Search Results (44)

Phoebe bournei, a rare tree species native to China, holds considerable economic importance. The heat shock protein 70 (Hsp70) family is a group of molecular chaperones that is broadly distributed across living organisms and play a critical role in processes like growth, development, and stress response. While Hsp70 genes have been identified and studied in various plant species, their specific functions in the growth and development of P. bournei remain unexplored. We performed a comprehensive analysis of the Hsp70 gene family in P. bournei, identifying a total of 45 Hsp70 genes, which were classified into four groups (I–IV) through phylogenetic analysis. All Hsp70 proteins possessed conserved structural domains, including motif 7, and introns were present in 77.8% of the genes. Chromosomal localization and collinearity analyses of the Hsp70 genes revealed their evolutionary relationships and potential gene duplication events. Examination of the cis-acting elements within the Hsp70 promoter regions revealed that the predominant elements were associated with growth and development, followed by those responsive to hormones, and then elements linked to abiotic stress. Nine genes with high expression were selected for RT-qPCR analysis. Under high-temperature stress, all nine genes were differentially upregulated, and most of these genes belonged to subfamilies II and III, indicating that these two subfamilies have strong potential for heat resistance. In this study, we have elucidated the molecular characteristics and heat response properties of the Hsp70 gene family in P. bournei, revealing the mechanisms behind its heat stress response. Our work provides a reference for stress breeding in P. bournei and a theoretical basis for the exploration of heat tolerance in woody plants. Full article

In previous studies, we isolated a series of novel gentisides with nerve growth factor (NGF)-mimic activities from Gentiana rigescens Franch and conducted continuous structure–activity relationship (SAR) studies. Recently, a lead compound named TBG096 was discovered with significant NGF-mimic activity, low toxicity, and ability to pass through the blood–brain barrier (BBB). At the cell level, TBG096 exerts NGF-mimic activity by regulation of heat-shock cognate protein 70 (Hsc70) and downstream proteins. Subsequently, high-fat diet (HFD)-induced Alzheimer disease (AD) mouse models were used to evaluate the anti-AD efficacy of the compound. TBG096 significantly improved the memory dysfunction of AD mice at doses of 0.1, 5, and 20 mg/kg, respectively. In order to elucidate the mechanism of action of the compound against AD, the RNA-sequence analysis of transcriptomics, quantitative real-time polymerase chain reaction (qRT-PCR), immunofluorescence staining, and Western blot analysis were performed using animal samples. TBG096 significantly increased the expression of the Wnt gene family (Wnt10b, Wnt5a, and Wnt1) and the number of mature neurons and newborn neurons in the hippocampus and cerebral cortex of AD mice, respectively. At the same time, it reduced the activity of microglia, astrocyte cells, and expression of inducible nitric oxide synthase (INOS) in the brain. Moreover, this compound significantly increased phosphorylated-adenosine 5′-monophosphate-activated protein kinase (AMPK), Hsc70, and lysosomal-associated membrane protein 2a (LAMP2A) and decreased the expression of hexokinase 2 (HK2), pyruvate kinase M2 (PKM2), amyloid precursor protein (APP), microtubule-associated protein tau (Tau), phosphoryl-Tau, and β-amyloid (Aβ) at the protein level. These results suggest that TBG096 produced the NGF-mimic activity and the anti-AD effect via promoting neurogenesis and modification of the Hsc70/HK2/PKM2/LAMP2A signaling pathway, proposing a potential novel approach to counteracting cognitive decline by developing small molecules that promote neurogenesis and the Hsc70 signaling pathway. Full article

Type 2 diabetes (T2D) is a chronic disease that damages blood vessels and increases the risk of cardiovascular disease (CVD). Heat-shock protein 70 (HSP70), a family of chaperone proteins, has been recently reported as a key player in vascular reactivity that affects large blood vessels like the aorta. Hyperglycemia, a hallmark of diabetes, correlates with the severity of vascular damage and circulating HSP70 levels. In diabetes, blood vessels often show impaired contractility, contributing to vascular dysfunction. However, HSP70’s specific role in T2D-related vascular contraction remains unclear. We hypothesized that blocking HSP70 would improve vascular function in a widely used diabetic mouse model (db/db). To test this, we measured both vascular intracellular and serum circulating HSP70 levels in control and diabetic male mice using immunofluorescence and Western blotting. We also examined the aorta’s contractile response using a wire myograph system, which measured the force produced in response to phenylephrine (PE), both with and without VER155008, a pharmacological inhibitor that targets the ATPase domain of HSP70, and after removing extracellular calcium. Our findings show that intracellular HSP70 (iHSP70) levels were similar in control and diabetic groups, while circulating HSP70 (eHSP70) levels were higher in the serum of diabetic mice, altering the iHSP70/eHSP70 ratio. Even though VER155008 attenuated both phases of the contractile curve in the diabetic and control groups, enhanced vasoconstriction to PE was only observed in the tonic phase of the curve in the db/db group, which was prevented by iHSP70 inhibition. This effect involved calcium mobilization, as both the maximal and total contraction forces to PE were restored in groups treated with VER155008. Additionally, internal calcium levels in aortic rings treated with VER155008 decreased, as observed in force generation upon calcium reintroduction, which was further corroborated using a biochemical calcium assay. In conclusion, our study demonstrates that blocking HSP70 improves vascular reactivity in the hyperglycemic state of T2D by restoring proper vascular contraction. Full article

Clock genes regulate physiological and metabolic processes by responding to changes in environmental light and temperature, and genetic variations in these genes may facilitate environmental adaptation, offering opportunities for resilience to climate change. However, the genetic and molecular mechanisms remain unclear in marine organisms. In this study, we investigated the role of a key clock gene, the circadian locomotor output cycles kaput (Clock), in thermal adaptation using DNA affinity purification sequencing (DAP-Seq) and RNA interference (RNAi)-based transcriptome analysis. In cold-adapted Crassostrea gigas and warm-adapted Crassostrea angulata, Clock was subject to environmental selection and exhibited contrasting expression patterns. The transcriptome analysis revealed 2054 differentially expressed genes (DEGs) following the knockdown of the Clock expression, while DAP-Seq identified 150,807 genes regulated by Clock, including 5273 genes located in promoter regions. The combined analyses identified 201 overlapping genes between the two datasets, of which 98 were annotated in public databases. These 98 genes displayed distinct expression patterns in C. gigas and C. angulata under heat stress, which were potentially regulated by Clock, indicating its role in a molecular regulatory network that responds to heat stress. Notably, a heat-shock protein 70 family gene (Hsp12b) and a tripartite motif-containing protein (Trim3) were significantly upregulated in C. angulata but showed no significant changes in C. gigas, further highlighting their critical roles in thermal adaptation. This study preliminarily constructs a thermal regulatory network involving Clock, providing insights into the molecular mechanisms of clock genes in thermal adaptation. Full article

The heat shock protein 70 (HSP70) family plays an important role in the growth and development of lettuce and in the defense response to high-temperature stress; however, its bioinformatics analysis in lettuce has been extremely limited. Genome-wide bioinformatics analysis methods such as chromosome location, phylogenetic relationships, gene structure, collinearity analysis, and promoter analysis were performed in the LsHSP70 gene family, and the expression patterns in response to high-temperature stress were analyzed. The mechanism of LsHSP70-19 in heat resistance in lettuce was studied by virus-induced gene silencing (VIGS) and transient overexpression techniques. The results showed that a total of 37 LsHSP70 genes were identified by the Hidden Markov Model (HMM) and Protein Family Database (Pfam). These 37 LsHSP70 genes were classified into groups A, B, C, and D by phylogenetic relationships. They were mainly localized on seven chromosomes except for chromosome 3; gene structure analysis showed that LsHSP70 contained 1–9 exons, and the protein structure domains of genes in the same group were highly conserved. The covariance analysis showed that nine pairs of LsHSP70 genes existed between LsHSP70 members, and lettuce LsHSP70 and sunflower HaHSP70 had been more conserved in the evolutionary process. The promoter analysis showed that there were a large number of cis-acting elements related to phytohormones, growth, development, stress, and light response in LsHSP70. In addition, the results of the expression pattern analysis for all LsHSP70 genes under high-temperature stress showed that 28 out of 37 LsHSP70 genes were able to respond to heat stress, and only LsHSP70-8, LsHSP70-14, LsHSP70-19, LsHSP70-23, and LsHSP70-24 were able to respond rapidly to heat stress (2 h). The expression of LsHSP70-19 was higher at different periods under high-temperature stress; the overexpression of LsHSP70-19, the plant fresh weight, and the root weight were better than the control (CK); and the heat resistance was better. These results suggest that LsHSP70-19 may play an important role under high-temperature stress in lettuce. Full article

Pineapple (Ananas comosus (L.) Merr.) is an economically significant and delicious tropical fruit. Pineapple commercial production faces severe decline due to abiotic stresses, which affect the development and quality of pineapple fruit. Heat shock protein 70 (HSP70) plays an essential role in abiotic stress tolerance. However, the pineapple HSP70 family identification and expression analysis in response to abiotic stresses has not been studied. To explore the functional role of AcHSP70, different abiotic stress treatments were applied to pineapple cultivar “Bali” seedlings. A total of 21 AcHSP70 members were identified in the pineapple genome. The identified genes were classified into four subfamilies (I–IV) using phylogenetic analysis. The AcHSP70 family is expressed under different stress conditions. Quantitative real time polymerase chain reaction (qRT-PCR) revealed the expression pattern of the AcHSP70 family under cold, drought, salt, and heat stress. The expression level of genes such as AcHSP70-2 increased under heat, cold, and drought stress, while the expression level of genes such as AcHSP70-3 decreased under salt stress. Furthermore, the expression profile of AcHSP70s in different tissues and development stages was analyzed using transcriptome analysis. The HSP70 genes exhibited unique expression patterns in pineapple tissue at different developmental stages. The study therefore provides a list of HSP70 genes with substantial roles in abiotic stress response and valuable information for understanding AcHSP70 functional characteristics during abiotic stress tolerance in pineapple. Full article

Hsp70s, a group of heat shock proteins, are ancient proteins that play a crucial part in maintaining the stability of cells when faced with various internal and external stresses. In this research, there are 72 CsHSP70 genes present and verified in Camelina sativa, all of which exhibit a wide range of physicochemical characteristics. Through evolutionary analysis, the Hsp70 family was categorized into five primary groups, and numerous segmental duplications were anticipated among the CsHSP70 genes. The GO enrichment analysis of co-expression network elements revealed a significant association between key signaling terms, such as phosphorelay signal transduction, and MAPK cascade with the function of CsHsp70. An analysis of transcriptome data exposed to cold, drought, salinity, and cadmium stress demonstrated the varied expression profiles of CsHsp70 genes. The expression levels of CsHSP70 genes varied across various organs and stages of development in camelina, although some of them illustrated tissue-specific expression. qRT-PCR analysis further disclosed that CsHsp70-60, -52, and -13 were up-regulated and CsHsp70-03, -58, and -09 showed down-regulation in response to salinity. Furthermore, CsHsp70 genes are categorized as late-responsive elements to salinity stress. Through docking analysis, the current research revealed that CsHsp70 proteins interacted with ABA, BR, and MeJA. Full article

Bovine respiratory syncytial virus (BRSV) is an enveloped RNA virus that utilizes clathrin-mediated endocytosis for cell entry and is a significant pathogen in bovine respiratory disease (BRD). Heat shock protein family A member 4 (HSPA4), a member of the HSP70 family, is known to be involved in the progression of various cancers. However, its role in virus entry has not been previously explored. Through experiments involving Western blot analysis, virus titer, and virus copies analysis, we demonstrated that HSPA4 can regulate BRSV entry and replication. The specific regulation mode is to enhance BRSV entry by promoting clathrin-mediated endocytosis. We used Western blot, virus titer, virus copies analysis, and IFA to demonstrate that HSPA4 can promote clathrin heavy chain protein (CHC) expression and further promote BRSV entry by activating the PI3K–Akt signaling pathway. Furthermore, we observed that HSPA4 boosts the efficiency of clathrin-mediated endocytosis by increasing the ATPase activity of heat shock cognate protein 70 (HSC70), thereby facilitating BRSV entry. Additionally, our investigation into the impact of HSPA4 on the entry of other viruses revealed that HSPA4 can facilitate the entry of a variety of viruses into host cells. Full article

More than four decades ago, the discovery of a companion protein of immunoglobulins in myeloma cells and soon after, of their ability to associate with heavy chains, made the term immunoglobulin binding protein (BiP) emerge, prompting a tremendous amount of effort to understand their versatile cellular functions. BiPs belong to the heat shock protein (Hsp) 70 family and are crucial for protein folding and cellular stress responses. While extensively studied in model organisms such as Chlamydomonas, their roles in dinoflagellates, especially in photosynthetic Symbiodiniaceae, remain largely underexplored. Given the importance of Symbiodiniaceae-cnidarian symbiosis, critical for the sustaining of coral reef ecosystems, understanding the contribution of Hsps to stress resilience is essential; however, most studies have focused on Hsps in general but none on BiPs. Moreover, despite the critical role of light in the physiology of these organisms, research on light effects on BiPs from Symbiodiniaceae has also been limited. This review synthesizes the current knowledge from the literature and sequence data, which reveals a high degree of BiP conservation at the gene, protein, and structural levels in Symbiodiniaceae and other dinoflagellates. Additionally, we show the existence of a potential link between circadian clocks and BiP regulation, which would add another level of regulatory complexity. The evolutionary relationship among dinoflagellates overall suggests conserved functions and regulatory mechanisms, albeit expecting confirmation by experimental validation. Finally, our analysis also highlights the significant knowledge gap and underscores the need for further studies focusing on gene and protein regulation, promoter architecture, and structural conservation of Symbiodiniaceae and dinoglagellate BiPs in general. These will deepen our understanding of the role of BiPs in the Symbiodiniaceae-cnidarian interactions and dinoflagellate physiology. Full article

Hsp40–Hsp70 typically function in concert as molecular chaperones, and their roles in post-infection immune responses are increasingly recognized. However, in the economically important fish species Scophthalmus maximus (turbot), there is still a lack in the systematic identification, interaction models, and binding site analysis of these proteins. Herein, 62 Hsp40 genes and 16 Hsp70 genes were identified in the turbot at a genome-wide level and were unevenly distributed on 22 chromosomes through chromosomal distribution analysis. Phylogenetic and syntenic analysis provided strong evidence in supporting the orthologies and paralogies of these HSPs. Protein–protein interaction and expression analysis was conducted to predict the expression profile after challenging with Aeromonas salmonicida. dnajb1b and hspa1a were found to have a co-expression trend under infection stresses. Molecular docking was performed using Auto-Dock Tool and PyMOL for this pair of chaperone proteins. It was discovered that in addition to the interaction sites in the J domain, the carboxyl-terminal domain of Hsp40 also plays a crucial role in its interaction with Hsp70. This is important for the mechanistic understanding of the Hsp40–Hsp70 chaperone system, providing a theoretical basis for turbot disease resistance breeding, and effective value for the prevention of certain diseases in turbot. Full article

In light of expected climate change, it is important to seek nature-based solutions that can contribute to the protection of our planet as well as to help overcome the emerging adverse changes. In an agricultural context, increasing plant resistance to abiotic stress seems to be crucial. Therefore, the scope of the presented research was focused on the application of botanical extracts that exerted positive effects on model plants growing under controlled laboratory conditions, as well as plants subjected to sorbitol-induced osmotic stress. Foliar spraying increased the length and fresh mass of the shoots (e.g., extracts from Taraxacum officinale, Trifolium pratense, and Pisum sativum) and the roots (e.g., Solidago gigantea, Hypericum perforatum, and Pisum sativum) of cabbage seedlings grown under stressful conditions, as well as their content of photosynthetic pigments (Pisum sativum, Lens culinaris, and Hypericum perforatum) along with total phenolic compounds (Hypericum perforatum, Taraxacum officinale, and Urtica dioica). The antioxidant activity of the shoots measured with the use of DDPH (Pisum sativum, Taraxacum officinale, Urtica dioica, and Hypericum perforatum), ABTS (Trifolium pratense, Symphytum officinale, Valeriana officinalis, Pisum sativum, and Lens culinaris), and FRAP (Symphytum officinale, Valeriana officinalis, Urtica dioica, Hypericum perforatum, and Taraxacum officinale) assays was also enhanced in plants exposed to osmotic stress. Based on these findings, the most promising formulation based on Symphytum officinale was selected and subjected to transcriptomic analysis. The modification of the expression of the following genes was noted: Bol029651 (glutathione S-transferase), Bol027348 (chlorophyll A-B binding protein), Bol015841 (S-adenosylmethionine-dependent methyltransferases), Bol009860 (chlorophyll A-B binding protein), Bol022819 (GDSL lipase/esterase), Bol036512 (heat shock protein 70 family), Bol005916 (DnaJ Chaperone), Bol028754 (pre-mRNA splicing Prp18-interacting factor), Bol009568 (heat shock protein Hsp90 family), Bol039362 (gibberellin regulated protein), Bol007693 (B-box-type zinc finger), Bol034610 (RmlC-like cupin domain superfamily), Bol019811 (myb_SHAQKYF: myb-like DNA-binding domain, SHAQKYF class), Bol028965 (DA1-like Protein). Gene Ontology functional analysis indicated that the application of the extract led to a decrease in the expression of many genes related to the response to stress and photosynthetic systems, which may confirm a reduction in the level of oxidative stress in plants treated with biostimulants. The conducted studies showed that the use of innovative plant-based products exerted positive effects on crops and can be used to supplement current cultivation practices. Full article

The study aimed to evaluate the mRNA expression levels of various local novel adipokines, including vaspin, adiponectin, visfatin, and resistin, along with their associated receptors, heat shock 70 protein 5, adiponectin receptor 1, and adiponectin receptor 2, in the corpus luteum (CL) during luteal regression, also known as luteolysis, in dairy cows. We selected Fleckvieh cows in the mid-luteal phase (days 8–12, control group) and administered cloprostenol (PGF analog) to experimentally induce luteolysis. We collected CL samples at different time points following PGF application: before treatment (days 8–12, control group) and at 0.5, 2, 4, 12, 24, 48, and 64 h post-treatment (n = 5) per group. The mRNA expression was measured via real-time reverse transcription polymerase chain reaction (RT-qPCR). Vaspin was characterized by high mRNA levels at the beginning of the regression stage, followed by a significant decrease 48 h and 64 h after PGF treatment. Adiponectin mRNA levels were elevated 48 h after PGF. Resistin showed upregulation 4 h post PGF application. In summary, the alterations observed in the adipokine family within experimentally induced regressing CL tissue potentially play an integral role in the local regulatory processes governing the sequence of events culminating in functional luteolysis and subsequent structural changes in the bovine ovary. Full article

Heat shock protein 70 (Hsp70) is a class of HSPs involved in plant growth and development, stress response and regulation. The Hsp70 proteins exist widely in the plant world, but the detail information about Hsp70s is still unclear in cucumber. Based on the available cucumber genome, a total of 12 Hsp70 genes (CsHsp70-1 to CsHsp70-12) were identified in this study, and they were distributed among five out of seven chromosomes. The CsHsp70s were divided into four groups based on a phylogenetic analysis by using protein sequences from cucumber and other plants, and their conserved motifs were relatively conserved. Gene duplication analysis showed that segmental duplication is the main driving force of expansion in cucumber CsHsp70 genes. Promoter analysis of CsHsp70 genes showed that they contained many cis-acting elements involved in hormone and stress responses. Expression analysis by RNA-seq and qRT-PCR indicated that the expression of most CsHsp70 genes was associated with multiple biotic and abiotic stresses in cucumber. This study introduces the characteristics of cucumber CsHsp70 genes and the regulation of their expression levels in various abiotic and biotic stresses, which provided a basis for functional exploration and utilization of CsHsp70 genes in the future. Full article

Heat shock protein 70 kDa (Hsp70) is a highly conserved heat stress protein that is important in biotic processes and responses to abiotic stress. Hsp70 genes may be important in Sebastiscus marmoratus, for it is a kind of nearshore reef fish, and habitat temperature change is more drastic during development. However, genome-wide identification and expression analysis in the Hsp70 gene family of S. marmoratus are still lacking. Here, a total of 15 Hsp70 genes in the genome of S. marmoratus are identified, and their expression patterns were investigated using transcriptomic data from thermal stress experiments. The expansion and gene duplication events of Hsp70 genes from the Hspa4, Hspa8, and Hspa12a subfamilies in S. marmoratus are revealed by phylogenetic analysis. qRT-PCR expression patterns demonstrated that seven Hsp70 genes were significantly up-regulated and none were significantly down-regulated after heat treatment. Only the hsp70 gene was significantly up-regulated after cold treatment. The selection test further showed a purifying selection on the duplicated gene pairs, suggesting that these genes underwent subfunctionalization. Our results add novel insight to aquaculture and biological research on S. marmoratus, providing important information on how Hsp70 genes are regulated in Scorpaeniformes under thermal stress. Full article

Heat shock protein 70 (HSP70) is an evolutionarily conserved protein chaperone in prokaryotic and eukaryotic organisms. This family is involved in the maintenance of physiological homeostasis by ensuring the proper folding and refolding of proteins. The HSP70 family in terrestrial plants can be divided into cytoplasm, endoplasmic reticulum (ER)-, mitochondrion (MT)-, and chloroplast (CP)-localized HSP70 subfamilies. In the marine red alga Neopyropia yezoensis, the heat-inducible expression of two cytoplasmic HSP70 genes has been characterized; however, little is known about the presence of other HSP70 subfamilies and their expression profiles under heat stress conditions. Here, we identified genes encoding one MT and two ER HSP70 proteins and confirmed their heat-inducible expression at 25 °C. In addition, we determined that membrane fluidization directs gene expression for the ER-, MT-, and CP-localized HSP70 proteins as with cytoplasmic HSP70s. The gene for the CP-localized HSP70 is carried by the chloroplast genome; thus, our results indicate that membrane fluidization is a trigger for the coordinated heat-driven induction of HSP70 genes harbored by the nuclear and plastid genomes in N. yezoensis. We propose this mechanism as a unique regulatory system common in the Bangiales, in which the CP-localized HSP70 is usually encoded in the chloroplast genome. Full article