scholarly journals Molecular and Cellular Functions of the Linker Histone H1.2

2022 ◽  
Vol 9 ◽  
Author(s):  
Shuting Lai ◽  
Jin Jia ◽  
Xiaoyu Cao ◽  
Ping-Kun Zhou ◽  
Shanshan Gao
Keyword(s):  
Genome Stability ◽  
Target Genes ◽  
Current Knowledge ◽  
Linker Histone ◽  
Cellular Functions ◽  
Cancer Cell Growth ◽  
Cell Growth And Migration ◽  
Chromatin Dynamics ◽  
Cellular Processes ◽  
And Migration

Linker histone H1.2, which belongs to the linker histone family H1, plays a crucial role in the maintenance of the stable higher-order structures of chromatin and nucleosomes. As a critical part of chromatin structure, H1.2 has an important function in regulating chromatin dynamics and participates in multiple other cellular processes as well. Recent work has also shown that linker histone H1.2 regulates the transcription levels of certain target genes and affects different processes as well, such as cancer cell growth and migration, DNA duplication and DNA repair. The present work briefly summarizes the current knowledge of linker histone H1.2 modifications. Further, we also discuss the roles of linker histone H1.2 in the maintenance of genome stability, apoptosis, cell cycle regulation, and its association with disease.

scholarly journals p66α Suppresses Breast Cancer Cell Growth and Migration by Acting as Co-Activator of p53

Cells ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 3593
Author(s):  
Qun Zhang ◽  
Yihong Zhang ◽  
Jie Zhang ◽  
Dan Zhang ◽  
Mengying Li ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Growth ◽  
Tumor Suppressor ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Target Genes ◽  
Cancer Cell Growth ◽  
Cell Growth And Migration ◽  
Breast Cancer Cell Growth ◽  
And Migration

p66α is a GATA zinc finger domain-containing transcription factor that has been shown to be essential for gene silencing by participating in the NuRD complex. Several studies have suggested that p66α is a risk gene for a wide spectrum of diseases such as diabetes, schizophrenia, and breast cancer; however, its biological role has not been defined. Here, we report that p66α functions as a tumor suppressor to inhibit breast cancer cell growth and migration, evidenced by the fact that the depletion of p66α results in accelerated tumor growth and migration of breast cancer cells. Mechanistically, immunoprecipitation assays identify p66α as a p53-interacting protein that binds the DNA-binding domain of p53 molecule predominantly via its CR2 domain. Depletion of p66α in multiple breast cells results in decreased expression of p53 target genes, while over-expression of p66α results in increased expression of these target genes. Moreover, p66α promotes the transactivity of p53 by enhancing p53 binding at target promoters. Together, these findings demonstrate that p66α is a tumor suppressor by functioning as a co-activator of p53.

scholarly journals Development of a Decellularized Porcine Esophageal Matrix for Potential Applications in Cancer Modeling

Cells ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1055
Author(s):  
Hersh Chaitin ◽  
Michael L. Lu ◽  
Michael B. Wallace ◽  
Yunqing Kang
Keyword(s):  
Cell Growth ◽  
Lymphatic Vessels ◽  
Significant Loss ◽  
Cancer Cell Growth ◽  
Cell Growth And Migration ◽  
Decellularized Extracellular Matrix ◽  
Cancer Models ◽  
The Matrix ◽  
Potential Applications ◽  
And Migration

Many decellularized extracellular matrix-derived whole organs have been widely used in studies of tissue engineering and cancer models. However, decellularizing porcine esophagus to obtain decellularized esophageal matrix (DEM) for potential biomedical applications has not been widely investigated. In this study a modified decellularization protocol was employed to prepare a porcine esophageal DEM for the study of cancer cell growth. The cellular removal and retention of matrix components in the porcine DEM were fully characterized. The microstructure of the DEM was observed using scanning electronic microscopy. Human esophageal squamous cell carcinoma (ESCC) and human primary esophageal fibroblast cells (FBCs) were seeded in the DEM to observe their growth. Results show that the decellularization process did not cause significant loss of mechanical properties and that blood ducts and lymphatic vessels in the submucosa layer were also preserved. ESCC and FBCs grew on the DEM well and the matrix did not show any toxicity to cells. When FBS and ESCC were cocultured on the matrix, they secreted more periostin, a protein that supports cell adhesion on matrix. This study shows that the modified decellularization protocol can effectively remove the cell materials and maintain the microstructure of the porcine esophageal matrix, which has the potential application of studying cell growth and migration for esophageal cancer models.

scholarly journals Relating GPI-Anchored Ly6 Proteins uPAR and CD59 to Viral Infection

Viruses ◽  
2019 ◽  
Vol 11 (11) ◽  
pp. 1060 ◽  
Author(s):  
Yu ◽  
Murthy ◽  
Liu
Keyword(s):  
Viral Infection ◽  
Viral Entry ◽  
Current Knowledge ◽  
Cellular Functions ◽  
Lymphocyte Antigen ◽  
Host Interaction ◽  
Type Plasminogen Activator ◽  
Cell Adhesion And Migration ◽  
And Migration

The Ly6 (lymphocyte antigen-6)/uPAR (urokinase-type plasminogen activator receptor) superfamily protein is a group of molecules that share limited sequence homology but conserved three-fingered structures. Despite diverse cellular functions, such as in regulating host immunity, cell adhesion, and migration, the physiological roles of these factors in vivo remain poorly characterized. Notably, increasing research has focused on the interplays between Ly6/uPAR proteins and viral pathogens, the results of which have provided new insight into viral entry and virus–host interactions. While LY6E (lymphocyte antigen 6 family member E), one key member of the Ly6E/uPAR-family proteins, has been extensively studied, other members have not been well characterized. Here, we summarize current knowledge of Ly6/uPAR proteins related to viral infection, with a focus on uPAR and CD59. Our goal is to provide an up-to-date view of the Ly6/uPAR-family proteins and associated virus–host interaction and viral pathogenesis.

scholarly journals Chromatin dynamics during interphase and cell division: similarities and differences between model and crop plants

2019 ◽  
Vol 71 (17) ◽  
pp. 5205-5222 ◽  
Author(s):  
Ales Pecinka ◽  
Christian Chevalier ◽  
Isabelle Colas ◽  
Kriton Kalantidis ◽  
Serena Varotto ◽  
...  
Keyword(s):  
Genetic Information ◽  
Molecular Mechanisms ◽  
Current Knowledge ◽  
Crop Plants ◽  
Regulatory Proteins ◽  
Abiotic And Biotic Stresses ◽  
Chromatin Dynamics ◽  
Biotic Stresses ◽  
Cellular Processes ◽  
Organismal Development

Abstract Genetic information in the cell nucleus controls organismal development and responses to the environment, and finally ensures its own transmission to the next generations. To achieve so many different tasks, the genetic information is associated with structural and regulatory proteins, which orchestrate nuclear functions in time and space. Furthermore, plant life strategies require chromatin plasticity to allow a rapid adaptation to abiotic and biotic stresses. Here, we summarize current knowledge on the organization of plant chromatin and dynamics of chromosomes during interphase and mitotic and meiotic cell divisions for model and crop plants differing as to genome size, ploidy, and amount of genomic resources available. The existing data indicate that chromatin changes accompany most (if not all) cellular processes and that there are both shared and unique themes in the chromatin structure and global chromosome dynamics among species. Ongoing efforts to understand the molecular mechanisms involved in chromatin organization and remodeling have, together with the latest genome editing tools, potential to unlock crop genomes for innovative breeding strategies and improvements of various traits.

ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors

2006 ◽  
Vol 291 (1) ◽  
pp. C1-C10 ◽  
Author(s):  
Haruhiko Ohtsu ◽  
Peter J. Dempsey ◽  
Satoru Eguchi
Keyword(s):  
G Protein ◽  
Egf Receptor ◽  
Current Knowledge ◽  
G Protein Coupled Receptors ◽  
Surface Proteins ◽  
Egf Receptors ◽  
Cellular Functions ◽  
Egfr Transactivation ◽  
And Migration ◽  
G Protein Coupled

A disintegrin and metalloprotease (ADAM) is a membrane-anchored metalloprotease implicated in the ectodomain shedding of cell surface proteins, including the ligands for epidermal growth factor (EGF) receptors (EGFR)/ErbB. It has been well documented that the transactivation of the EGFR plays critical roles for many cellular functions, such as proliferation and migration mediated through multiple G protein-coupled receptors (GPCRs). Recent accumulating evidence has suggested that ADAMs are the key metalloproteases activated by several GPCR agonists to produce a mature EGFR ligand leading to the EGFR transactivation. In this review, we describe the current knowledge on ADAMs implicated in mediating EGFR transactivation. The major focus of the review will be on the possible upstream mechanisms of ADAM activation by GPCRs as well as downstream signal transduction and the pathophysiological significances of ADAM-dependent EGFR transactivation.

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