Heat Shock Protein HSPA1L: Potential Drug Target and Biomarker

Target Name: HSPA1L

NCBI ID: G3305

Heat Shock Protein HSPA1L: Potential Drug Target and Biomarker

Heat shock protein 1L (HSPA1L), also known as heat shock protein 70 kDa (HSP70), is a protein that is expressed in a variety of cell types and is involved in the regulation of various cellular processes. HSPA1L has been identified as a potential drug target and biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

HSPA1L is a heat shock protein that is expressed in a variety of cell types, including muscle, nerve, heart, and cancer cells. It is characterized by a molecular weight of approximately 18 kDa and a calculated pI of 6.9. HSPA1L is involved in the regulation of various cellular processes, including cell growth, apoptosis, angiogenesis, and inflammation.

One of the key functions of HSPA1L is its role in the regulation of cell growth. HSPA1L has been shown to play a negative role in the regulation of cell growth by suppressing the activities of the oncogenic K-factor kinases, which promote cell growth and contribute to the development of cancer. Additionally, HSPA1L has been shown to play a positive role in the regulation of cell differentiation by promoting the activities of the anti-proliferative microRNA-21 (miRNA-21), which targets and inhibits the expression of pro-proliferative genes.

Another function of HSPA1L is its role in the regulation of apoptosis, which is the process by which cells undergo programmed cell death. HSPA1L has been shown to play a negative role in the regulation of apoptosis by suppressing the activities of the pro-apoptotic protein Bcl-2, which promotes the survival of cells and contributes to the development of neurodegenerative diseases.

HSPA1L is also involved in the regulation of angiogenesis, which is the process by which new blood vessels are formed. HSPA1L has been shown to play a positive role in the regulation of angiogenesis by promoting the activities of the pro-angiogenic protein PDGF-2, which contributes to the development of vascular diseases such as heart failure and cancer.

In addition to its role in cell growth, apoptosis, and angiogenesis, HSPA1L is also involved in the regulation of inflammation. HSPA1L has been shown to play a negative role in the regulation of inflammation by suppressing the activities of the pro-inflammatory protein TNF-alpha, which contributes to the development of inflammatory diseases such as rheumatoid arthritis and cancer.

HSPA1L has also been shown to play a role in the regulation of cellular signaling pathways, including the TGF-beta pathway. HSPA1L has been shown to play a negative role in the regulation of TGF-beta signaling by suppressing the activities of the transcription factor Smad2, which contributes to the development of TGF-beta-related diseases such as fibrosis.

In conclusion, HSPA1L is a protein that is involved in the regulation of various cellular processes and has been identified as a potential drug target and biomarker for various diseases. Further research is needed to fully understand the role of HSPA1L in the regulation of cellular processes and its potential as a drug target.

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

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 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 (PubMed:26865365). Positive regulator of PRKN translocation to damaged mitochondria (PubMed:24270810)

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