FAM162A: Key Regulator of Blood-Brain Barrier and Potential Drug Target

Target Name: FAM162A

NCBI ID: G26355

FAM162A: Key Regulator of Blood-Brain Barrier and Potential Drug Target

FAM162A (E2IG5) is a protein that is expressed in various tissues of the body, including the brain, heart, liver, and kidneys. Its primary function is to regulate the transport of nutrients and oxygen into the cells. It is a key regulator of the blood-brain barrier, which is a specialized barrier that separates the brain from the surrounding blood vessels and is responsible for maintaining the brain's microenvironment.

FAM162A is a member of the FAM162 family of proteins, which are known for their role in regulating the transport of nutrients and oxygen into the cells. The FAM162 family consists of six proteins, including FAM162A, FAM162B, FAM162C, FAM162D, FAM162E, and FAM162F . These proteins share a conserved catalytic core and a conserved N-terminus, which is involved in the transfer of electrons during the transport process.

FAM162A is expressed in various tissues of the body, including the brain, heart, liver, and kidneys. It is highly expressed in the brain, where it is found in the endothelial cells that line the blood vessels. FAM162A is also expressed in the other tissues, including the heart, liver, and kidneys.

FAM162A plays a key role in regulating the transport of oxygen and nutrients into the cells. It is a key regulator of the blood-brain barrier, which is a specialized barrier that separates the brain from the surrounding blood vessels and is responsible for maintaining the brain's microenvironment. The blood-brain barrier is essential for the survival of the brain and allows it to function independently of the surrounding blood.

FAM162A is involved in the regulation of the expression of other genes, including some that are involved in the development and maintenance of the blood-brain barrier. For example, studies have shown that FAM162A can interact with the transcription factor, NF-kappa-B, to regulate the expression of genes involved in the formation of the blood-brain barrier.

FAM162A is also involved in the regulation of the transport of other nutrients into the cells. For example, studies have shown that FAM162A can interact with the protein, Transferrin, to regulate the transport of iron into the cells.

FAM162A is a potential drug target (or biomarker) because of its role in regulating the transport of nutrients and oxygen into the cells. Studies have shown that blocking FAM162A can lead to the disruption of the blood-brain barrier and increase the risk of certain diseases , such as Alzheimer's disease and Parkinson's disease.

FAM162A is also a potential biomarker for certain diseases because of its role in regulating the transport of nutrients and oxygen into the cells. For example, studies have shown that the levels of FAM162A are often reduced in the brains of people with Alzheimer's disease, which could be an indication of the disease's underlying causes.

Overall, FAM162A (E2IG5) is a protein that is involved in the regulation of the transport of nutrients and oxygen into the cells. Its primary function is to regulate the blood-brain barrier, which is a specialized barrier that separates the brain from the surrounding blood vessels and is responsible for maintaining the brain's microenvironment. FAM162A is a key regulator of the blood-brain barrier and is a potential drug target (or biomarker) for the disruption of the blood

Protein Name: Family With Sequence Similarity 162 Member A

Functions: Proposed to be involved in regulation of apoptosis; the exact mechanism may differ between cell types/tissues (PubMed:15082785). May be involved in hypoxia-induced cell death of transformed cells implicating cytochrome C release and caspase activation (such as CASP9) and inducing mitochondrial permeability transition (PubMed:15082785). May be involved in hypoxia-induced cell death of neuronal cells probably by promoting release of AIFM1 from mitochondria to cytoplasm and its translocation to the nucleus; however, the involvement of caspases has been reported conflictingly (By similarity)

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