keyword
https://read.qxmd.com/read/38672583/heat-shock-proteins-a-double-edged-sword-significance-in-cancer-progression-chemotherapy-resistance-and-novel-therapeutic-perspectives
#1
REVIEW
Dominika Kunachowicz, Magdalena Król-Kulikowska, Wiktoria Raczycka, Jakub Sleziak, Marta Błażejewska, Julita Kulbacka
Heat shock proteins (Hsps) are involved in one of the adaptive mechanisms protecting cells against environmental and metabolic stress. Moreover, the large role of these proteins in the carcinogenesis process, as well as in chemoresistance, was noticed. This review aims to draw attention to the possibilities of using Hsps in developing new cancer therapy methods, as well as to indicate directions for future research on this topic. In order to discuss this matter, a thorough review of the latest scientific literature was carried out, taking into account the importance of selected proteins from the Hsp family, including Hsp27, Hsp40, Hsp60, Hsp70, Hsp90 and Hsp110...
April 14, 2024: Cancers
https://read.qxmd.com/read/38660660/prognosis-value-of-heat-shock-proteins-in-esophageal-and-esophagogastric-cancer-a-systematic-review-and-meta-analysis
#2
JOURNAL ARTICLE
Eric Toshiyuki Nakamura, Amanda Park, Marina Alessandra Pereira, Daniel Kikawa, Francisco Tustumi
BACKGROUND: Heat shock proteins (HSPs) are molecular chaperones that play an important role in cellular protection against stress events and have been reported to be overexpressed in many cancers. The prognostic significance of HSPs and their regulatory factors, such as heat shock factor 1 (HSF1) and CHIP, are poorly understood. AIM: To investigate the relationship between HSP expression and prognosis in esophageal and esophagogastric cancer. METHODS: A systematic review was conducted in accordance with PRISMA recommendations (PROSPERO: CRD42022370653), on Embase, PubMed, Cochrane, and LILACS...
April 15, 2024: World Journal of Gastrointestinal Oncology
https://read.qxmd.com/read/38657882/modulating-responses-of-indicator-genes-in-cellular-homeostasis-immune-defense-and-apoptotic-process-in-the-macrophthalmus-japonicus-exposed-to-di-2-ethylhexyl-phthalate-as-a-plastic-additive
#3
JOURNAL ARTICLE
Kiyun Park, Ihn-Sil Kwak
Di(2-ethylhexyl) phthalate (DEHP), have been increasingly used as plasticizers to manufacture soft and flexible materials and ubiquitously found in water and sediments in the aquatic ecosystem. The aim of the present study was to evaluate the effect of DEHP exposure on cellular homeostasis (HSF1 and seven HSPs), immune responses (ILF), and apoptotic responses (p53, BAX, Bcl-2). DEHP exposure upregulated the expression of HSF1 and ILF. Moreover, it altered the expression levels of HSPs (upregulation of HSP70, HSP90, HSP40, HSP83, and HSP67B2 and downregulation of HSP60 and HSP21) in conjunction with HSF1 and ILF in the gills and hepatopancreas of M...
April 22, 2024: Environmental Toxicology and Pharmacology
https://read.qxmd.com/read/38648719/mrj-is-a-chaperone-of-the-hsp40-family-that-regulates-orb2-oligomerization-and-long-term-memory-in-drosophila
#4
JOURNAL ARTICLE
Meghal Desai, Hemant, Ankita Deo, Jagyanseni Naik, Prathamesh Dhamale, Avinash Kshirsagar, Tania Bose, Amitabha Majumdar
Orb2 the Drosophila homolog of cytoplasmic polyadenylation element binding (CPEB) protein forms prion-like oligomers. These oligomers consist of Orb2A and Orb2B isoforms and their formation is dependent on the oligomerization of the Orb2A isoform. Drosophila with a mutation diminishing Orb2A's prion-like oligomerization forms long-term memory but fails to maintain it over time. Since this prion-like oligomerization of Orb2A plays a crucial role in the maintenance of memory, here, we aim to find what regulates this oligomerization...
April 2024: PLoS Biology
https://read.qxmd.com/read/38599159/molecular-strategies-of-the-pygmy-grasshopper-eucriotettix-oculatus-adapting-to-long-term-heavy-metal-pollution
#5
JOURNAL ARTICLE
Xiao-Dong Li, Guo-Fang Jiang, Ran Li, Yi Bai, Guo-Song Zhang, Shu-Juan Xu, Wei-An Deng
To study the heavy metal accumulation and its impact on insect exterior and chromosome morphology, and reveal the molecular mechanism of insects adapting to long-term heavy metal compound pollution habitats, this study, in the Diaojiang river basin, which has been polluted by heavy metals(HMs) for nearly a thousand years, two Eucriotettix oculatus populations was collected from mining and non-mining areas. It was found that the contents of 7 heavy metals (As, Cd, Pb, Zn, Cu, Sn, Sb) in E. oculatus of the mining area were higher than that in the non-mining 1-11 times...
April 9, 2024: Ecotoxicology and Environmental Safety
https://read.qxmd.com/read/38597740/the-plasma-proteome-is-linked-with-left-ventricular-and-left-atrial-function-parameters-in-patients-with-chronic-heart-failure
#6
JOURNAL ARTICLE
S Abou Kamar, K Andrzejczyk, T B Petersen, J F Chin, Y S Aga, M de Bakker, K M Akkerhuis, M Geleijnse, J J Brugts, O Sorop, R A de Boer, D Rizopoulos, F W Asselbergs, E Boersma, H den Ruijter, B M van Dalen, I Kardys
BACKGROUND: Examining the systemic biological processes in the heterogeneous syndrome of heart failure with reduced ejection fraction (HFrEF), as reflected by circulating proteins, in relation to echocardiographic characteristics, may provide insights into HF pathophysiology. OBJECTIVE: We investigated the link of 4210 repeatedly measured circulating proteins with repeatedly measured echocardiographic parameters, as well as with elevated left atrial pressure (LAP), in HFrEF patients, to provide insights into underlying mechanisms...
April 10, 2024: European Heart Journal Cardiovascular Imaging
https://read.qxmd.com/read/38534118/hsp90-a-team-player-in-protein-quality-control-and-the-stress-response-in-bacteria
#7
REVIEW
Anushka C Wickramaratne, Sue Wickner, Andrea N Kravats
SUMMARYHeat shock protein 90 (Hsp90) participates in proteostasis by facilitating protein folding, activation, disaggregation, prevention of aggregation, degradation, and protection against degradation of various cellular proteins. It is highly conserved from bacteria to humans. In bacteria, protein remodeling by Hsp90 involves collaboration with the Hsp70 molecular chaperone and Hsp70 cochaperones. In eukaryotes, protein folding by Hsp90 is more complex and involves collaboration with many Hsp90 cochaperones as well as Hsp70 and Hsp70 cochaperones...
March 27, 2024: Microbiology and Molecular Biology Reviews: MMBR
https://read.qxmd.com/read/38529663/comparative-structural-and-functional-analysis-of-the-glycine-rich-regions-of-class-a-and-b-j-domain-protein-cochaperones-of-hsp70
#8
JOURNAL ARTICLE
Szymon J Ciesielski, Brenda A Schilke, Milena Stolarska, Marco Tonelli, Bartlomiej Tomiczek, Elizabeth A Craig
J-domain proteins are critical Hsp70 co-chaperones. A and B types have a poorly understood glycine-rich region (Grich ) adjacent to their N-terminal J-domain (Jdom ). We analyzed the ability of Jdom /Grich segments of yeast Class B Sis1 and a suppressor variant of Class A, Ydj1, to rescue the inviability of sis1-∆. In each, we identified a cluster of Grich residues required for rescue. Both contain conserved hydrophobic and acidic residues and are predicted to form helices. While, as expected, the Sis1 segment docks on its J-domain, that of Ydj1 does not...
March 26, 2024: FEBS Letters
https://read.qxmd.com/read/38518665/intermittent-mild-cold-acclimation-ameliorates-intestinal-inflammation-and-immune-dysfunction-in-acute-cold-stressed-broilers-by-regulating-the-tlr4-myd88-nf-%C3%AE%C2%BAb-pathway
#9
JOURNAL ARTICLE
Yanju Bi, Haidong Wei, Yiwen Chai, Hongyu Wang, Qiang Xue, Jianhong Li
To investigate the potential protective effect of prior cold stimulation on broiler intestine induced by acute cold stress (ACS). A total of 384 one-day-old broilers were divided into control (CON), ACS, cold stimulation Ⅰ (CS3+ACS), and cold stimulation Ⅱ (CS9+ACS) groups. Broilers in CON and ACS groups were reared normally, and birds in CS3+ACS and CS9+ACS groups were reared at 3℃ and 9℃ below CON group for 5 h, respectively, on alternate days from d 15 to 35. Broilers in ACS, CS3+ACS, and CS9+ACS groups were subjected to 10℃ for 24 h on d 43...
March 8, 2024: Poultry Science
https://read.qxmd.com/read/38483597/fungal-heat-shock-proteins-molecular-phylogenetic-insights-into-the-host-takeover
#10
JOURNAL ARTICLE
João Pedro Nunes Sagini, Rodrigo Ligabue-Braun
Heat shock proteins are constitutively expressed chaperones induced by cellular stress, such as changes in temperature, pH, and osmolarity. These proteins, present in all organisms, are highly conserved and are recruited for the assembly of protein complexes, transport, and compartmentalization of molecules. In fungi, these proteins are related to their adaptation to the environment, their evolutionary success in acquiring new hosts, and regulation of virulence and resistance factors. These characteristics are interesting for assessment of the host adaptability and ecological transitions, given the emergence of infections by these microorganisms...
March 14, 2024: Die Naturwissenschaften
https://read.qxmd.com/read/38473160/selection-signal-analysis-reveals-hainan-yellow-cattle-are-being-selectively-bred-for-heat-tolerance
#11
JOURNAL ARTICLE
Liuhao Wang, Xuehao Yan, Hongfen Wu, Feifan Wang, Ziqi Zhong, Gang Zheng, Qian Xiao, Kebang Wu, Wei Na
Hainan yellow cattle are indigenous Zebu cattle from southern China known for their tolerance of heat and strong resistance to disease. Generations of adaptation to the tropical environment of southern China and decades of artificial breeding have left identifiable selection signals in their genomic makeup. However, information on the selection signatures of Hainan yellow cattle is scarce. Herein, we compared the genomes of Hainan yellow cattle with those of Zebu, Qinchuan, Nanyang, and Yanbian cattle breeds by the composite likelihood ratio method (CLR), Tajima's D method, and identifying runs of homozygosity (ROHs), each of which may provide evidence of the genes responsible for heat tolerance in Hainan yellow cattle...
February 29, 2024: Animals: An Open Access Journal From MDPI
https://read.qxmd.com/read/38449709/heat-shock-protein-paradigms-in-cancer-progression-future-therapeutic-perspectives
#12
REVIEW
Y Mohammed Tausif, Dithu Thekkekkara, Thummuru Ekshita Sai, Vaishnavi Jahagirdar, H R Arjun, S K Meheronnisha, Amrita Babu, Aniruddha Banerjee
Heat-shock proteins (HSPs), also known as stress proteins, are ubiquitously present in all forms of life. They play pivotal roles in protein folding and unfolding, the formation of multiprotein complexes, the transportation and sorting of proteins into their designated subcellular compartments, the regulation of the cell cycle, and signalling processes. These HSPs encompass HSP27, HSP40, HSP70, HSP60, and HSP90, each contributing to various cellular functions. In the context of cancer, HSPs exert influence by either inhibiting or activating diverse signalling pathways, thereby impacting growth, differentiation, and cell division...
April 2024: 3 Biotech
https://read.qxmd.com/read/38418371/plasmodium-falciparum-j-dot-localized-j-domain-protein-a8ijp-modulates-the-chaperone-activity-of-human-hspa8
#13
JOURNAL ARTICLE
Welka Sahu, Tapaswini Bai, Aleena Das, Subhadip Mukherjee, Aradhana Prusty, Nipa Rani Mallick, Selvakumar Elangovan, K Sony Reddy
Plasmodium falciparum renovates the host erythrocyte to survive during intraerythrocytic development. This renovation requires many parasite proteins to unfold and move outside the parasitophorous vacuolar membrane, and chaperone-regulated protein folding becomes essential for the exported proteins to function. We report on a type-IV J domain protein (JDP), PF3D7_1401100, which we found to be processed before export and trafficked inside the lumen of parasite-derived structures known as J-dots. We found this protein to have holdase activity, as well as stimulate the ATPase and aggregation suppression activity of the human HSP70 chaperone HsHSPA8; thus, we named it "HSPA8-interacting J protein" (A8iJp)...
February 28, 2024: FEBS Letters
https://read.qxmd.com/read/38403745/tissue-distribution-of-cysteine-string-protein-dnajc5-in-c-elegans-analysed-by-crispr-cas9-mediated-tagging-of-endogenous-dnj-14
#14
JOURNAL ARTICLE
Eleanor Barker, Alan Morgan, Jeff W Barclay
Cysteine string protein (CSP) is a member of the DnaJ/Hsp40 family of molecular chaperones. CSP is enriched in neurons, where it mainly localises to synaptic vesicles. Mutations in CSP-encoding genes in flies, worms, mice and humans result in neuronal dysfunction, neurodegeneration and reduced lifespan. Most attention has therefore focused on CSP's neuronal functions, although CSP is also expressed in non-neuronal cells. Here, we used genome editing to fluorescently tag the Caenorhabditis elegans CSP orthologue, dnj-14, to identify which tissues preferentially express CSP and hence may contribute to the observed mutant phenotypes...
February 26, 2024: Cell and Tissue Research
https://read.qxmd.com/read/38379086/control-of-meiotic-crossover-interference-by-a-proteolytic-chaperone-network
#15
JOURNAL ARTICLE
Heejin Kim, Jaeil Kim, Namil Son, Pallas Kuo, Chris Morgan, Aurélie Chambon, Dohwan Byun, Jihye Park, Youngkyung Lee, Yeong Mi Park, John A Fozard, Julie Guérin, Aurélie Hurel, Christophe Lambing, Martin Howard, Ildoo Hwang, Raphael Mercier, Mathilde Grelon, Ian R Henderson, Kyuha Choi
Meiosis is a specialized eukaryotic division that produces genetically diverse gametes for sexual reproduction. During meiosis, homologous chromosomes pair and undergo reciprocal exchanges, called crossovers, which recombine genetic variation. Meiotic crossovers are stringently controlled with at least one obligate exchange forming per chromosome pair, while closely spaced crossovers are inhibited by interference. In Arabidopsis, crossover positions can be explained by a diffusion-mediated coarsening model, in which large, approximately evenly spaced foci of the pro-crossover E3 ligase HEI10 grow at the expense of smaller, closely spaced clusters...
February 20, 2024: Nature Plants
https://read.qxmd.com/read/38377589/the-regulatory-effect-of-huangshui-polysaccharides-on-intestinal-microbiota-and-metabolites-during-in-vitro-fermentation
#16
JOURNAL ARTICLE
Mei Li, Jian Su, Jihong Wu, Dong Zhao, Mingquan Huang, Yanping Lu, Jia Zheng, Fuping Zheng, Baoguo Sun, Haiyan Liang
Huangshui polysaccharides (HSPs) have attracted extensive attention recently for their biological activity and physicochemical property. This research investigated the extraction, structural characterization, and prebiotic activity of three different HSPs (HSP40-0, HSP60-0, and HSP80-0) in vitro to reveal the scientific support for the high-value utilization of Huangshui. HSPs were heteropolysaccharide with diverse structures and surface morphologies. Comprehensive analysis was conducted through 16S rRNA gene sequencing and metabolite profiling techniques, and results showed that HSPs had different potentials to regulate the gut microbiota due to their different structures; for instance, both HSP40-0 and HSP80-0 could notably increase the relative abundance of Bacteroidota, whereas HSP60-0 could increase the relative abundance of Phascolarctobacterium ...
February 20, 2024: Journal of Agricultural and Food Chemistry
https://read.qxmd.com/read/38339390/the-interplay-between-heat-shock-proteins-and-cancer-pathogenesis-a-novel-strategy-for-cancer-therapeutics
#17
REVIEW
Prathap Somu, Sonali Mohanty, Nagaraj Basavegowda, Akhilesh Kumar Yadav, Subhankar Paul, Kwang-Hyun Baek
Heat shock proteins (HSPs) are developmentally conserved families of protein found in both prokaryotic and eukaryotic organisms. HSPs are engaged in a diverse range of physiological processes, including molecular chaperone activity to assist the initial protein folding or promote the unfolding and refolding of misfolded intermediates to acquire the normal or native conformation and its translocation and prevent protein aggregation as well as in immunity, apoptosis, and autophagy. These molecular chaperonins are classified into various families according to their molecular size or weight, encompassing small HSPs (e...
February 1, 2024: Cancers
https://read.qxmd.com/read/38310824/molecular-mechanism-of-selenium-against-lead-induced-apoptosis-in-chicken-brainstem-relating-to-heat-shock-protein-selenoproteins-and-inflammatory-cytokines
#18
JOURNAL ARTICLE
Dechun Chen, Weikang Yu, Zhiyu Hao, Minna Qiu, Jiawen Cui, You Tang, Xiaohua Teng, Yuhao Liu, Haifeng Liu
Extensive application of lead (Pb) brought about environmental pollution and toxic reactions of organisms. Selenium (Se) has the effect of antagonizing Pb poisoning in humans and animals. However, it is still unclear how Pb causes brainstem toxicity. In the present study, we wanted to investigate whether Se can alleviate Pb toxicity in chicken brainstems by reducing apoptosis. One hundred and eighty chickens were randomly divided into four groups, namely the control group, the Se group, the Pb group, and the Se/Pb group...
February 2, 2024: Ecotoxicology and Environmental Safety
https://read.qxmd.com/read/38291012/reactive-metabolite-of-trovafloxacin-activates-inflammasomes-implications-for-trovafloxacin-induced-liver-injury
#19
JOURNAL ARTICLE
Saori Tanaka, Takumi Noda, Kazuya Urashima, Yoshio Ijiri, Yuka Kohda, Ryuji Kato
Trovafloxacin is a quinolone antibiotic drug with broad-spectrum activity, which was withdrawn from a global market relatively soon after approval because of serious liver injury. The characteristics of trovafloxacin-induced liver injury are consistent with an idiosyncratic reaction; however, the details of the mechanism have not been elucidated. We examined whether trovafloxacin induces the release of damage-associated molecular patterns (DAMPs) that activate inflammasomes. We also tested ciprofloxacin, levofloxacin, gatifloxacin, and grepafloxacin for their ability to activate inflammasomes...
January 30, 2024: Journal of Applied Toxicology: JAT
https://read.qxmd.com/read/38255948/heat-shock-proteins-and-breast-cancer
#20
REVIEW
Miao Zhang, Xiaowen Bi
Heat shock proteins (Hsps) are a group of stress-induced proteins involved in protein folding and maturation. Based on their molecular weight, Hsps can be divided into six families: small Hsps, Hsp40, Hsp60, Hsp70, Hsp90, and large Hsps. In the process of breast cancer tumorigenesis, Hsps play a central role in regulating cell reactions and functions including proliferation, metastasis, and apoptosis. Moreover, some of the critical Hsps also regulate the fine balance between the protective and destructive immunological responses within the tumor microenvironment...
January 10, 2024: International Journal of Molecular Sciences
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