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Topic Review
HO-1 in Cancer Cell Survival
Heme oxygenases (HOs) act on heme degradation to produce carbon monoxide (CO), free iron, ferritin, and biliverdin. Upregulation of cellular HO-1 levels is signature of oxidative stress for its downstream effects particularly under pro-oxidative status. Subcellular traffics of HO-1 to different organelles constitute a network of interactions compromising a variety of effectors such as pro-oxidants, ROS, mitochondrial enzymes, and nucleic transcription factors. Some of the compartmentalized HO-1 have been demonstrated as functioning in the progression of cancer. Emerging data show the multiple roles of HO-1 in tumorigenesis from pathogenesis to the progression to malignancy, metastasis, and even resistance to therapy. However, the role of HO-1 in tumorigenesis has not been systematically addressed.
  • 523
  • 28 Sep 2021
Topic Review
Homologous Recombination Repair Deficiency
Homologous recombination repair deficiency (HRD) can be observed in virtually all cancer types. Cells possess a complex set of non-redundant and partially overlapping pathways to detect and repair DNA damage. In cancer, DNA damage repair (DDR) is frequently disrupted, leading to genomic instability. One of the pathways that is regularly altered in cancer is HR. HR is an important pathway for the repair of double-strand DNA breaks (DSBs) during the S and G2 phase of the cell cycle, i.e., after DNA replication has occurred. HR is considered a relatively error-free process because it uses an intact sister chromatid to guide DNA repair. HR deficiency (HRD) leads to enhanced reliance on alternative pathways involved in DSB repair, i.e., classical NHEJ, alternative end joining, and single-strand annealing. These pathways repair DSBs without a homologous DNA template, resulting in characteristic genomic scars across the genome.
  • 785
  • 25 May 2021
Topic Review
Homology-Directed Repair in Cell Cycle
Genome editing is currently widely used in biomedical research; however, the use of this method in the clinic is still limited because of its low efficiency and possible side effects. Moreover, the correction of mutations that cause diseases in humans seems to be extremely important and promising. Numerous attempts to improve the efficiency of homology-directed repair-mediated correction of mutations in mammalian cells have focused on influencing the cell cycle. Homology-directed repair is known to occur only in the late S and G2 phases of the cell cycle, so safe ways are studied to enrich the cell culture with cells in these phases of the cell cycle. 
  • 643
  • 24 Jun 2022
Topic Review
Host Cell Signatures within Beta-Herpes Virions
Beta-herpesviruses infect a large proportion of the human population and are associated with a variety of pathophysiological conditions. They are DNA viruses with a large genome that encodes a relatively large number of gene products for the construction of new viral progeny and the establishment of a complex series of interactions with infected cells.
  • 444
  • 22 Sep 2022
Topic Review
Host-Released Extracellular Vesicles
Extracellular vesicles (EVs) are mediators of communication by transferring messenger bioactive molecules including proteins, lipids, and miRNAs between cells and tissues. The specific functions of EVs principally depend on the internal cargo, which upon delivery to target cells trigger signal events that modulate cellular functions. The vesicular cargo is greatly influenced by genetic, pathological, and environmental factors.
  • 551
  • 09 Apr 2021
Topic Review
HSP-Related iPS Cell Lines
Hereditary spastic paraplegias (HSPs) comprise a family of degenerative diseases mostly hitting descending axons of corticospinal neurons. Depending on the gene and mutation involved, the disease could present as a pure form with limb spasticity, or a complex form associated with cerebellar and/or cortical signs such as ataxia, dysarthria, epilepsy, and intellectual disability. The progressive nature of HSPs invariably leads patients to require walking canes or wheelchairs over time. The advent of induced pluripotent stem (iPS) cells allowed instead the direct study of morphological and molecular properties of the patient’s affected neurons generated upon in vitro differentiation.
  • 223
  • 12 Mar 2024
Topic Review
HSP60
Heat shock proteins are generally responsible for preventing damage to proteins in response to high levels of heat. Heat shock proteins are classified into six major families based on their molecular mass: small HSPs, HSP40, HSP60, HSP70, HSP90, and HSP110 HSP60 is implicated in mitochondrial protein import and macromolecular assembly. It may facilitate the correct folding of imported proteins, and may also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. HSP60 interacts with HRAS and with HBV protein X and HTLV-1 protein p40tax. HSP60 belongs to the chaperonin (HSP60) family. Note: This description may include information from UniProtKB. Alternate Names: 60 kDa chaperonin, Chaperonin 60, CPN60, Heat shock protein 60, HSP-60, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein, HSPD1 Heat shock protein 60 (HSP60) is a mitochondrial chaperonin that is typically held responsible for the transportation and refolding of proteins from the cytoplasm into the mitochondrial matrix. In addition to its role as a heat shock protein, HSP60 functions as a chaperonin to assist in folding linear amino acid chains into their respective three-dimensional structure. Through the extensive study of groEL, HSP60’s bacterial homolog, HSP60 has been deemed essential in the synthesis and transportation of essential mitochondrial proteins from the cell's cytoplasm into the mitochondrial matrix. Further studies have linked HSP60 to diabetes, stress response, cancer and certain types of immunological disorders.
  • 848
  • 22 Nov 2022
Topic Review
HSP70 in Cancer
The 70-kDa heat shock proteins (HSP70s) are abundantly present in cancer, providing malignant cells selective advantage by suppressing multiple apoptotic pathways, regulating necrosis, bypassing cellular senescence program, interfering with tumor immunity, promoting angiogenesis and supporting metastasis. This direct involvement of HSP70 in most of the cancer hallmarks explains the phenomenon of cancer “addiction” to HSP70, tightly linking tumor survival and growth to the HSP70 expression. HSP70 operates in different states through its catalytic cycle, suggesting that it can multi-function in malignant cells in any of these states. Clinically, tumor cells intensively release HSP70 in extracellular microenvironment, resulting in diverse outcomes for patient survival. Given its clinical significance, small molecule inhibitors were developed to target different sites of the HSP70 machinery. Furthermore, several HSP70-based immunotherapy approaches were assessed in clinical trials.
  • 808
  • 19 May 2021
Topic Review
Hsp90α and Hsp90β
Hsp90α and Hsp90β are both ubiquitously expressed in all cell types, but assigned for distinct and irreplaceable functions. Hsp90β is essential during mouse development and Hsp90α only maintains male reproductivity in adult mice. Neither Hsp90β nor Hsp90α could substitute each other under these biological processes. Hsp90β alone maintains cell survival in culture and Hsp90α cannot substitute it. Hsp90α also has extracellular functions under stress and Hsp90β does not.
  • 395
  • 02 Feb 2023
Topic Review
Human In Vitro Stem Cell-Derived Models of Epilepsy
The challenges in making animal models of complex human epilepsy phenotypes with varied aetiology highlights the need to develop alternative disease models that can address the limitations of animal models by effectively recapitulating human pathophysiology. The advances in stem cell technology provide an opportunity to use human iPSCs to make disease-in-a-dish models.
  • 513
  • 26 Dec 2022
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