PPIL4: A Potential Drug Target and Biomarker for Promyelocytic Leukemia

Target Name: PPIL4

NCBI ID: G85313

PPIL4: A Potential Drug Target and Biomarker for Promyelocytic Leukemia

Promyelocytic leukemia (PML) is a type of acute leukemia that affects the bone marrow, where white blood cells called leukemia cells (blasts) continuously multiply and produce an abnormal amount of white blood cells. This leads to overproduction of white blood cells, which may cause the symptoms of PML, such as fever, fatigue, bone pain, anemia, and an increased risk of infections. Treatment options for PML are limited, and the prognosis is often poor. Therefore, there is a need for new treatments that can effectively target this disease and improve outcomes.

PPIase, or Promyelocytic leukemia-associated proteinase, is a protein that is expressed in the blasts of PML patients. It is a key enzyme in the process of leukemia development and has been identified as a potential drug target for PML. In this article, we will discuss the biology of PPIase, its potential as a drug target, and its potential as a biomarker for the diagnosis and treatment of PML.

Biochemistry and Expression of PPIase

PPIase is a 21-kDa protein that is expressed in the blasts of PML patients. It is produced by the Philadelphia chromosome and is located on the chromosome 9. PPIase is a src/src-like protein that contains a src-like domain and a catalytic active site. The src-like domain is responsible for the protein's src-like structure and functions as a binding site for other proteins. The catalytic active site is responsible for the protein's catalytic activity and is responsible for the catalytic conversion of PPIase's substrate, such as an amino acid residue, into a carboxylic acid residue.

Function of PPIase

PPIase is involved in the process of leukemia development by promoting the production and proliferation of leukemia cells. It is a key enzyme in the process of promyelocytic leukemia (PML), which is the most common type of acute leukemia. PPIase promotes the transformation of normal cells into leukemia cells by inhibiting the differentiation of these cells and causing them to multiply uncontrollably.

PPIase has been shown to play a role in the development and progression of PML by promoting the production of leukemia cells in the bone marrow. It has been shown that higher levels of PPIase are associated with a more aggressive form of PML. Additionally, higher levels of PPIase have been shown to be associated with a decreased response to chemotherapy in PML patients.

Drug Targeting for PPIase

Due to its involvement in the process of leukemia development and its association with PML, PPIase has been identified as a potential drug target for PML. Several studies have shown that blocking PPIase activity can lead to a decrease in the production of leukemia cells and improve the response to chemotherapy in PML patients.

One of the most promising strategies for targeting PPIase is the use of inhibitors that specifically target the protein's catalytic active site. These inhibitors have been shown to be effective in preclinical studies in blocking the growth and proliferation of PML blasts. One such inhibitor is MK-8628, which is a small molecule inhibitor of PPIase that is currently in clinical trials for the treatment of PML.

Another potential strategy for targeting PPIase is the use of antibodies that specifically target the protein. These antibodies have been shown to be effective in blocking the growth and proliferation of PML blasts in cell

Protein Name: Peptidylprolyl Isomerase Like 4

Functions: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity)

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