ADPRS as A Potential Drug Target and Biomarker for Neurodegenerative Diseases

Target Name: ADPRS

NCBI ID: G54936

ADPRS as A Potential Drug Target and Biomarker for Neurodegenerative Diseases

ADPRS (ADP-ribosylserine hydrolase), also known as HSP70B3, is a protein that is expressed in various tissues and cells throughout the body. It is a member of the HSP70 family of proteins, which are known for their role in various cellular processes such as stress response, DNA repair, and signaling pathways. In recent years, researchers have become interested in studying the potential drug targets of ADPRS, particularly in the context of neurodegenerative diseases.

The neurodegenerative diseases that are currently affecting millions of people around the world, such as Alzheimer's disease, Parkinson's disease, and Huntington's disease, are characterized by the progressive loss of brain cells and the damage to neural circuits that support brain function. These diseases are typically treated with a combination of drugs that aim to slow down or halt the progression of the disease. However, these drugs often have limited efficacy and can cause various side effects. Therefore, there is a need for new drug targets and biomarkers that can provide more targeted and effective treatments.

ADPRS is a potential drug target and biomarker due to its unique structure and biology. The HSP70 family of proteins plays a central role in the regulation of protein homeostasis, which is the balance between the levels of protein in the cytoplasm and the levels in the nucleus. ADPRS is a member of the HSP70 family that is involved in the regulation of protein homeostasis in the cytoplasm.

Studies have shown that ADPRS is involved in various cellular processes that are important for brain function. For example, ADPRS has been shown to be involved in the regulation of the levels of protein involved in the neurotransmitter systems, such as dopamine and serotonin. It has also been shown to play a role in the regulation of the levels of protein involved in the cytoskeleton and cell signaling pathways.

In addition to its role in cellular processes, ADPRS has also been shown to be involved in the regulation of cellular stress responses. During stress, cells are able to respond by increasing their levels of various proteins, including those involved in signaling pathways. This increase in protein levels is important for the cell to respond to stress and maintain homeostasis. However, if the stress response is not properly regulated, it can lead to a variety of cellular and organizational changes that can contribute to the development of stress-related diseases.

One of the key challenges in studying ADPRS is its complex biology. The HSP70 family of proteins is known for its diverse range of functions, and it is not yet fully understood how these functions are regulated. However, researchers have made some progress in understanding the regulation of ADPRS.

One of the key regulators of ADPRS is its expression level. The levels of ADPRS are typically increased in response to various stressors, such as stress, starvation, or exercise. This increase in ADPRS levels is important for the cell to respond to stress and maintain homeostasis. However, if the stress response is not properly regulated, it can lead to a variety of cellular and organizational changes that can contribute to the development of stress-related diseases.

Another important factor that affects the expression of ADPRS is its localization. ADPRS is typically localized to the cytoplasm, where it is involved in the regulation of protein homeostasis. However, its localization can also be influenced by various factors, such as the presence of other proteins and the cellular environment. Understanding the localization of ADPRS is important for the development of new drug targets and biomarkers.

In conclusion, ADPRS is a protein that is involved in various cellular processes that are important for brain function. Its diverse biology and complex regulation make it an attractive target for new drug

Protein Name: ADP-ribosylserine Hydrolase

Functions: ADP-ribosylhydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine and threonine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose (PubMed:21498885, PubMed:30830864, PubMed:33769608, PubMed:30045870, PubMed:29907568, PubMed:34321462, PubMed:30401461, PubMed:33186521, PubMed:34019811, PubMed:33894202, PubMed:34479984, PubMed:34625544). Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response (PubMed:28650317, PubMed:29234005, PubMed:33186521, PubMed:34625544, PubMed:30045870, PubMed:34019811). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:29480802, PubMed:33186521, PubMed:34625544). Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (PubMed:16278211, PubMed:33769608). Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos (PubMed:16278211). Also hydrolyzes free poly(ADP-ribose) in mitochondria (PubMed:22433848). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (PubMed:17075046, PubMed:21498885). Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers (PubMed:21498885)

More Common Targets