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Topic Review
Subtypes of PPARs and Breast Cancer
Breast cancer is a malignant tumor with high morbidity and lethality. Its pathogenesis is related to the abnormal expression of many genes. The peroxisome proliferator-activated receptors (PPARs) are a class of ligand-dependent transcription factors in the nuclear receptor superfamily. They can regulate the transcription of a large number of target genes, which are involved in life activities such as cell proliferation, differentiation, metabolism, and apoptosis, and regulate physiological processes such as glucose metabolism, lipid metabolism, inflammation, and wound healing. Further, the changes in its expression are associated with various diseases, including breast cancer. The PPARα, PPARβ/δ and PPARγ express differently in different tissues, with differences in target genes, biological activities, and ligand affinities. The PPARs participate in the regulation of carbohydrate and lipid metabolism and homeostasis, as well as various physiological processes such as cell differentiation, proliferation, inflammation, and vascular biology. In addition, the three subtypes of PPARs also regulate the occurrence and development of many malignant tumors via different mechanisms; breast cancer is one of them.
  • 322
  • 24 Feb 2023
Topic Review
Subtype-Specific Cardiomyocytes
Cardiogenesis produces multiple cardiac muscle cell subtypes, including the contractile cardiomyocytes constituting the four heart chambers and the non-contractile cardiomyocytes forming the cardiac conduction system. The various cardiac cellular subtypes (e.g. atrial, ventricular, nodal) are highly specified, with each subtype expressing a unique set of structural proteins, ion channels and transcription factors. Stringent spatiotemporal molecular, transcriptomic, and electrophysiological regulation gives rise to the differentiation and maturation of the multiple cardiomyocyte subtypes. The precise generation of subtype-specific cardiomyocytes is necessary for translational applications of stem cell-derived cardiomyocytes for regenerative medicine.  
  • 951
  • 21 Apr 2021
Topic Review
Sublethal Cell Death Signaling
An important role of cell death pathways is to protect tissues and minimize disease by limiting the transference of potentially oncogenic mutations to daughter clones. However, there is increasing evidence demonstrating that activation of sublethal cell death signaling pathways, in particular apoptotic signaling, in the absence of direct DNA damaging stimuli, can promote genomic instability in cells that fail to die. This may increase the risk of the formation of subsequent neoplasms. Apoptosis-mediated mutagenesis occurs indirectly via sublethal activation of caspases and apoptotic nucleases (specifically CAD). On the other hand, cells surviving sublethal necroptotic signaling did not acquire mutations, most likely due to caspase-independent pathways, although the possibility of mutagenesis under conditions of oxidative stress are still elusive. It may therefore be possible for necroptosis-inducing anti-cancer drugs to be less likely than apoptosis-inducing or DNA damaging drugs to trigger therapy-related cancers.
  • 775
  • 12 Jul 2021
Topic Review
Subcellular Localization of Membrane-Type-1 Matrix Metalloproteinase
Matrix metalloproteinases (MMPs) are critical enzymes involved in a variety of cellular processes. MMPs are well known for their ability to degrade the extracellular matrix (ECM) and their extracellular role in cell migration. Membrane-type-1 matrix metalloproteinase (MT1-MMP), a transmembrane protein, is first known to localize to the cell membrane.
  • 501
  • 15 Sep 2022
Topic Review
STxB in Mucosal Vaccination
One mucosal vaccine candidate is the B-subunit of Shiga toxin, STxB. STxB is a non-toxic protein that binds to a glycosylated lipid, termed globotriaosylceramide (Gb3), which is preferentially expressed by dendritic cells. 
  • 489
  • 25 Mar 2022
Topic Review
Structure, Expression Regulation, and Subcellular Localization of USP16
Ubiquitin-specific peptidase 16 (USP16) is a deubiquitinase that plays a role in the regulation of gene expression, cell cycle progression, and various other functions. It was originally identified as the major deubiquitinase for histone H2A and has since been found to deubiquitinate a range of other substrates, including proteins from both the cytoplasm and nucleus. USP16 is phosphorylated when cells enter mitosis and dephosphorylated during the metaphase/anaphase transition. While much of USP16 is localized in the cytoplasm, separating the enzyme from its substrates is considered an important regulatory mechanism. Some of the functions that USP16 has been linked to include DNA damage repair, immune disease, tumorigenesis, protein synthesis, coronary artery health, and male infertility. The strong connection to immune response and the fact that multiple oncogene products are substrates of USP16 suggests that USP16 may be a potential therapeutic target for the treatment of certain human diseases.
  • 760
  • 06 Apr 2023
Topic Review
Structure and Function of Peroxiredoxin IV
Peroxiredoxin IV (Prx4) is a 2-Cysteine peroxidase with ubiquitous expression in human tissues. Prx4 scavenges hydrogen peroxide and participates in oxidative protein folding in the endoplasmic reticulum. In addition, Prx4 is secreted outside the cell. Prx4 is upregulated in several cancers and is a potential therapeutic target. Here, the resarchers have summarized the structure and function of Prx4. Oxidative stress is known to activate pro-inflammatory pathways. Chronic inflammation is a risk factor for cancer development. Hence, redox enzymes such as Prx4 are important players in the crosstalk between inflammation and cancer. Understanding molecular mechanisms of regulation of Prx4 expression and associated signaling pathways in normal physiological and disease conditions should reveal new therapeutic strategies. Although Prx4 is a promising therapeutic target for inflammatory diseases and cancer, further research needs to be conducted to bridge the gap to clinical application. 
  • 441
  • 17 Oct 2022
Topic Review
Structure and Architecture of BRCT Domains
The human BRCT domain was first resolved from the crystal structure of the N-terminal BRCT of the X-ray repair cross-complementing protein 1 (XRCC1), determined by X-ray crystallography to a 3.2 Å resolution. Its tertiary structure features a central core of four-stranded parallel β-sheet (β1, β2, β3, and β4) flanked by two α-helices (α1 and α3) on the C-terminal end, a single α-helix (α2) on the N-terminal end, and two surface loops connecting β1 with α1 and α2 with β3 (the overall structure being β1-α1-β2-β3-α2-β4-α3). BRCT domains have been identified in a wide group of living organisms (from bacteria, parasites to mammals) and viruses. As mentioned above, those domains take part in a variety of important cell processes including DDR and cell cycle control. In addition, a few of these protein modules have been shown to be involved in pathologies such as cancer or infectious diseases including leishmaniasis. Therefore, significant efforts have been made towards finding compounds able to specifically inhibit the functions of these protein domains.
  • 291
  • 24 Jul 2023
Topic Review
Structural Glial–Neuronal Mechanisms of Mitochondrial Transfer
Glial–neuronal mitochondrial transfer is mediated via a number of active processes including the release of extracellular vesicles, the formation of tunnelling nanotubes, and potentially other mechanisms.
  • 623
  • 07 Dec 2022
Topic Review
Stress Granules Dynamics during Acute Ischemic Stroke
Ischemic stroke is a leading cause of death and disability worldwide. Following an ischemic insult, cells undergo endoplasmic reticulum (ER) stress, which increases the ER’s protein-folding and degradative capacities and blocks the global synthesis of proteins by phosphorylating the eukaryotic translation initiation factor 2-alpha (eIF2α). Phosphorylation of eIF2α is directly related to the dynamics of stress granules (SGs), which are membraneless organelles composed of RNA-binding proteins and mRNA. SGs play a critical role in mRNA metabolism and translational control. Other translation factors are also linked to cellular pathways, including SG dynamics following a stroke. Because the formation of SGs is closely connected to mRNA translation, it is interesting to explore the relationship between SG dynamics and cellular outcome in cases of ischemic damage.
  • 469
  • 19 Apr 2022
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