VAMP8: A Potential Drug Target and Biomarker (G8673)

Target Name: VAMP8

NCBI ID: G8673

VAMP8: A Potential Drug Target and Biomarker

Vesicle-associated membrane protein 8 (VAMP8) is a protein that is expressed in various cell types, including neurons, endothelial cells, and epithelial cells. It is a member of the family of vesicle-associated membrane proteins (VAMMs), which are involved in the regulation of intracellular signaling pathways. VAMP8 has been shown to play a role in several cellular processes, including cell signaling, migration, and invasion. As a result, VAMP8 has potential as a drug target or biomarker.

The discovery of VAMP8

VAMP8 was first identified in the late 1990s as a gene that was expressed in the brain and was shown to be involved in the development and maintenance of the blood-brain barrier. Subsequent studies have shown that VAMP8 is involved in several cellular processes, including the regulation of neurotransmitter release, synaptic plasticity, and cell signaling.

VAMP8 functions as a protein that can interact with various intracellular signaling pathways. It has been shown to interact with several protein partners, including the neurotransmitter acetylcholine, which is involved in memory and cognitive processes. Additionally, VAMP8 has been shown to interact with the protein PDZP2, which is involved in the regulation of synaptic plasticity.

VAMP8 as a drug target

VAMP8 has been shown to have several potential as a drug target. One of the main targets of VAMP8 is the neurotransmitter acetylcholine, which is involved in memory and cognitive processes. Studies have shown that inhibiting VAMP8 can increase the levels of acetylcholine in the brain, which can improve memory and cognitive function.

Another potential target of VAMP8 is the protein PDZP2, which is involved in the regulation of synaptic plasticity. Studies have shown that VAMP8 can interact with PDZP2 and that inhibiting VAMP8 can decrease the levels of PDZP2 in the brain, which can improve synaptic plasticity.

VAMP8 as a biomarker

VAMP8 has also been shown to be involved in several biomarkers that are relevant to human disease, including cancer. Studies have shown that VAMP8 is involved in the regulation of cell proliferation and that it can be used as a biomarker for several types of cancer, including breast, ovarian, and prostate cancer.

In addition to its role in cancer, VAMP8 has also been shown to be involved in the regulation of other types of inflammation, such as neuroinflammation. Studies have shown that VAMP8 is involved in the production of pro-inflammatory cytokines and that it can contribute to neuroinflammation.

Conclusion

VAMP8 is a protein that has been shown to play a role in several cellular processes, including cell signaling, migration, and invasion. As a result, VAMP8 has potential as a drug target or biomarker. The discovery of VAMP8 has led to a better understanding of the role of vesicle-associated membrane proteins in cellular processes and has implications for the development of new treatments for a variety of diseases. Further research is needed to fully understand the role of VAMP8 in cellular processes and to develop effective treatments based on its properties .

Protein Name: Vesicle Associated Membrane Protein 8

Functions: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane via its interaction with the STX17-SNAP29 binary t-SNARE complex (PubMed:23217709, PubMed:25686604). Also required for dense-granule secretion in platelets (PubMed:12130530). Also plays a role in regulated enzyme secretion in pancreatic acinar cells (By similarity). Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells (By similarity). Involved in the homotypic fusion of early and late endosomes (By similarity). Participates also in the activation of type I interferon antiviral response through a TRIM6-dependent mechanism (PubMed:31694946)

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