AI Article Synopsis
- Heat shock proteins (HSP) are important cellular proteins that help with proper protein function and are involved in various biological processes, including cancer development.
- HSPs like HSP90, HSP70, and HSP27 are well-studied for their roles in cancer growth and resistance to treatment, while HSP20 (HSPB6) has been less explored despite its significance in the cardiovascular system.
- This review highlights the emerging role of HSP20 in various cancers, showing it primarily has a protective and anticancer effect, suggesting it could be valuable in improving cancer diagnosis and treatment strategies.
Article Abstract
Heat shock proteins (HSP) are a large family of peptide proteins that are widely found in cells. Studies have shown that the expression and function of HSPs in cells are very complex, and they can participate in cellular physiological and pathological processes through multiple pathways. Multiple heat shock proteins are associated with cancer cell growth, proliferation, metastasis, and resistance to anticancer drugs, and they play a key role in cancer development by ensuring the correct folding or degradation of proteins in cancer cells. As research hotspots, HSP90, HSP70 and HSP27 have been extensively studied in cancer so far. However, HSP20, also referred to as HSPB6, as a member of the small heat shock protein family, has been shown to play an important role in the cardiovascular system, but little research has been conducted on HSP20 in cancer. This review summarizes the current cellular functions of HSP20 in different cancer types, as well as its effects on cancer proliferation, progression, prognosis, and its other functions in cancer, to illustrate the close association between HSP20 and cancer. We show that, unlike most HSPs, HSP20 mainly plays an active anticancer role in cancer development, which is expected to provide new ideas and help for cancer diagnosis and treatment and research.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.cellsig.2023.110928 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
XopAE Effector from pv. Targets HSP20-Like p23 Cochaperone to Suppress Plant Basal Immunity.
Mol Plant Microbe Interact
January 2025
Universidad de los Andes, Biology, Cra 1 # 18A-10, Bogota, Cundinamarca, Colombia, 110121;
Pathogenic bacteria use Type 3 effector proteins to manipulate host defenses and alter metabolism to favor their survival and spread. The non-model bacterial pathogen pv. () causes devastating disease in cassava.
View Article and Find Full Text PDFExploring the antifungal potential of -derived stilbenoids and cannabinoids against novel targets through protein interaction profiling.
Front Chem
January 2025
Department of Surgery, Pirogov Russian National Research Medical University, Moscow, Russia.
Cannabinoid and stilbenoid compounds derived from were screened against eight specific fungal protein targets to identify potential antifungal agents. The proteins investigated included Glycosylphosphatidylinositol (GPI), Enolase, Mannitol-2-dehydrogenase, GMP synthase, Dihydroorotate dehydrogenase (DHODH), Heat shock protein 90 homolog (Hsp90), Chitin Synthase 2 (CaChs2), and Mannitol-1-phosphate 5-dehydrogenase (M1P5DH), all of which play crucial roles in fungal survival and pathogenicity. This research evaluates the binding affinities and interaction profiles of selected cannabinoids and stilbenoids with these eight proteins using molecular docking and molecular dynamics simulations.
View Article and Find Full Text PDFThermo-sensitive polycaprolactone coacervates for preventing protein aggregation under thermal stress.
J Mater Chem B
January 2025
Shanghai Key Laboratory of Advanced Polymeric Materials, Key Laboratory for Ultrafine Materials of Ministry of Education, School of Materials Science and Engineering, East China University of Science and Technology, Shanghai, 200237, China.
Inspired from heat shock proteins (HSPs), a thermo-sensitive coacervate-forming polycaprolactone (CPCL) was designed as a natural chaperone mimic to protect proteins from thermal stress. Unlike the coil-globule polymers of poly(-isopropyl acrylamide) (PNIPAM), the as-designed CPCL underwent a partial dehydration during heating, characterizing it as a coacervate-forming polymer. With its ability to transform between the coil and coacervate states in response to temperature, theCPCL spontaneously captured and released targeted proteins, thereby behaving like a natural chaperone of HSPs.
View Article and Find Full Text PDFExposure to lower temperature during early development decreases hypoxia tolerance in juvenile Fundulus heteroclitus.
J Exp Biol
January 2025
Department of Zoology, University of British Columbia, Vancouver, BC, Canada.
Cross-protection occurs when exposure to one stressor confers heightened tolerance against a different stressor. Alternatively, exposure to one stressor could result in reduced tolerance against other stressors. Although cross-protection has been documented in a wide range of taxa at juvenile and adult life stages, whether early developmental exposure to a stressor confers cross-protection or reduced tolerance to other stressors later in life through developmental plasticity remains largely unexplored.
View Article and Find Full Text PDFAutoimmune sensorineural hearing loss/Meniere's disease possibly triggered by neurocysticercosis: a case report.
J Med Case Rep
January 2025
Centers for Advanced Ent, Woodbridge, VA, US.
Background: Meniere's disease arises when an abnormal fluid accumulation results in heightened pressure within the inner ear or labyrinth. Its symptoms encompass vertigo, tinnitus, hearing loss, and a sensation of fullness in the ear. Various triggers for Meniere's disease are known, from smoking and alcohol consumption to recent viral illnesses, allergies, and anxiety.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!