Epigenetic Antibodies

Epigenetic signalling is a process that regulates gene expression. It involves the covalent modification of DNA, histones and other proteins that interact with DNA. These epigenetic modifications can either increase or decrease gene expression. Epigenetics plays a role in many diseases, including cancer, autoimmune diseases and psychiatric disorders. Epigenetic therapies are currently being developed to treat cancer. These therapies aim to restore the epigenetic balance in cancer cells and halt tumour growth.

Acetylation is a post translational modification (PTM) that can have a profound effect on proteins. Acetylation occurs when an acetyl group is added to a protein at a nitrogen atom of an amino acid residue. Acetylation can have a number of effects on proteins, including altering their function, stability, and location. Acetylation is a reversible process and can be removed by enzymes called deacetylases. Deacetylases are thought to be involved in a number of diseases, including cancer. Acetylation is a co-translational and post-translational modification of proteins, such as histones, p53, and tubulins.

The most common acetylated proteins are histones. Histones play a role in DNA packaging and help to regulate gene expression. Acetylation of histones is thought to be involved in the regulation of a number of biological processes, including cell division, cell death, and inflammation. Acetylation can also affect the function of other proteins, such as enzymes. For example, acetylation has been shown to increase the activity of some enzymes involved in metabolism. Almost every enzyme in glycolysis, gluconeogenesis, the tricarboxylic acid (TCA) cycle, the urea cycle, fatty acid metabolism and glycogen metabolism were discovered to be acetylated in human liver cells.

DNA methylation is the most well-known epigenetic signal and it can either activate or suppress gene expression. DNA methylation is the process by which methyl groups are added directly to a cytosine nucleotide within a cytosine-guanine sequence (CpG) by DNA methyltransferase enzymes. CpG islands are formed by repeated CpGs and 70% of gene promoters are located within CpG islands. The newly methylated CpGs result in gene silencing due to the recruitment of gene suppressor proteins and decrease interactions between DNA and transcription factors. Heterochromatin formation is also aided by methylated cytosines, which prevent the transcriptional machinery from interacting with DNA.

Crotonylation is a PTM that has been shown to play an important role in regulating proteins. This process occurs when a Crotonyl-CoA molecule is attached to a lysine amino acid residue on a protein, mainly the epsilon/ε-amino group of lysine in histones. Crotonyl-CoA is produced in the mitochondria through the action of crotonase enzymes. Crotonase enzymes are responsible for the removal of two carbons from fatty acids. The resulting Crotonyl-CoA molecule can then be used to modify proteins. Crotonylation has been shown to occur on a variety of proteins, including histones, transcription factors and enzymes. Crotonylation can affect the function and stability of proteins and may even play a role in diseases such as cancer. Crotonylation can increase or decrease the activity of a protein, depending on the location of the Crotonyl-CoA molecule.

Formylation is one of the most common PTMs that occur on proteins and it involves the addition of a formyl group to a molecule. Formylation typically occurs at the N-terminus of a protein, but it can also occur on other amino acids, such as cysteine and histidine. Formylation is thought to play a role in cellular signalling, metabolism, and development. Formylation can have a number of effects on proteins, including altering their folding, stability and function. Formylated proteins are often less stable than unmodified proteins and can be more susceptible to degradation. Formylation can also alter the activity of proteins, making them either more or less active than unmodified proteins.

Propionylation is a process that involves the addition of a propionate group to a lysine amino acid residue of a protein. Propionyl-CoA is the substrate for protein propionylation. The enzyme propionyl-CoA carboxylase metabolizes Propionyl-CoA in the cell. Propionylation is a highly regulated process and it is essential for the proper functioning of proteins in cells. Propionylation plays a critical role in many important processes, including protein synthesis, cell division and cell death. When propionylation is impaired, these processes can be disrupted which can have serious implications for cellular health. Propionylation has been shown to play a role in the development of cancer, Parkinson's disease and Alzheimer's disease.

Phosphorylation is the process of adding a phosphate group to a molecule. This process occurs in all cells of the body and is responsible for many important cellular functions. Protein phosphorylation is the PTM of proteins in which an amino acid residue is phosphorylated by a protein kinase, producing a covalently bonded phosphate group. Protein phosphorylation modifies the structure of a protein, turning it into activated or inactive, or changing its function. Protein phosphatases accelerate the reverse reaction, which is known as dephosphorylation. The most frequently phosphorylated amino acids in eukaryotes are serine, threonine, and tyrosine. Protein and DNA function can be significantly influenced by phosphorylation changes.

Butyrylation occurs when butyrate, a small molecule, attaches to a protein. Butyrate is derived from butanol, which is found in many food sources. When butyrate binds to a protein, it changes the shape of the protein and alters its function. In some cases, butyrylation can activate a protein, while in other cases it can inhibit a protein. Butyrylation is a versatile modification that can be used to regulate many different proteins.

Butyrylation can be found on histones, which are proteins that package and protect DNA. Histone butyrylation has been shown to have a variety of effects on gene expression. In some cases, butyrylation can lead to the activation of genes, while in other cases it can lead to the repression of genes. Butyrylation is also thought to play a role in the development of cancer.

Beta-hydroxy-butyrylation is a process by which enzymes attach beta-hydroxybutyrate, a ketone body, to histone proteins. This modification can impact the function of histones, and has been implicated in a variety of diseases. A recent study found that beta-hydroxy-butyrylation leads to the formation of new histone proteins and that these proteins are different from those that are not beta-hydroxy-butyrylated. The study also found that beta-hydroxy-butyrylation affects the structure of histone proteins, which could impact their function. These findings suggest that beta-hydroxy-butyrylation is a potential target for the treatment of diseases associated with histone proteins.

Succinylation is a PTM that occurs when succinyl CoA is attached to a protein. This process can have a number of effects on the protein, including altering its function, stability and localization. One major target of succinylation are histones that play a critical role in the regulation of gene expression. Succinylation of histones was found to increase the transcription of genes involved in cell proliferation and metabolism. In addition to its effects on histones, succinylation has also been shown to alter the localization of proteins. For example, succinylation has been shown to target proteins for degradation by the proteasome. This suggests that succinylation can be used as a way to regulate protein levels in cells.

Glutarylation is a dynamic process, meaning that glutamic acid residues can be added to or removed from proteins at any time. The tails of histones are subject to a variety of PTMs, including glutarylation. Glutarylation can modulate a protein's function in response to changes in the cell's environment. For example, glutarylation has been shown to increase a protein's activity, stability or solubility. It can also alter a protein's interaction with other proteins or small molecules.

Glutarylation of histones has been shown to impact gene expression in a number of ways. For example, glutarylation of histone H33 has been shown to increase its interaction with the transcription factor Sp-family proteins. This, in turn, leads to increased gene activation and expression. In addition to its impact on gene expression, glutarylation of histones has also been shown to affect DNA replication and repair. For example, glutarylation of histone H37 has been shown to promote DNA replication by interacting with the replication origin recognition complex. Lysine glutarylation (Kglu) is a newly discovered post-translational modification (PTM) that is thought to be reversible, dynamic and shared by prokaryotes and eukaryotes.

Malonylation is the addition of malonate to a protein. This process can have a significant effect on the protein's structure and function. This PTM can be catalyzed by enzymes known as malonyltransferases, which transfer malonate from coenzyme A (CoA) to the protein. Malonylation has been shown to have a wide range of effects on protein structure and function. For example, malonylation can alter the tertiary structure of a protein, change its activity or affect its interactions with other proteins. Malonylation has been shown to be involved in the regulation of cell proliferation, cell death, and gene expression. Additionally, malonylation has been implicated in the development of cancer and it is thought to be a potential target for cancer therapy.

Proteins can be modified by myristoylation, a process that adds myristic acid to the protein via an amide bond. Myristoylation is a lipid modification because myristic acid is a lipid. Myristic acid is a saturated fatty acid with 14 carbon atoms. This modification alters the function of the protein and in some cases can be essential for its activity. For example, myristoylation is required for the function of certain G protein-coupled receptors. Myristoylation can also affect the localization of a protein, as myristoylated proteins are often found in membranes. This modification is reversible and myristoylated proteins can be demyristoylated by specific enzymes. Although myristoylation is a relatively common modification, its exact role in protein function is still not fully understood.

Histone citrullination is an epigenetic PTM that alters the function of histones. Histone citrullination converts histone arginine (Arg) to citrulline and this change impacts gene expression by changing the structure of chromatin. This can lead to the activation or repression of genes depending on the location of the citrullination. This process can be regulated by enzymes called peptidylarginine deiminases (PADs). PADs convert arginine residues to citrulline in a reversible manner. Histone citrullination has been implicated in a variety of biological processes, including cell proliferation, differentiation and apoptosis. Histone citrullination has been found to be dysregulated in cancer and it is thought that this contributes to tumorigenesis. Histone citrullination is an important epigenetic modification that should be further studied to improve our understanding of gene regulation and disease pathogenesis.

O-linked-N-acetylglucosaminylation (O-GlcNAcylation)occurs when a O-GlcNAc is added onto serine or threonine residues of proteins by O-GlcNAc transferase (OGT). O-GlcNAcylation is a reversible process whereby it can be removed by O-GlcNAcase (OGA). O-GlcNAcylation aids in coupling the processes of nutrient sensing, metabolism, signal transduction and transcription. O-GlcNAcylation also plays an important role in normal physiology and physiopathology.

Histone lactylation is the addition of a lactyl group to a histone. This process can help to modify the activity of genes and gene expression. Histone lactylation is also involved in DNA replication and chromatin remodeling. Histone lactylation can be either reversible or irreversible. Research has shown that histone lactylation has been implicated in cancer development. For example, histone lactylation can help to stabilize oncogenes, which are genes that promote cancer growth.

Ubiquitylation is a post-translational modification that affects the function of proteins. It occurs when ubiquitin, a small protein (76-amino acid), is attached to another protein. Ubiquitination also has the added effect of tagging the target protein for degradation by either proteasomes or lysosomes. There are three main types of ubiquitination and they are called are called "monoubiquitination," "polyubiquitination" and "multisite mono-ubiquitination". Monoubiquitinated proteins are only attached once with one single ubiquitin molecule. Polyubiquitinated proteins are when multiple ubiquitin molecules are attached to a single protein. Multisite mono-ubiquitinated proteins are when more than one ubiquitin molecule is attached to a single lysine residue of a target protein.

Sumoylation is a PTM that involves the attachment of a small protein called sumo to another protein. SUMO proteins are ubiquitin-like molecules that are considered to be members of the ubiquitin family of proteins. Sumoylation can affect protein function in a number of ways, including changing its location within the cell, altering its interaction with other proteins and even leading to its degradation. One of the most well-characterized examples of sumoylation is its role in regulating the localization of proteins within the cell. For instance, sumoylation has been shown to target proteins to specific subcellular locations, such as the nucleus or mitochondria. In addition, sumoylation can also affect protein stability, with sumoylated proteins often being more stable than their unmodified counterparts.

Neddylation is the process by which the ubiquitin-like protein NEDD8 is conjugated to its target proteins. NEDD8 plays an important role in regulating cellular activity and is involved in a variety of processes such as cell growth, viability and development. Neddylation is a PTM that occurs after a protein has been translated from RNA. This process is similar to ubiquitination, except it uses its own E1 and E2 enzymes. Neddylation is important for the proper function of many proteins and can be dysregulated in a variety of diseases. Neddylation is a reversible process and NEDD-conjugated proteins can be de-neddylated by specific enzymes. Neddylation is linked to Alzheimer's disease and its activation appears to induce cell cycle reentry in neurons, which might drive them into apoptosis.

Histone modification is another common epigenetic signal which can either activate or suppress gene expression. Chemical modification of the histone proteins serves as a molecular switch, either turning gene expression on or off. Enzymatic acetylation, methylation, phosphorylation, and ubiquitylation are some of the chemical modifications that occur.