VCP: A Promising Drug Target for Diabetes and Heart Disease (G7415)

Target Name: VCP

NCBI ID: G7415

Content of Review Report on VCP Target / Biomarker

VCP

VCP: A Promising Drug Target for Diabetes and Heart Disease

VCP (Vinogradolipen) is a lipid-lowering drug that is currently being investigated as a potential treatment for various diseases, including diabetes and heart disease. It works by inhibiting the production of low-density lipoprotein (LDL) cholesterol, which is a major risk factor for the development of heart disease and stroke.

Research on VCP has been ongoing for several years, and there is some evidence to suggest that it may have potential as a drug target for several diseases. In particular, VCP has been shown to be effective in treating diabetes, which is a disease that affects millions of people around the world and is a major contributor to the development of cardiovascular disease.

One of the potential benefits of VCP as a drug target is its ability to improve insulin sensitivity. Insulin resistance is a condition in which the body's cells become less responsive to insulin, making it difficult for the body to use the hormone to lower blood sugar levels. This can lead to high blood sugar levels, which can contribute to the development of type 2 diabetes.

VCP has been shown to improve insulin sensitivity in several animal models of type 2 diabetes. In one study, researchers found that VCP treatment significantly improved insulin sensitivity in obese rats. Another study found that VCP treatment significantly improved insulin sensitivity in diabetic rats.

In addition to its potential benefits for diabetes, VCP has also been shown to have potential as a drug target for other diseases. For example, VCP has been shown to have anti-inflammatory properties, which can help to reduce the risk of cardiovascular disease. In addition, VCP has been shown to have neuroprotective properties, which can help to reduce the risk of neurodegenerative diseases.

VCP has also been shown to have potential as a drug target for cancer. For example, VCP has been shown to have anti-tumor properties in several types of cancer, including breast, lung, and ovarian cancer. In addition, VCP has been shown to have the potential to enhance the effectiveness of some chemotherapy drugs.

Despite the potential benefits of VCP as a drug target, there are also some concerns about its safety and effectiveness. For example, some studies have suggested that VCP may cause side effects in certain individuals, such as nausea and vomiting. In addition, there is some evidence to suggest that VCP may cause an increase in blood pressure, which can be a potential risk factor for cardiovascular disease.

Overall, VCP is a promising drug target for the treatment of various diseases, including diabetes and heart disease. Further research is needed to fully understand its potential benefits and to determine its safety and effectiveness.

Protein Name: Valosin Containing Protein

Functions: Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation (PubMed:26565908). Plays a role in the regulation of stress granules (SGs) clearance process upon arsenite-induced response (PubMed:29804830). Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites (PubMed:22020440, PubMed:22120668). Recruited to stalled replication forks by SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage (PubMed:23042607, PubMed:23042605). Together with SPRTN metalloprotease, involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis (PubMed:32152270). Involved in interstrand cross-link repair in response to replication stress by mediating unloading of the ubiquitinated CMG helicase complex (By similarity). Mediates extraction of PARP1 trapped to chromatin: recognizes and binds ubiquitinated PARP1 and promotes its removal (PubMed:35013556). Required for cytoplasmic retrotranslocation of stressed/damaged mitochondrial outer-membrane proteins and their subsequent proteasomal degradation (PubMed:16186510, PubMed:21118995). Essential for the maturation of ubiquitin-containing autophagosomes and the clearance of ubiquitinated protein by autophagy (PubMed:20104022, PubMed:27753622). Acts as a negative regulator of type I interferon production by interacting with RIGI: interaction takes place when RIGI is ubiquitinated via 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit RNF125 and promote ubiquitination and degradation of RIGI (PubMed:26471729). May play a role in the ubiquitin-dependent sorting of membrane proteins to lysosomes where they undergo degradation (PubMed:21822278). May more particularly play a role in caveolins sorting in cells (PubMed:21822278, PubMed:23335559). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333)

The "VCP 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 VCP 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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