S100A9: Potential Drug Target Or Biomarker for Various Diseases

Target Name: S100A9

NCBI ID: G6280

S100A9: Potential Drug Target Or Biomarker for Various Diseases

S100A9 (MRP14) is a protein that is expressed in various tissues throughout the body. It is a member of the S100 family of proteins, which are known for their role in cell signaling and signaling pathways. S100A9 has been identified as a potential drug target or biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

The S100A9 protein is composed of 215 amino acid residues and has a calculated molecular mass of 33.1 kDa. It is expressed in a variety of tissues, including the brain, heart, skeletal muscles, liver, and pancreas. S100A9 is involved in several cellular processes, including cell signaling, cell adhesion, and cytoskeletal organization.

One of the functions of S100A9 is to regulate the activity of other proteins that are involved in cell signaling pathways. It does this by interacting with these proteins and modulating their activity. S100A9 has been shown to play a role in several signaling pathways, including the TGF-β pathway, the Wnt pathway, and the Hedgehog pathway.

In addition to its role in cell signaling, S100A9 is also involved in the regulation of cell adhesion. Adhesion is the process by which cells stick together to form tissues and organs. S100A9 is shown to play a role in the regulation of cell adhesion by interacting with cadherins, which are a family of transmembrane proteins that are involved in cell-cell adhesion.

S100A9 is also involved in the regulation of cytoskeletal organization. Cytoskeletal organization is the process by which cells maintain their shape and structure. S100A9 is shown to play a role in the regulation of cytoskeletal organization by interacting with microtubules, which are the protein structures that make up the cytoskeleton.

S100A9 has also been shown to be involved in several signaling pathways that are involved in cancer progression. For example, S100A9 has been shown to play a role in the regulation of the PI3K/Akt signaling pathway, which is involved in the regulation of cell growth and survival. Additionally, S100A9 has been shown to play a role in the regulation of the T-cell receptor signaling pathway, which is involved in the regulation of immune responses.

S100A9 has also been identified as a potential biomarker for several diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. For example, studies have shown that S100A9 is downregulated in several types of cancer, including breast, ovarian, and colorectal cancer. Additionally, S100A9 has been shown to be involved in the regulation of neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease.

In conclusion, S100A9 is a protein that is involved in several cellular processes that are important for cell signaling and organization. Its role in these processes makes it a potential drug target or biomarker for a variety of diseases. Further research is needed to fully understand the function of S100A9 and its potential as a drug or biomarker.

Protein Name: S100 Calcium Binding Protein A9

Functions: S100A9 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response (PubMed:12626582, PubMed:15331440, PubMed:20103766, PubMed:8423249, PubMed:16258195, PubMed:19122197, PubMed:21325622). It can induce neutrophil chemotaxis, adhesion, can increase the bactericidal activity of neutrophils by promoting phagocytosis via activation of SYK, PI3K/AKT, and ERK1/2 and can induce degranulation of neutrophils by a MAPK-dependent mechanism (PubMed:12626582, PubMed:15331440, PubMed:20103766). Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions (PubMed:8423249, PubMed:16258195, PubMed:19122197). The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase (PubMed:15331440, PubMed:21325622). Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX (PubMed:15642721, PubMed:22808130). The extracellular functions involve pro-inflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities (PubMed:8423249, PubMed:19534726). Its pro-inflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration (PubMed:15598812, PubMed:21487906). Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER) (PubMed:19402754). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the pro-inflammatory cascade (PubMed:19402754, PubMed:22804476). Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth (PubMed:19087201). Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3 (PubMed:19935772). Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK (PubMed:22363402). Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants (PubMed:22489132, PubMed:21912088). Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread (PubMed:16258195). Has transnitrosylase activity; in oxidatively-modified low-densitity lipoprotein (LDL(ox))-induced S-nitrosylation of GAPDH on 'Cys-247' proposed to transfer the NO moiety from NOS2/iNOS to GAPDH via its own S-nitrosylated Cys-3 (PubMed:25417112). The iNOS-S100A8/A9 transnitrosylase complex is proposed to also direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif (PubMed:25417112)

More Common Targets