Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 20 de 11.145
Filtrar
1.
Bull Exp Biol Med ; 176(4): 477-480, 2024 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-38492099

RESUMO

Adaptor proteins stress induced phosphoprotein 1 (STIP1) and ST13 Hsp70 interacting protein (ST13) may play a crucial role in the pathophysiology of ischemic stroke through controlling protein folding, neuronal survival, and regulation of HSP70/HSP90. The present pilot study investigated whether tagSNPs in genes encoding ST13 (rs138335, rs138344, rs7290793, and rs138344) and STIP1 (rs4980524) are associated with ischemic stroke. DNA samples from 721 ischemic stroke patients and 471 healthy controls were genotyped using the MassArray-4. Our research revealed a relationship between rs138344 ST13 and the risk of ischemic stroke, which was seen only in females (risk allele G; OR=1.34, 95%CI=1.07-1.69; p=0.01). The haplotype rs138335G-rs138344C-rs7290793C ST13 was linked with lower risk of ischemic stroke in females: OR=0.42; 95%CI=0.26-0.68; p=0.0005. Thus, ST13 represents a novel genetic marker for ischemic stroke.


Assuntos
Proteínas de Choque Térmico , AVC Isquêmico , Chaperonas Moleculares , Proteínas Supressoras de Tumor , Feminino , Humanos , Genótipo , Proteínas de Choque Térmico/genética , Proteínas de Choque Térmico HSP70/metabolismo , Chaperonas Moleculares/genética , Projetos Piloto , Polimorfismo Genético , Proteínas Supressoras de Tumor/genética
2.
Genes (Basel) ; 15(3)2024 Feb 25.
Artigo em Inglês | MEDLINE | ID: mdl-38540349

RESUMO

For marine invertebrates, the disruption of organismal physiology and behavior by nanoplastics (NPs) has been extensively reported. Heat shock proteins (Hsps) are important for redundant protein breakdown, environmental changes, and intracellular protein transport. An exhaustive identification of Hsp70 genes and an experiment where different concentrations of NPs were stressed were performed to study how Hsp70 genes respond to NPs stress in Monodonta labio. Our results identified 15 members of Hsp70 within the genome of M. labio and provided insights into their responses to different concentrations of acute NP stress. Phylogenetic analyses revealed extensive amplification of the Hsp70 genes from the Hsc70 subfamily, with gene duplication events. As a result of NP stress, five of fifteen genes showed significant upregulation or downregulation. Three Hsp70 genes were highly expressed at an NP concentration of 0.1 mg/L, and no genes were downregulated. At 10 mg/L, they showed significant upregulation of two genes and significant downregulation of two genes. At 1 mg/L treatment, three genes were significantly downregulated, and no genes were significantly upregulated. Moreover, a purifying selection was revealed using a selection test conducted on duplicate gene pairs, indicating functional redundancy. This work is the first thorough examination of the Hsp70s in Archaeogastropoda. The findings improve knowledge of Hsp70s in molluscan adaptation to NP stress and intertidal living and offer essential data for the biological study of M. labio.


Assuntos
Gastrópodes , Microplásticos , Animais , Filogenia , Proteínas de Choque Térmico HSP70/genética , Proteínas de Choque Térmico HSP70/metabolismo , Proteínas de Choque Térmico/genética , Gastrópodes/genética , Gastrópodes/metabolismo , Perfilação da Expressão Gênica
3.
Poult Sci ; 103(4): 103537, 2024 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-38428202

RESUMO

Over the past years, the poultry industry has been assigned to greater production performance but has become highly sensitive to environmental changes. The average world temperature has recently risen and is predicted to continue rising. In open-sided houses, poultry species confront high outside temperatures, which cause heat stress (HS) problems. Cellular responses are vital in poultry, as they may lead to identifying confirmed HS biomarkers. Heat shock proteins (HSP) are highly preserved protein families that play a significant role in cell function and cytoprotection against various stressors, including HS. The optimal response in which the cell survives the HS elevates HSP levels that prevent cellular proteins from damage caused by HS. The HSP have chaperonic action to ensure that stress-denatured proteins are folded, unfolded, and refolded. The HSP70 and HSP90 are the primary HSP in poultry with a defensive function during HS. HSP70 was the optimal biological marker for assessing HS among the HSP studied. The current review attempts to ascertain the value of HSP as a heat stress defense mechanism in poultry.


Assuntos
Proteínas de Choque Térmico , Aves Domésticas , Animais , Proteínas de Choque Térmico/genética , Proteínas de Choque Térmico/metabolismo , Aves Domésticas/metabolismo , Galinhas/metabolismo , Proteínas de Choque Térmico HSP70 , Resposta ao Choque Térmico/fisiologia , Mecanismos de Defesa
4.
J Therm Biol ; 120: 103824, 2024 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-38428104

RESUMO

This research endeavored to elucidate the transcriptional modulation of heat shock proteins and adipogenic regulators in bovine subcutaneous adipocytes following thermal exposure. Post-differentiation, mature adipocytes were subjected to three treatments of control (CON), moderate (MHS), and extreme (EHS) heat stress. These treatments consist of thermal conditions at temperatures of 38 °C (CON), 39.5 °C (MHS), or 41 °C (EHS) along with of 3 or 12 h. There was no statistically significant variations observed in the gene expressions of HSP27 and HSP70 when comparing CON with MHS across both exposures. Contrastingly, when comparing CON with EHS, an upregulation (P < 0.01) in HSP27 gene expression was evident for both 3 and 12 h of incubation, while HSP70 gene expression exhibited elevation (P < 0.01) at the 3-h mark, with no change observed at 12 h. Protein quantification, however, revealed an elevation (P < 0.01) in HSP27 and HSP70 for both CON vs. MHS and CON vs. EHS at the 12-h exposure. This trend in protein level mirrored (P < 0.05) that of proliferator-activated receptor-gamma (PPARγ). Elevated (P < 0.05) protein levels of fatty acid synthase (FAS) were exclusively discernible in the CON vs. MHS. Increased (P < 0.01) transcriptional activity of PPARγ, CCAAT/enhancer-binding protein alpha (C/EBPα), stearoyl-CoA desaturase (SCD), and FAS was evident in the CON vs. EHS comparison. Complementary to these molecular findings, an augmented lipid droplet accumulation was observed (P < 0.01) in EHS-exposed adipocytes progressively from day 6 through day 9. Our current study highlights how different levels and lengths of heat stress can impact the activity of important heat-related proteins and factors that play a role in fat development in beef cattle. These findings can help guide strategies to manage how beef cattle are exposed to heat, which can affect fat storage and ultimately the quality of the meat's marbling.


Assuntos
Proteínas de Choque Térmico HSP27 , PPAR gama , Bovinos , Animais , PPAR gama/genética , PPAR gama/metabolismo , Proteínas de Choque Térmico HSP27/metabolismo , Adipócitos/metabolismo , Proteínas de Choque Térmico/genética , Proteínas de Choque Térmico/metabolismo , Proteínas de Transporte , Proteínas de Choque Térmico HSP70/metabolismo
5.
J Vis Exp ; (205)2024 Mar 08.
Artigo em Inglês | MEDLINE | ID: mdl-38526131

RESUMO

Heat shock protein 70 (Hsp70) is a conserved protein that facilitates the folding of other proteins within the cell, making it a molecular chaperone. While Hsp70 is not essential for E. coli cells growing under normal conditions, this chaperone becomes indispensable for growth at elevated temperatures. Since Hsp70 is highly conserved, one way to study the chaperone function of Hsp70 genes from various species is to heterologously express them in E. coli strains that are either deficient in Hsp70 or express a native Hsp70 that is functionally compromised. E. coli dnaK756 cells are unable to support λ bacteriophage DNA. Furthermore, their native Hsp70 (DnaK) exhibits elevated ATPase activity while demonstrating reduced affinity for GrpE (Hsp70 nucleotide exchange factor). As a result, E. coli dnaK756 cells grow adequately at temperatures ranging from 30 °C to 37 °C, but they die at elevated temperatures (>40 °C). For this reason, these cells serve as a model for studying the chaperone activity of Hsp70. Here, we describe a detailed protocol for the application of these cells to conduct a complementation assay, enabling the study of the in cellulo chaperone function of Hsp70.


Assuntos
Proteínas de Escherichia coli , Proteínas de Choque Térmico HSP70 , Proteínas de Choque Térmico HSP70/genética , Proteínas de Choque Térmico HSP70/metabolismo , Escherichia coli/genética , Escherichia coli/metabolismo , Proteínas de Choque Térmico/genética , Proteínas de Escherichia coli/genética , Proteínas de Escherichia coli/metabolismo , Chaperonas Moleculares/metabolismo , Dobramento de Proteína , Proteínas de Bactérias/metabolismo
6.
J Orthop Surg Res ; 19(1): 156, 2024 Mar 01.
Artigo em Inglês | MEDLINE | ID: mdl-38429742

RESUMO

Heat-shock protein beta1 (HSPB1) is a member of the small HSP family, downregulated in osteoarthritis (OA) chondrocytes and demonstrated the capacity to serve as an RNA-binding protein (RBP). This work aimed to explore the profile of HSPB1 bound RNA and reveal the potential regulation mechanism of HSPB1 in OA. In this work, we captured an unbiased HSPB1-RNA interaction map in Hela cells using the iRIP-seq. The results demonstrated that HSPB1 interacted with plentiful of mRNAs and genomic location toward the CDS region. Functional enrichment of HSPB1-related peaks showed the involvement in gene expression, translation initiation, cellular protein metabolic process, and nonsense-mediated decay. HOMER software analysis showed that HSPB1 bound peaks were over-represented in GAGGAG sequences. In addition, ABLIRC and CIMS algorithm indicated that HSPB1 bound to AU-rich motifs and the proportion of AU-rich peaks in 3' UTR were slightly higher than that in other regions. Moreover, HSPB1-binding targets analysis revealed several gens were associated with OA including EGFR, PLEC, COL5A1, and ROR2. The association of OA-related mRNAs to HSPB1 was additionally confirmed in OA tissues by the quantitative RIP-PCR experiments. Further experiment demonstrated the downregulation of HSPB1 in OA tissues. In conclusion, our current study confirmed HSPB1 as an RNA-binding protein and revealed its potential function in the pathological process of OA, providing a reliable insight to further investigate the molecular regulation mechanism of HSPB1 in OA.


Assuntos
Proteínas de Choque Térmico , Osteoartrite , Humanos , Proteínas de Choque Térmico/genética , Células HeLa , Proteínas de Ligação a RNA/genética , Proteínas de Ligação a RNA/metabolismo , RNA Mensageiro/genética , RNA Mensageiro/metabolismo , Regiões 3' não Traduzidas/genética , Osteoartrite/metabolismo , Chaperonas Moleculares/genética
7.
Naturwissenschaften ; 111(2): 16, 2024 Mar 14.
Artigo em Inglês | MEDLINE | ID: mdl-38483597

RESUMO

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. Based on phylogenetic inferences, we compared the sequences of HSP9, HSP12, HSP30, HSP40, HSP70, HSP90, and HSP110 to elucidate the evolutionary relationships of different fungal organisms to suggest evolutionary patterns employing the maximum likelihood method. By the different reconstructions, our inference supports the hypothesis that these classes of proteins are associated with pathogenic gains against endothermic hosts, as well as adaptations for phytopathogenic fungi.


Assuntos
Proteínas de Choque Térmico , Chaperonas Moleculares , Proteínas de Choque Térmico/genética , Proteínas de Choque Térmico/química , Proteínas de Choque Térmico/metabolismo , Filogenia , Sequência de Aminoácidos , Chaperonas Moleculares/metabolismo , Proteínas de Choque Térmico HSP70/genética , Proteínas de Choque Térmico HSP70/metabolismo
8.
Microbiol Res ; 282: 127626, 2024 May.
Artigo em Inglês | MEDLINE | ID: mdl-38330817

RESUMO

Bloodstream infection (BSI) refers to the infection of blood by pathogens. Severe immune response to BSI can lead to sepsis, a systemic infection leading to multiple organ dysfunction, coupled with drug resistance, mortality, and limited clinical treatment options. This work aims to further investigate the new interplay between bacterial exocrine regulatory protein and host immune cells in the context of highly drug-resistant malignant BSI. Whether interfering with related regulatory signaling pathways can reverse the inflammatory disorder of immune cells. In-depth analysis of single-cell sequencing results in Septic patients for potential immunodeficiency factors. Analysis of key proteins enriched by host cells and key pathways using proteomics. Cell models and animal models validate the pathological effects of DnaK on T cells, MAITs, macrophages, and osteoclasts. The blood of patients was analyzed for the immunosuppression of T cells and MAITs. We identified that S. maltophilia-DnaK was enriched in immunodeficient T cells. The activation of the JAK2/STAT1 axis initiated the exhaustion of T cells. Septic patients with Gram-negative bacterial infections exhibited deficiencies in MAITs, which correspond to IFN-γ. Cellular and animal experiments confirmed that DnaK could facilitate MAIT depletion and M1 polarization of macrophages. Additionally, Fludarabine mitigated M1 polarization of blood, liver, and spleen in mice. Interestingly, DnaK also repressed osteoclastogenesis of macrophages stimulated by RANKL. S.maltophilia-DnaK prompts the activation of the JAK2/STAT1 axis in T cells and the M1 polarization of macrophages. Targeting the DnaK's crosstalk can be a potentially effective approach for treating the inflammatory disorder in the broad-spectrum drug-resistant BSI.


Assuntos
Anti-Infecciosos , Sepse , Humanos , Animais , Camundongos , Proteínas de Choque Térmico/genética , Proteínas de Choque Térmico/metabolismo , Macrófagos , Fígado , Anti-Infecciosos/metabolismo , Proteínas de Bactérias/metabolismo , Linfócitos T/metabolismo , Fator de Transcrição STAT1/metabolismo , Janus Quinase 2/metabolismo
9.
JCI Insight ; 9(7)2024 Apr 08.
Artigo em Inglês | MEDLINE | ID: mdl-38421727

RESUMO

Myocardial ischemia/reperfusion (MI/R) injury is a major cause of adverse outcomes of revascularization following myocardial infarction. Anaerobic glycolysis during myocardial ischemia is well studied, but the role of aerobic glycolysis during the early phase of reperfusion is incompletely understood. Lactylation of Histone H3 (H3) is an epigenetic indicator of the glycolytic switch. Heat shock protein A12A (HSPA12A) is an atypic member of the HSP70 family. In the present study, we report that, during reperfusion following myocardial ischemia, HSPA12A was downregulated and aerobic glycolytic flux was decreased in cardiomyocytes. Notably, HSPA12A KO in mice exacerbated MI/R-induced aerobic glycolysis decrease, cardiomyocyte death, and cardiac dysfunction. Gain- and loss-of-function studies demonstrated that HSPA12A was required to support cardiomyocyte survival upon hypoxia/reoxygenation (H/R) challenge and that its protective effects were mediated by maintaining aerobic glycolytic homeostasis for H3 lactylation. Further analyses revealed that HSPA12A increased Smurf1-mediated Hif1α protein stability, thus increasing glycolytic gene expression to maintain appropriate aerobic glycolytic activity to sustain H3 lactylation during reperfusion and, ultimately, improving cardiomyocyte survival to attenuate MI/R injury.


Assuntos
Infarto do Miocárdio , Isquemia Miocárdica , Traumatismo por Reperfusão Miocárdica , Animais , Camundongos , Proteínas de Choque Térmico/genética , Proteínas de Choque Térmico/metabolismo , Infarto do Miocárdio/metabolismo , Isquemia Miocárdica/metabolismo , Traumatismo por Reperfusão Miocárdica/genética , Traumatismo por Reperfusão Miocárdica/metabolismo , Miócitos Cardíacos/metabolismo
10.
FEBS Lett ; 598(6): 635-657, 2024 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-38366111

RESUMO

The response to proteotoxic stresses such as heat shock allows organisms to maintain protein homeostasis under changing environmental conditions. We asked what happens if an organism can no longer react to cytosolic proteotoxic stress. To test this, we deleted or depleted, either individually or in combination, the stress-responsive transcription factors Msn2, Msn4, and Hsf1 in Saccharomyces cerevisiae. Our study reveals a combination of survival strategies, which together protect essential proteins. Msn2 and 4 broadly reprogram transcription, triggering the response to oxidative stress, as well as biosynthesis of the protective sugar trehalose and glycolytic enzymes, while Hsf1 mainly induces the synthesis of molecular chaperones and reverses the transcriptional response upon prolonged mild heat stress (adaptation).


Assuntos
Proteínas de Saccharomyces cerevisiae , Fatores de Transcrição , Proteínas de Ligação a DNA/genética , Proteínas de Ligação a DNA/metabolismo , Fatores de Transcrição de Choque Térmico/genética , Fatores de Transcrição de Choque Térmico/metabolismo , Proteínas de Choque Térmico/genética , Proteínas de Choque Térmico/metabolismo , Resposta ao Choque Térmico/genética , Estresse Proteotóxico , Saccharomyces cerevisiae/metabolismo , Proteínas de Saccharomyces cerevisiae/metabolismo , Fatores de Transcrição/metabolismo
11.
Aging (Albany NY) ; 16(3): 2517-2541, 2024 Jan 31.
Artigo em Inglês | MEDLINE | ID: mdl-38305786

RESUMO

With the global rise in cancer incidence and mortality rates, research on the topic has become increasingly urgent. Among the significant players in this field are heat shock proteins (HSPs), particularly HSPA4 from the HSP70 subfamily, which has recently garnered considerable interest for its role in cancer progression. However, despite numerous studies on HSPA4 in specific cancer types, a comprehensive analysis across all cancer types is lacking. This study employs various bioinformatics techniques to delve into the role of HSPA4 in pan-cancer. Our objective is to assess its potential in clinical diagnosis, prognosis, and as a future molecular target for therapy. The research findings reveal significant differences in HSPA4 expression across different cancer types, suggesting its diagnostic value and close association with cancer staging and patient survival rates. Furthermore, genetic variations and methylation status of HSPA4 play critical roles in tumorigenesis. Lastly, the interaction of HSPA4 with immune cells is linked to the tumor microenvironment (TME) and immunotherapy. In summary, HSPA4 emerges as a promising cancer biomarker and a vital member of the HSPs family, holding potential applications in diagnosis, prognosis, and immunotherapy.


Assuntos
Proteínas de Choque Térmico HSP110 , Neoplasias , Humanos , Proteínas de Choque Térmico HSP110/genética , Proteínas de Choque Térmico HSP110/metabolismo , Prognóstico , Neoplasias/diagnóstico , Neoplasias/genética , Neoplasias/terapia , Proteínas de Choque Térmico HSP70/genética , Proteínas de Choque Térmico/genética , Imunoterapia , Microambiente Tumoral/genética
12.
Mar Genomics ; 73: 101085, 2024 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-38301367

RESUMO

We present a de novo transcriptome assembly for the non-model Antarctic polychaete worm Microspio moorei (Spionidae) collected during Antarctic field expedition in Fildes Bay, King George Island, Antarctic Peninsula, in 2017. Here, we report the first transcriptome reference array for Microspio spp. The gene sequences of the spionid worm were annotated from a wide range of functions (i.e., biological, and metabolic processes, catalytic processes, and catalytic activity). HSP70, HSP90 SOD and CAT families were compared to reported annelid transcriptomes and proteomes. The phylogenetic analysis using COI, 16S, and 18S markers effectively clusters the species within the family. However, it also casts uncertainty on the monophyletic nature of the Microspio genera, indicating the necessity for additional data and potentially requiring a reevaluation of its grouping. Within these protein families, 3D model software was used to create one representative of their protein structures. Structural predictions were compared with related reported annelids living at different temperatures and a human X-ray reference. We found structural differences (RMSE >1.8) between the human HSP proteins but no significant differences between the polychaete-predicted proteins (RMSE <1.2). These results encourage further research of heat stress-related proteins, the development of genetic markers for climate change-induced temperature stress, and the study of the underlying mechanisms of the heat response. Moreover, these results motivate the extension of these findings to congeneric species.


Assuntos
Proteínas de Choque Térmico , Transcriptoma , Humanos , Proteínas de Choque Térmico/genética , Filogenia , Regiões Antárticas , Resposta ao Choque Térmico , Superóxido Dismutase/genética
13.
Ecotoxicol Environ Saf ; 272: 116028, 2024 Mar 01.
Artigo em Inglês | MEDLINE | ID: mdl-38310824

RESUMO

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. Morphological examination, ultrastructural observation, relative mRNA expressions of genes on heat shock proteins (HSPs); selenoproteins; inflammatory cytokines; and apoptosis-related factors were investigated. The results showed that Pb exposure led to tissue damage and apoptosis in chicken brainstems. Furthermore, an atypical expression of HSPs (HSP27, HSP40, HSP60, HSP70, and HSP90); selenoprotein family glutathione peroxidase (GPx) 1, GPx2, GPx3, and GPx4), thioredoxin reductases (Txnrd) (Txnrd1, Txnrd2, and Txnrd3), dio selenoprotein famliy (diodothyronine deiodinases (Dio)1, Dio2, and Dio3), as well as other selenoproteins (selenoprotein (Sel)T, SelK, SelS, SelH, SelM, SelU, SelI, SelO, Selpb, selenoprotein n1 (Sepn1), Sepp1, Sepx1, Sepw1, 15-kDa selenoprotein (Sep15), and selenophosphate synthetases 2 (SPS2)); inflammatory cytokines (Interleukin 2 (IL-2), IL-4, IL-6, IL-12ß, IL-17, and Interferon-γ (IFN-γ)); and apoptosis-related genes (B-cell lymphoma-2 (Bcl-2), tumor protein 53 (p53), Bcl-2 Associated X (Bax), Cytochrome c (Cyt c), and Caspase-3) were identified. An inflammatory reaction and apoptosis were induced in chicken brainstems after exposure to Pb. Se alleviated the abnormal expression of HSPs, selenoproteins, inflammatory cytokines, and apoptosis in brainstem tissues of chickens treated with Pb. The results indicated that HSPs, selenoproteins, inflammatory, and apoptosis were involved in Se-resisted Pb poisoning. Overall, Se had resistance effect against Pb poisoning, and can be act as an antidote for Pb poisoning in animals.


Assuntos
Selênio , Humanos , Animais , Selênio/farmacologia , Galinhas/metabolismo , Citocinas/genética , Chumbo , Selenoproteínas/genética , Selenoproteínas/metabolismo , Proteínas de Choque Térmico/genética , Proteínas Proto-Oncogênicas c-bcl-2
14.
Int J Hyperthermia ; 41(1): 2290913, 2024.
Artigo em Inglês | MEDLINE | ID: mdl-38191150

RESUMO

Some heat shock proteins (HSPs) have been shown to influence tumor prognosis, but their prognostic significance in colorectal cancer (CRC) remains unclear. This study explored the prognostic significance of HSP-related genes in CRC. Transcriptional data and clinical information of CRC patients were obtained from The Cancer Genome Atlas (TCGA) database, and a literature search was conducted to identify HSP-related genes. Using Least Absolute Selection and Shrinkage Operator (LASSO) regression and univariate/multivariate Cox regression analyses, 12 HSP-related genes demonstrating significant associations with CRC survival were successfully identified and employed to formulate a predictive risk score model. The efficacy and precision of this model were validated utilizing TCGA and Gene Expression Omnibus (GEO) datasets, demonstrating its reliability in CRC prognosis prediction. gene ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analyses revealed significant disparities between high- and low-risk groups in chromatin remodeling biological functions and neutrophil extracellular trap formation pathways. Single sample gene set enrichment analysis (ssGSEA) further revealed differences in immune cell types and immune functional status between the two risk groups. Differential analysis showed higher expression of immune checkpoints within the low-risk group, while the high-risk group exhibited notably higher Tumor Immune Dysfunction and Exclusion (TIDE) scores. Additionally, we predicted the sensitivity of different prognosis risk patients to various drugs, providing potential drug choices for tailored treatment. Combined, our study successfully crafted a novel CRC prognostic model that can effectively predict patient survival, immune landscape, and treatment response, providing important support and guidance for CRC patient prognosis.


Assuntos
Neoplasias Colorretais , Proteínas de Choque Térmico , Humanos , Prognóstico , Reprodutibilidade dos Testes , Proteínas de Choque Térmico/genética , Análise Multivariada , Neoplasias Colorretais/genética
15.
BMC Plant Biol ; 24(1): 5, 2024 Jan 02.
Artigo em Inglês | MEDLINE | ID: mdl-38163899

RESUMO

Yellow Camellia (Camellia sect. chrysantha) is a rare ornamental plant and an important germplasm resource globally. Camellia nitidissima thrives in normal acidic soils, while Camellia limonia can adapt to the calcareous soils found in karst areas. Our previous study on the karst adaptation of yellow camellias revealed that the expression levels of heat shock protein 20(HSP20) were higher in Camellia limonia than in Camellia nitidissima. However, the functions of the HSP20 gene of Camellia limonia remain unclear to data. In this study, the HSP20 genes of Camellia limonia (ClHSP20-OE lines) and Camellia. nitidissima (CnHSP20-OE lines) were cloned and overexpressed heterologously in Arabidopsis thaliana. Additionally, we overexpressed the HSP20 gene of Arabidopsis (AtHSP20-OE lines) was also overexpressed, and the T-DNA inserted mutants (athspmutant lines) were also used to determine the functions of HSP20 genes. Under high calcium stress, the chlorophyll, nitrogen, water content and humidity of leaves were increased in ClHSP20-OE lines, while those of other lines were declined. The size of the stomatal apertures, stomatal conductance, and the photosynthetic efficiency of ClHSP20-OE lines were higher than those of the other lines. However, the accumulation of H2O2 and O2- in the leaves of ClHSP20-OE lines was the lowest among all the lines. Energy spectrum scanning revealed that the percentage of calcium on the surfaces of the leaves of ClHSP20-OE lines was relatively low, while that of athspmutant lines was the highest. The ClHSP20 gene can also affected soil humidity and the contents of soil nitrogen, phosphorus, and potassium. Transcriptome analysis revealed that the expressions of FBA5 and AT5G10770 in ClHSP20-OE lines was significantly up-regulated compared to that of CnHSP20-OE lines. Compared to that of athspmutant lines, the expressions of DREB1A and AT3G30460 was significantly upregulated in AtHSP20-OE lines, and the expression of POL was down-regulated. Our findings suggest that the HSP20 gene plays a crucial role in maintained photosynthetic rate and normal metabolism by regulating the expression of key genes under high-calcium stress. This study elucidates the mechanisms underlying the karst adaptation in Camellia. limonia and provides novel insights for future research on karst plants.


Assuntos
Arabidopsis , Camellia , Camellia/genética , Arabidopsis/genética , Cálcio , Proteínas de Choque Térmico/genética , Peróxido de Hidrogênio , Nitrogênio , Solo , Regulação da Expressão Gênica de Plantas
16.
Int J Mol Sci ; 25(2)2024 Jan 19.
Artigo em Inglês | MEDLINE | ID: mdl-38279240

RESUMO

In this study, we examined the effects of rumen-protected L-tryptophan supplementation on the productivity and physiological metabolic indicators in lactating Holstein cows under heat stress conditions. The study involved eight early lactating Holstein cows (days in milk = 40 ± 9 days; milk yield 30 ± 1.5 kg/day; parity 1.09 ± 0.05, p < 0.05), four cows per experiment, with environmentally controlled chambers. In each experiment, two distinct heat stress conditions were created: a low-temperature and low-humidity (LTLH) condition at 25 °C with 35-50% humidity and a high-temperature and high-humidity (HTHH) condition at 31 °C with 80-95% humidity. During the adaptation phase, the cows were subjected to LTLH and HTHH conditions for 3 days. This was followed by a 4-day heat stress phase and then by a 7-day phase of heat stress, which were complemented by supplementation with rumen-protected L-tryptophan (ACT). The findings revealed that supplementation with ACT increased dry matter intake as well as milk yield and protein and decreased water intake, heart rate, and rectal temperature in the HTHH group (p < 0.05). For plateletcrit (PCT, p = 0.0600), the eosinophil percentage (EOS, p = 0.0880) showed a tendency to be lower, while the monocyte (MONO) and large unstained cells (LUC) amounts were increased in both groups (p < 0.05). Albumin and glucose levels were lower in the HTHH group (p < 0.05). The gene expressions of heat shock proteins 70 and 90 in the peripheral blood mononuclear cells were higher in the ACT group (HTHH, p < 0.05). These results suggest that ACT supplementation improved productivity, physiological indicators, blood characteristics, and gene expression in the peripheral blood mononuclear cells of early lactating Holstein cows under heat-stress conditions. In particular, ACT supplementation objectively relieved stress in these animals, suggesting that L-tryptophan has potential as a viable solution for combating heat-stress-induced effects on the cattle in dairy farming.


Assuntos
Proteínas de Choque Térmico , Lactação , Gravidez , Feminino , Bovinos , Animais , Proteínas de Choque Térmico/genética , Proteínas de Choque Térmico/metabolismo , Dieta/veterinária , Triptofano/farmacologia , Triptofano/metabolismo , Rúmen , Leucócitos Mononucleares , Leite/metabolismo , Resposta ao Choque Térmico/fisiologia , Suplementos Nutricionais , Expressão Gênica , Temperatura Alta
17.
J Therm Biol ; 119: 103791, 2024 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-38281316

RESUMO

The growing interest in countering the adverse effects of heat stress in poultry using phytogenic feed additives has garnered considerable attention in recent times, this research sought to examine the impact of rosemary leaves extract (RLE) and oregano leaves extract (OLE) on the growth performance, physiological responses, and hepatic mRNA expression of heat shock proteins in broiler chickens exposed to heat stress. A total of 150 male Indian River chicks, aged one day, were randomly allocated into five equally sized groups, each consisting of six replicates. The initial group was designated as the control and was provided with the basal diet. The second and third groups (R1 and R2) were administered the basal diet enriched with 50 and 100 mg/kg of rosemary leaves extract (RLE), respectively. The fourth and fifth groups (O1 and O2) were fed the basal diet supplemented with 50 and 100 mg/kg of oregano leaves extract (OLE), respectively. These chicks were reared in a controlled environmental chamber maintained at a temperature of 32±2 °C and relative humidity of 50 ± 5 %. Ferruginol was the leading component in RLE, whereas thymol was the prevalent constituent in OLE. RLE and OLE both have high DPPH• and ABTS•+ antioxidant potential. Among the experimental groups, the fourth group (O1) showed the heaviest live body weight and the lowest feed conversion ratio, indicating improved growth performance. There was a significant reduction in plasma total lipids and LDL-cholesterol levels within the R2 and O2 groups, respectively. Enhanced total antioxidant capacity and an improvement in the T3 hormone were observed in the R1 and R2 groups. In the second and fourth groups, the mRNA expression of hsp70 and 90A were both found to be significantly downregulated, respectively. In conclusion, the addition of 50 mg/kg of oregano leaves extract (OLE) to the diets of heat-stressed broilers resulted in improved hepatic heat shock proteins, along with certain physiological responses, ultimately contributing to enhanced growth performance.


Assuntos
Origanum , Rosmarinus , Animais , Masculino , Ração Animal/análise , Antioxidantes/metabolismo , Galinhas/fisiologia , Dieta/veterinária , Suplementos Nutricionais , Proteínas de Choque Térmico/genética , Proteínas de Choque Térmico/metabolismo , Resposta ao Choque Térmico , RNA Mensageiro/metabolismo
18.
Artigo em Inglês | MEDLINE | ID: mdl-38224831

RESUMO

Salinity and temperature influence growth, survival, and reproduction of crustacean species such as Penaeus vannamei where Na +/K+-ATPase plays a key role in maintaining osmotic homeostasis in different salinity conditions. This ability is suggested to be mediated by other proteins including neuropeptides such as the crustacean hyperglycemic hormones (CHHs), and heat shock proteins (HSPs). The mRNA expression of Na+/K+-ATPase, HSP60, HSP70, CHH-A, and CHH-B1, was analyzed by qPCR in shrimp acclimated to different salinities (10, 26, and 40 PSU) and temperature conditions (20, 23, 26, 29, and 32 °C) to evaluate their uses as molecular stress biomarkers. The results showed that the hemolymph osmoregulatory capacity in shrimp changed with exposure to the different salinities. From 26 to 32 °C the Na+/K+-ATPase expression increased significantly at 10 PSU relative to shrimp acclimated at 26 PSU and at 20 °C increased at similar values independently of salinity. The highest HSP expression levels were obtained by HSP70 at 20 °C, suggesting a role in protecting proteins such as Na+/K+ -ATPase under low-temperature and salinity conditions. CHH-A was not expressed in the gill under any condition, but CHH-B1 showed the highest expression at the lowest temperatures and salinities, suggesting its participation in the Na+/K+-ATPase induction. Since Na+/K+-ATPase, HSPs, and CHHs seem to participate in maintaining the osmo-ionic balance and homeostasis in P. vannamei, their expression levels may be used as a stress biomarkers to monitor marine crustacean health status when acclimated in low salinity and temperature conditions.


Assuntos
Penaeidae , Animais , Penaeidae/metabolismo , Salinidade , Adenosina Trifosfatases/metabolismo , Temperatura , Proteínas de Choque Térmico/genética , Proteínas de Choque Térmico/metabolismo , ATPase Trocadora de Sódio-Potássio/genética , ATPase Trocadora de Sódio-Potássio/metabolismo , Brânquias/metabolismo
19.
Future Oncol ; 20(1): 17-23, 2024 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-38189148

RESUMO

Background: Heat shock proteins (HSP) protect cancer cells. Gastrointestinal bacteria contain HSP genes and can release extracellular vesicles which act as biological shuttles. Stress from treatment may result in a microbial community with more HSP genes, which could contribute to circulating HSP levels. Methods: The authors examined the abundance of five bacterial HSP genes pre-treatment and during induction in stool sequences from 30 pediatric acute lymphoblastic leukemia patients. Results: Decreased mean HTPG counts (p = 0.0024) pre-treatment versus induction were observed. During induction, HTPG, Shannon diversity and Bacteroidetes decreased (p = 7.5e-4; 1.1e-3; 8.6e-4), while DNAK and Firmicutes increased (p = 6.9e-3; 9.2e-4). Conclusion: Understanding microbial HSP gene community changes with treatment is the first step in determining if bacterial HSPs are important to the tumor microenvironment and leukemia treatment.


Assuntos
Proteínas de Choque Térmico , Leucemia-Linfoma Linfoblástico de Células Precursoras , Humanos , Criança , Proteínas de Choque Térmico/genética , Proteínas de Choque Térmico/metabolismo , Quimioterapia de Indução , Leucemia-Linfoma Linfoblástico de Células Precursoras/tratamento farmacológico , Leucemia-Linfoma Linfoblástico de Células Precursoras/genética , Proteínas de Choque Térmico HSP70/genética , Proteínas de Choque Térmico HSP70/metabolismo , Proteínas de Choque Térmico HSP90/genética , Proteínas de Choque Térmico HSP90/metabolismo , Microambiente Tumoral
20.
Int J Biol Macromol ; 256(Pt 1): 128379, 2024 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-38000583

RESUMO

Extreme changes in weather including heat-wave and high-temperature fluctuations are predicted to increase in intensity and duration due to climate change. Wheat being a major staple crop is under severe threat of heat stress especially during the grain-filling stage. Widespread food insecurity underscores the critical need to comprehend crop responses to forthcoming climatic shifts, pivotal for devising adaptive strategies ensuring sustainable crop productivity. This review addresses insights concerning antioxidant, physiological, molecular impacts, tolerance mechanisms, and nanotechnology-based strategies and how wheat copes with heat stress at the reproductive stage. In this study stress resilience strategies were documented for sustainable grain production under heat stress at reproductive stage. Additionally, the mechanisms of heat resilience including gene expression, nanomaterials that trigger transcription factors, (HSPs) during stress, and physiological and antioxidant traits were explored. The most reliable method to improve plant resilience to heat stress must include nano-biotechnology-based strategies, such as the adoption of nano-fertilizers in climate-smart practices and the use of advanced molecular approaches. Notably, the novel resistance genes through advanced molecular approach and nanomaterials exhibit promise for incorporation into wheat cultivars, conferring resilience against imminent adverse environmental conditions. This review will help scientific communities in thermo-tolerance wheat cultivars and new emerging strategies to mitigate the deleterious impact of heat stress.


Assuntos
Proteínas de Choque Térmico , Triticum , Proteínas de Choque Térmico/genética , Triticum/genética , Mudança Climática , Antioxidantes , Resposta ao Choque Térmico , Grão Comestível/genética
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...