Heat Shock Protein 1A: A Potential Drug Target (G3303)

Target Name: HSPA1A

NCBI ID: G3303

HSPA1A

Heat Shock Protein 1A: A Potential Drug Target

Heat shock protein 1A (HSPA1A) is a protein that is expressed in a variety of cell types, including neurons, muscle cells, and red blood cells. It is also a key regulator of the heat shock response, which is a critical stress response that helps the cell adapt to and recover from temperature changes.

HSPA1A has been identified as a potential drug target and has been shown to play a role in a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

One of the key functions of HSPA1A is its ability to regulate the production of reactive oxygen species (ROS), which are highly reactive molecules that can cause damage to cells if not properly controlled. During the heat shock response, HSPA1A helps to reduce the production of ROS by interacting with antioxidants and by directly modulating the activity of genes involved in ROS production.

This ability of HSPA1A to regulate ROS production makes it an attractive target for researchers interested in treating diseases that are characterized by oxidative stress. One of the leading theories of aging is that the accumulation of ROS in cells contributes to the aging process, and HSPA1A may be a key regulator of this process.

HSPA1A has also been shown to play a role in a variety of neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and Huntington's disease. These conditions are characterized by the progressive loss of brain cells and the development of neurofibrillary tangles, which are thought to be caused by the buildup of ROS in the brain.

In addition to its role in neurodegenerative diseases, HSPA1A has also been shown to be involved in cancer. Many studies have suggested that HSPA1A may be a promising biomarker for the early detection of cancer, as its expression has been observed in a variety of cancer types.

HSPA1A is also expressed in red blood cells, which play a critical role in transporting oxygen throughout the body. The heat shock response is critical for the maintenance of red blood cell function, and HSPA1A may be involved in regulating the production of new red blood cells in response to changes in oxygen demand.

In conclusion, HSPA1A is a protein that has important functions in a variety of cell types, including neurons, muscle cells, and red blood cells. Its ability to regulate the production of ROS and its involvement in the heat shock response make it an attractive target for researchers interested in treating diseases characterized by oxidative stress. In addition to its role in neurodegenerative diseases and cancer, HSPA1A may also be a promising biomarker for the early detection of these conditions. Further research is needed to fully understand the functions of HSPA1A and its potential as a drug target.

Protein Name: Heat Shock Protein Family A (Hsp70) Member 1A

Functions: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24012426, PubMed:26865365, PubMed:24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). Involved in the clearance of misfolded PRDM1/Blimp-1 proteins. Sequesters them in the cytoplasm and promotes their association with SYNV1/HRD1, leading to proteasomal degradation (PubMed:28842558)

The "HSPA1A Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about HSPA1A comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   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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