SLC1A5: A Potential Drug Target and Biomarker for Neutral Amino Acid Transporter B(0) (ISO Form 2)

Target Name: SLC1A5

NCBI ID: G6510

SLC1A5

SLC1A5: A Potential Drug Target and Biomarker for Neutral Amino Acid Transporter B(0) (ISO Form 2)

Sodium-dependent chloride transport ATPase (SLC1A5) is a transmembrane protein that plays a crucial role in regulating essential amino acids (EAs) uptake and excretion in the body. It is a member of the SLC gene family, which encodes for a family of Na+-dependent chloride transport proteins. SLC1A5 is expressed in most tissues and cells and is involved in maintaining the homeostasis of intracellular EAs.

SLC1A5 functions as a transporter for the amino acid neutral amino acid transporter B(0) (ISO Form 2). B(0) is a critical regulator of intracellular amino acid levels and is involved in the maintenance of cellular homeostasis. SLC1A5-mediated transport of B(0) is a critical mechanism for maintaining the levels of neutral amino acids (NAs) in the cytosol and for preventing the accumulation of adverse side effects associated with high levels of these acids.

SLC1A5 is a potential drug target and biomarker due to its central role in the regulation of NA transport. Activation of SLC1A5 has been shown to increase B(0) levels in the cytosol, leading to increased NA uptake and retention. This increase in NA uptake can lead to increased cellular concentrations of these acids, which can cause various cellular stress responses, including inflammation, oxidative stress, and neurodegeneration.

SLC1A5 is also a potential biomarker for monitoring the efficacy of NA transport inhibitors. Since SLC1A5 is involved in the regulation of NA transport, inhibitors of SLC1A5 function can be used to assess the ability of these inhibitors to disrupt NA transport and improve the efficacy of other NA transport inhibitors.

SLC1A5 Expression and Localization

SLC1A5 is highly expressed in most tissues and cells and is primarily located in the cytosol. It is a monomeric protein that consists of an N-terminal transmembrane domain and a C-terminal cytoplasmic domain. The N-terminal transmembrane domain contains a putative ATP-binding site and is involved in the regulation of Na+ and Cl- transport. The C-terminal cytoplasmic domain contains a putative nucleotide-binding site (NBS) and is involved in the regulation of protein stability and localization.

SLC1A5 is predominantly expressed in the brain, heart, and muscle, where it is involved in the regulation of NA transport and the maintenance of cellular homeostasis. It is also expressed in other tissues, including the liver, where it is involved in the regulation of NA transport and the detoxification of NA-loaded drugs.

SLC1A5 Interaction with Other Proteins

SLC1A5 interacts with several other proteins, including Na+/K+-ATPase (NKATPase), Na+/H+ exchange pump (NaHX), and Na+/IP3-dependent kinase (NaIP3-K). SLC1A5 is also involved in the regulation of the activity of these proteins and is a negative regulator for NaHX and NaIP3-K.

SLC1A5 also interacts with the protein PyH, which is involved in the detoxification of NA-loaded drugs. SLC1A5 inhibits the activity of PyH, leading to increased NA uptake and retention.

Drug Treatment and SLC1A5 Expression

SLC1A5 can be inhibited by various drug treatments, including small molecules, peptides, and antibodies. Inhibition of SLC1A5 function has been shown to improve the efficacy of NA transport inhibitors, such as aminoglycoside antibiotics, and to protect against neurotoxicity associated with high levels of NA.

Conclusion

SLC1A5 is a transmembrane protein that is involved in the regulation of essential amino

Protein Name: Solute Carrier Family 1 Member 5

Functions: Sodium-coupled antiporter of neutral amino acids. In a tri-substrate transport cycle, exchanges neutral amino acids between the extracellular and intracellular compartments, coupled to the inward cotransport of at least one sodium ion (PubMed:23756778, PubMed:26492990, PubMed:17094966, PubMed:34741534, PubMed:29872227, PubMed:8702519). The preferred substrate is the essential amino acid L-glutamine, a precursor for biosynthesis of proteins, nucleotides and amine sugars as well as an alternative fuel for mitochondrial oxidative phosphorylation. Exchanges L-glutamine with other neutral amino acids such as L-serine, L-threonine and L-asparagine in a bidirectional way. Provides L-glutamine to proliferating stem and activated cells driving the metabolic switch toward cell differentiation (PubMed:23756778, PubMed:24953180). The transport cycle is usually pH-independent, with the exception of L-glutamate. Transports extracellular L-glutamate coupled to the cotransport of one proton and one sodium ion in exchange for intracellular L-glutamine counter-ion. May provide for L-glutamate uptake in glial cells regulating glutamine/glutamate cycle in the nervous system (PubMed:32733894). Can transport D-amino acids. Mediates D-serine release from the retinal glia potentially affecting NMDA receptor function in retinal neurons (PubMed:17094966). Displays sodium- and amino acid-dependent but uncoupled channel-like anion conductance with a preference SCN(-) >> NO3(-) > I(-) > Cl(-) (By similarity). Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development (PubMed:10708449, PubMed:23492904)

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