Unlocking the Potential of ATPase6V1E1: A drug Target and Biomarker for Intracellular H(+) Transport
Unlocking the Potential of ATPase6V1E1: A drug Target and Biomarker for Intracellular H(+) Transport
Introduction
ATP (adenylyl cyclic nucleotide) is the primary energy source for all cellular processes, and its production and breakdown are tightly regulated. One of the critical ATP-producing mechanisms is the H(+)-ATPase, a transmembrane protein that catalyzes the conversion of ATP to ADP and Pi, while releasing H+ ions into the cytosol. The H(+)-ATPase is a two-sector ATPase, which means that it consists of two distinct subunits connected by a cytoplasmic region. One of the subunits, ATP6V1E1, has been identified as a potential drug target and biomarker for intracellular H(+) transport.
The H(+)-ATPase is an essential enzyme for maintaining cellular homeostasis and is involved in various cellular processes, including intracellular signaling, ion homeostasis, and cell survival. The H(+)-ATPase plays a crucial role in regulating the cytosolic H+ ion concentration, which is critical for maintaining the proper pH balance and supporting the survival of many cellular processes.
ATP6V1E1: A Candidate Drug Target
The identification of ATP6V1E1 as a potential drug target and biomarker for intracellular H(+) transport is based on several factors. Firstly, ATP6V1E1 is a well-established H(+)-ATPase with a known subunit structure. The 31kDa subunit has been shown to catalyze the H(+)-ATPase reaction with high efficiency and is the most abundant subunit in human cells. Secondly, several studies have demonstrated that inhibition of the H(+)-ATPase led to increased intracellular H(+) ion concentration, suggesting that it plays a critical role in maintaining the cytosolic H(+) ion balance.
Furthermore, several drugs have been shown to inhibit the H(+)-ATPase and increase intracellular H(+) ion concentration. These drugs have been tested in various cellular models and have been shown to have potential therapeutic benefits, including cancer treatment and neurodegenerative diseases. Therefore, ATP6V1E1 is a promising target for the development of new drugs with therapeutic applications.
Biomarker Potential
The H(+)-ATPase is involved in various cellular processes, including intracellular signaling, ion homeostasis, and cell survival. Therefore, it is important to study its function and determine if it can be used as a biomarker for various diseases. Several studies have shown that the H(+)-ATPase is involved in the regulation of various cellular processes, including cell adhesion, migration, and survival.
One of the most promising applications of the H(+)-ATPase as a biomarker is its potential to diagnose and monitor various diseases, including cancer. The H(+)-ATPase is involved in the regulation of cell adhesion, which is critical for the development and progression of cancer. Therefore, inhibition of the H(+)-ATPase has been shown to be effective in cancer treatment. Additionally, the H(+)-ATPase is involved in the regulation of ion homeostasis, which is critical for maintaining the proper pH balance in cancer cells. Therefore, inhibition of the H(+)-ATPase has been shown to be effective in neutralizing the effects of cancer cells on the body's pH balance.
Conclusion
In conclusion, ATP6V1E1 is a well-established H(+)-ATPase with a known subunit structure that has been shown to catalyze the H(+)-ATPase reaction with high efficiency. Several studies have demonstrated that inhibition of the H(+) -ATPase led to increased intracellular H(+) ion concentration, suggesting that it plays a critical role in maintaining the cytosolic H(+) ion balance. Furthermore, several studies have shown that the H(+)-ATPase is involved in the regulation of various cellular processes, including cell adhesion, migration, and survival. Therefore, ATP6V1E1 is a promising target for
Protein Name: ATPase H+ Transporting V1 Subunit E1
Functions: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:33065002, PubMed:32001091). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (PubMed:32001091)
More Common Targets
ATP6V1E2 | ATP6V1F | ATP6V1FNB | ATP6V1G1 | ATP6V1G1P1 | ATP6V1G2 | ATP6V1G2-DDX39B | ATP6V1G3 | ATP6V1H | ATP7A | ATP7B | ATP8 | ATP8A1 | ATP8A2 | ATP8B1 | ATP8B1-AS1 | ATP8B2 | ATP8B3 | ATP8B4 | ATP8B5P | ATP9A | ATP9B | ATPAF1 | ATPAF2 | ATPase | ATPSCKMT | ATR | ATRAID | Atrial natriuretic peptide (ANP) receptor | ATRIP | ATRN | ATRNL1 | ATRX | ATXN1 | ATXN10 | ATXN1L | ATXN2 | ATXN2L | ATXN3 | ATXN3L | ATXN7 | ATXN7L1 | ATXN7L2 | ATXN7L3 | ATXN7L3B | ATXN8OS | Augmin | AUH | AUNIP | AUP1 | AURKA | AURKAIP1 | AURKAP1 | AURKB | AURKC | Aurora Kinase | AUTS2 | AVEN | AVIL | AVL9 | AVP | AVPI1 | AVPR1A | AVPR1B | AVPR2 | AWAT1 | AWAT2 | AXDND1 | AXIN1 | AXIN2 | AXL | Axonemal dynein complex | AZGP1 | AZGP1P1 | AZGP1P2 | AZI2 | AZIN1 | AZIN2 | AZU1 | B-cell Antigen Receptor Complex | B2M | B3GALNT1 | B3GALNT2 | B3GALT1 | B3GALT1-AS1 | B3GALT2 | B3GALT4 | B3GALT5 | B3GALT5-AS1 | B3GALT6 | B3GALT9 | B3GAT1 | B3GAT1-DT | B3GAT2 | B3GAT3 | B3GLCT | B3GNT2 | B3GNT3 | B3GNT4 | B3GNT5