VIL1: A Potential Drug Target and Biomarker (G7429)

Target Name: VIL1

NCBI ID: G7429

VIL1: A Potential Drug Target and Biomarker

Villin-1 (VIL1) is a protein that is expressed in various tissues of the human body, including the skin, hair, and nails. It is a member of the insulin-like growth factor receptor (IGFR) family and has been implicated in several cellular processes, including cell signaling, angiogenesis, and tissue repair. In addition, VIL1 has also been shown to play a role in the development and progression of certain diseases, such as cancer. As such, targeting VIL1 has the potential to be a new drug target and biomarker for a variety of therapeutic indications.

Targeting VIL1: Potential Therapeutic Benefits

One of the main potential therapeutic benefits of targeting VIL1 is its potential as a cancer therapeutic. Cancer is a leading cause of death worldwide, and there is a significant need for new, effective treatments to address this devastating disease. VIL1 has been shown to be involved in the development and progression of several types of cancer, including skin cancer, hair loss, and nail fungus. By targeting VIL1, researchers may be able to develop new treatments for these diseases that specifically target this protein and have the potential to be more effective than current treatments.

In addition to its potential as a cancer therapeutic, VIL1 has also been shown to be involved in the development of other diseases. For example, VIL1 has been implicated in the development of certain types of skin disorders, such as acne and psoriasis. It has also been shown to play a role in the development of certain types of hair loss, such as androgen-sensitive alopecia. Additionally, VIL1 has been linked to the development of certain types of nail fungus, such as onychomycosis. By targeting VIL1 in these diseases, researchers may be able to develop new treatments that specifically target this protein and have the potential to be more effective than current treatments.

Measuring VIL1: Potential Biomarkers

Measuring VIL1 is a potential biomarker for several types of diseases, including cancer, skin disorders, and hair loss. One approach to measuring VIL1 is through the use of antibodies that recognize specific regions of the protein. These antibodies can be used to detect VIL1 protein in a variety of tissues, including cells, tissues, and biological samples. By detecting VIL1 protein in these samples, researchers can measure the level of the protein and potentially use this information to understand how VIL1 is involved in the development and progression of certain diseases.

In addition to antibodies, researchers may also use other techniques to measure VIL1, such as mass spectrometry. This technique involves the use of a mass spectrometer, which can identify the specific amino acids that make up VIL1 protein. By analyzing the mass spectrometry data from these samples, researchers can identify the level of VIL1 protein and potentially use this information to understand how this protein is involved in the development and progression of certain diseases.

Conclusion

VIL1 is a protein that is expressed in various tissues of the human body and has been implicated in several cellular processes, including cell signaling and tissue repair. In addition, VIL1 has also been shown to play a role in the development and progression of certain diseases, such as cancer and skin disorders. As such, targeting VIL1 has the potential to be a new drug target and biomarker for a variety of therapeutic indications. Additionally, measuring VIL1 using antibodies and mass spectrometry may be a useful way to assess the level of this protein and potentially use this information to understand how VIL1 is involved in the development and progression of certain diseases.

Protein Name: Villin 1

Functions: Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination

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