China
Africa
Explore chapters and articles related to this topic
Role of Histone Methyltransferase in Breast Cancer
Published in Meenu Gupta, Rachna Jain, Arun Solanki, Fadi Al-Turjman, Cancer Prediction for Industrial IoT 4.0: A Machine Learning Perspective, 2021
Surekha Manhas, Zaved Ahmed Khan
However, G9a displays its action as histone protein, such as lysine methyltransferase. Numerous studies have described G9a as also having the potential to methylate various other non-protein targets, which include G9a itself, p53, SIRT1, p21, Reptin, MyoD, WIZ and ACINUS, CDYL1, C/EBPβ, and range of numerous non-histone based targets, such as G9a itself [110], CDYL1, ACINUS, C/EBPβ, WIZ histone deacetylase (HDAC)1, CSB, KLF12, and mAM [118]. Moreover, the precise posttranslational methylation role on the protein’s function remains unclear; non-histone protein methylation might affect protein-based interactions, protein stability, subcellular localization, and subcellular function [119].
Senescent Cells as Drivers of Age-Related Diseases
Published in Shamim I. Ahmad, Aging: Exploring a Complex Phenomenon, 2017
Cielo Mae D. Marquez, Michael C. Velarde
HMGB1 is a nuclear non-histone protein that controls gene expression by bending chromatin structures to allow transcription factors to gain access to promoter regions of DNA [97,98]. HMGB1 is also involved in DNA repair pathways [99]. It attaches to DNA lesions caused by irradiation and chemotherapeutic reagents, and it is involved in nucleotide excision repair [100–102]. Aside from its role in activating transcription and DNA repair, HMGB1 may also function by inducing inflammation. As a member of the alarmin family, HMGB1 is secreted intracellularly in response to cell and tissue damage caused by trauma and pathogens [103–105].
Combination of podophyllotoxin and rutin modulate radiation-induced alterations of jejunal proteome in mice
Published in International Journal of Radiation Biology, 2020
Sania Bajaj, Syed Imteyaz Alam, Basir Ahmad, Humaira Farooqi, Manju Lata Gupta
Cytochrome c oxidase subunit 5 A (cox5a), GTP-specific succinyl-CoA synthetase beta subunit and Rho GDP, related to energy production and conversion; and signal transduction mechanisms, showed significant downregulation. PDZ and LIM domain protein 1 was the only protein of this category to show upregulated response post-radiation exposure. Except for chymotrypsinogen B precursor, G-003M could modulate the expression of rest of the identified proteins with the levels near to the untreated control animals by 840 h. Proliferating cell nuclear antigen (Pcna), a nuclear non-histone protein, essential for DNA replication and repair (Boehm et al. 2016) was significantly downregulated at 72 h and 216 h post-irradiation whereas in the G-003M pretreatment group the expression got reversed. Apoptosis Speck like protein containing card or ASC, part of inflammation machinery and also known for assisting caspase related apoptosis (Hu et al. 2016), increased gradually to 1.56 ± 0.46-fold at 216 h post-radiation exposure. A reversal in its expression levels was observed with G-003M pretreatment.
The role of pharmacogenomics in adverse drug reactions
Published in Expert Review of Clinical Pharmacology, 2019
Ramón Cacabelos, Natalia Cacabelos, Juan C. Carril
Histone deacetylation is involved in transcriptional repression and closed chromatin structure. In mammals, there are 18 HDACs, which are organized into 4 classes according to their homology to yeast. Histone deacetylation is catalyzed by these 4 classes of HDACs (class I, II, III, IV). Class I HDACs (HDAC1, 2, 3, and 8) are nuclear proteins; HDAC1 and HDAC2 are often found in transcriptional corepressor complexes (SIN3A, NuRD, CoREST), and HDAC3 is found in other complexes (SMRT/N-CoR); class II HDACs are subdivided into class IIa (HDAC4, 5,7, and 9), and IIb (HDAC6 and 10), which are located in the nucleus-cytoplasm interface and in the cytoplasm, respectively. Class III HDCAs belong to the sirtuin family, with nuclear (SIRT1, 2, 6, 7), mitochondrial (SIRT3, 4, 5), or cytoplasmic (SIRT1, 2) localization. Class IV HDAC (HDAC11) is a nuclear protein [27]. Histone deacetylases deacetylate histone and non-histone protein targets. Aberrant HDAC expression and function have been observed in several diseases. Eight types of short-chain Lys acylations have recently been identified on histones, including propionylation, butyrylation, 2-hydroxyisobutyrylation, succinylation, malonylation, glutarylation, crotonylation and β-hydroxybutyrylation. These histone modifications affect gene expression and are structurally and functionally different from the widely-studied histone Lys acetylation [68].
Non-histone substrates of histone deacetylases as potential therapeutic targets in epilepsy
Published in Expert Opinion on Therapeutic Targets, 2021
Sonali Kumar, Diksha Attrish, Arpna Srivastava, Jyotirmoy Banerjee, Manjari Tripathi, P Sarat Chandra, Aparna Banerjee Dixit
Current evidence demonstrates that alteration in the expression of HDACs and their aberrant activity significantly contributes to epileptogenesis as well as epilepsy. Over the years, the number of identified non-histone protein targets has significantly increased and these substrates are known to play an important role in several processes such as inflammation, cell death, neurogenesis, synaptic plasticity, etc. In this context, HDACs and its non-histone substrates can serve as an emerging class of molecular targets for various purposes (Figure 2).