomarker.

Expression and Functions of PPI

PPI is a member of the superfamily of serine proteases and is involved in the regulation of protein levels and post-translational modifications. PPI functions as a critical enzyme in the breakdown of peptidyl prolyl is backups (PPI-backups), which are incorrectly translated or mutated proteins that accumulate in the cell and contribute to various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. PPI is involved in the recognition and cleavage of PPI-backups, thereby promoting their degradation and removing them from the cell.

PPIAP22: A Pseudogene Encoding the Functional Subunit of PPI

PPIAP22 is a pseudogene that encodes the functional subunit of PPI, which is responsible for the catalytic activity of the enzyme. The PPIAP22 gene was identified through DNA sequencing and has been shown to encode a protein with a calculated molecular mass of 11.4 kDa. PPIAP22 is a single gene that encodes the full-length protein, and its expression is highly conserved across various species, including humans.

Functional Characterization of PPIAP22

Functional characterization of PPIAP22 has been primarily conducted using biochemical and cellular assays. Initial studies demonstrated that PPIAP22 is a protein that is expressed and purified from various cell types, including HEK293 cells, human embryonic kidney (HES) cells, and human liver cells. Additionally, the protein has been shown to have catalytic activity, as it can catalyze the hydrolysis of the protein ppi and generate a peptidyl-prolyl isomerase activity.

Expression and Localization of PPIAP22

Expression of PPIAP22 has been shown to be highly dependent on various factors, including cell type, growth conditions, and treatments. For example, it has been shown that PPIAP22 is highly expressed in human cancer cell lines, such as the HeLa and MDA-MB-4 cell lines, compared to normal human tissues, such as the skin and heart. Additionally, the expression of PPIAP22 has been shown to be regulated by various signaling pathways, including TGF-β, NF-kappa-B, and PI3K/AKT signaling pathways.

Bioinformatics Analysis of PPIAP22

To understand the functional implications of PPIAP22, bioinformatics analysis was conducted to predict its potential interactions and modulators. The results of these analyses have identified several potential interactors and regulators, including tyrosine kinase (TK), tyrosine phosphatase (TTP), and dephosphorylase (DPL). These interactions may contribute to the regulation of PPIAP22 function and its role in various cellular processes.

Drug Targeting and Biomarker Potential

The potential drug targeting of PPIAP22 is based on its involvement in the regulation of protein levels and post

Protein Name: Peptidylprolyl Isomerase A Pseudogene 22

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