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Nanotechnology-Mediated Strategy for the Treatment of Neuropathic Pain
Published in Cherry Bhargava, Amit Sachdeva, Nanotechnology, 2020
Pankaj Prashar, Ankita Sood, Anamika Gautam, Pardeep Kumar Sharma, Bimlesh Kumar, Indu Melkani, Sakshi Panchal, Sachin Kumar Singh, Monica Gulati, Narendra Kumar Pandey, Linu Dash, Anupriya, Varimadugu Bhanukirankumar Reddy
Histone deacetylase enzymes (HDAC) together with histone acetyltransferase (HAT) regulate the acetylation cycle of histone lysine residues (like lysine residue9), that further amplify transcription, expression and also facilitate transcriptional elongation. Histone acetylation is among the epigenetic pathways which are believed to trigger NP, the reasons for which are mainly focused on impaired transcriptional function (Khangura et al. 2017). Histone deacetylase 4 is gradually released as a consequence of spinal nerve ligation in rats. Histone deacetylase 4 inhibition, utilizing LMK 235, stopped allodynia. A rise in histone deacetylase 1 and reduction in histone (H3) acetylation has been shown in the spinal nerve ligation model (Elsherbiny et al. 2019; Zhao and Wu 2018). Treatment with baicalin (anti-inflammatory flavonoid) greatly decreased production of deacetylase 1 and reverse pain response. Nerve disruption can be speculated to contribute to epigenetic modifications attributable to the stimulation of histone-deacetylase enzymes. This can reduce histone acetylation induction, and inhibitors of histone-deacetylase can be used to prevent NP (Z. Li et al. 2019; Van Helleputte 2018).
Epigenetic control of cell fate and behavior
Published in David M. Gardiner, Regenerative Engineering and Developmental Biology, 2017
Acetylation of histones is nearly always associated with genes that are actively transcribed. The most commonly studied sites of acetylation are on lysine residues of histones 3 and 4. Lysine is a positively charged amino acid, which facilitates binding with negatively charged DNA. The acetylation of lysine effectively neutralizes the positive charge and weakens the affinity of DNA for the histone (Struhl 1998). In doing so, the DNA becomes more accessible to positively regulating transcription factors and, in some cases, recruits the transcription factors directly. Enzymes known as histone acetyltransferases (HATs) perform the placement of acetyl groups on histones, and the removal of acetyl groups is performed by histone deacetylases (HDACs).
Epigenotoxicity: a danger to the future life
Published in Journal of Environmental Science and Health, Part A, 2023
Farzaneh Kefayati, Atoosa Karimi Babaahmadi, Taraneh Mousavi, Mahshid Hodjat, Mohammad Abdollahi
DNA methyltransferases (DNMTs) are a group of enzymes that transmit a methyl group to the C-5 position of DNA cytosines from their cofactor s-adenosylmethionine via specific reactions. They are classified according to their function into two groups of maintenance enzymes and de novo. De novo DNMTs put methyl groups in places that already lack methyl, while maintenance of DNMTs adds methyl to hemi methyl moieties.[9] DNA methylation also occurs during cell division and is transferred to daughter cells along with the DNA sequence. DNMT1 is responsible for replicating the methylation pattern from the parent to the daughter string. As a maintenance methyltransferase, this enzyme is associated with hemimethylated DNA, showing signs of methylation in only one strand. DNMT1 also binds to hemimethylated DNA and helps methylate the daughter strand to recover fully methylated CpG dinucleotides. Thus, DNMT1 maintains the stability of this epigenetic mark across different generations. Methylated CPGs may bind to methyl-CPG proteins associated with methyl CpG binding proteins 1 and 2 (MECP1 and MECP2 (MBDs)), which can alter transcription. Methylated DNA harbors additional proteins known as methyl-CpG binding domain proteins, which interact with other proteins such as histone deacetylase (HDAC) and thus create compressed and inactive chromatin.[11] DNA methylation by DNA de novo 3 A (DNMT3A) and 3B (DNMT3B) methyltransferases is essential for genome regulation. Irregularities in the activity of these enzymes cause various diseases, especially cancer. DNMT3A is significant for establishing patterns for DNA methylation during development before birth.[12]