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1
Bala, Nurudeen Muhammad, and Suhailan Bin Safei. "A Hybrid Harmony Search and Particle Swarm Optimization Algorithm (HSPSO) for Testing Non-functional Properties in Software System." Statistics, Optimization & Information Computing 10, no. 3 (January 9, 2021): 968–82. http://dx.doi.org/10.19139/soic-2310-5070-1039.
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An important aspect of improving software system is testing. However, it is time demanding and sometimeslabour intensive if done manually. In this paper, we developed an automatic search-based approach for testing the nonfunctional properties of a software system using hybrid harmony search and particle swarm optimization algorithms. The approach birthed a new algorithm named HSPSO, which is proposed based on the strength of HS over Genetic algorithm (GA) in terms of less adjustable parameters, quick convergence and smooth implementation. On the other hand, we propose the PSO to complement the drawback of HS in terms of time consumption problem. Besides, we used four programs for the comparative efficiency analysis of the proposed algorithm in relation to competing algorithms based on average branch coverage and execution time. The results from the analysis showed that the HSPSO algorithm was able to achieve 100% average coverage with a fewer number of generated test cases and under limited execution time.
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Xu, Ji, Hong Zhou, Yanjun Fang, and Lan Liu. "Data-Driven Approach for the Short-Term Business Climate Forecasting Based on Power Consumption." Wireless Communications and Mobile Computing 2022 (April 27, 2022): 1–11. http://dx.doi.org/10.1155/2022/4037053.
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With the fast development of intelligent data-mining technologies, some advanced artificial intelligence approaches are widely developed and employed to help the decision-making of enterprises and government. The application of advanced and intelligent approaches successfully helps the enterprises and government find out the valuable information hidden in the massive economic data. This study presents a novel data-driven approach to forecast the short-term business climate using the electric power consumption data of large enterprises. In addition, the climate conditions, interactions between different industries, the business cycle, and some other related variables are also considered and included in the developed forecasting model. To be specific, the business climate prediction model based on support vector machine (SVM) is proposed firstly, and the human-simulated particle swarm optimization algorithm (HSPSO) in our previous work is employed to optimize the parameters of the developed forecasting model. Secondly, a novel power-consumption-based business climate index (BCI) system is developed and comprehensively analyzed. The developed BCI system that contains the index for each separate industry (BCI-I), the index for tertiary industry (BCI-T), the index for secondary industry (BCI-S), and the index for the entire province (BCI-P) is proposed. In addition, the developed BCI system is employed to normalize the output of SVM-based forecasting model to directly indicate the business climate, which is very important to the decision-making of enterprises and government under the background of smart cities. Finally, the real data of Guangdong province in China, including the gross output values (GOV) and detailed power consumptions of more than 38000 enterprises, are employed to test the proposed approach. Experimental results show that the GOV of each industry and the whole society predicted by HSPSO-SVM matches the real data well. Moreover, the predicted BCI can directly indicate the business climate in advance, which is of great value for economic-decision and policy-making of both enterprises and government.
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Banu, P. K. Nizar, and S. Andrews. "Harmony Search PSO Clustering for Tumor and Cancer Gene Expression Dataset." International Journal of Swarm Intelligence Research 5, no. 3 (July 2014): 1–21. http://dx.doi.org/10.4018/ijsir.2014070101.
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Enormous quantity of gene expression data from diverse data sources are accumulated due to the modern advancement in microarray technology that leads to major computational challenges. The foremost step towards addressing this challenge is to cluster genes which reveal hidden gene expression patterns and natural structures to find the interesting patterns from the underlying data that in turn helps in disease diagnosis and drug development. Particle Swarm Optimization (PSO) technique is extensively used for many practical applications but fails in finding the initial seeds to generate clusters and thus reduces the clustering accuracy. One of the meta-heuristic optimization algorithms called Harmony Search is free from divergence and helps to find out the near-global optimal solutions by searching the entire solution space. This paper proposes a novel Harmony Search Particle Swarm Optimization (HSPSO) clustering algorithm and is applied for Brain Tumor, Colon Cancer, Leukemia Cancer and Lung Cancer gene expression datasets for clustering. Experimental results show that the proposed algorithm produces clusters with better compactness and accuracy, in comparison with K-means clustering, PSO clustering (swarm clustering) and Fuzzy PSO clustering.
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Kaneda, F., and P. G. Kwiat. "High-efficiency single-photon generation via large-scale active time multiplexing." Science Advances 5, no. 10 (October 2019): eaaw8586. http://dx.doi.org/10.1126/sciadv.aaw8586.
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Deterministic generation of single- and multiphoton states is a key requirement for large-scale optical quantum information and communication applications. While heralded single-photon sources (HSPSs) using nonlinear optical processes have enabled proof-of-principle demonstrations in this area of research, they are not scalable as their probabilistic nature severely limits their generation efficiency. We overcome this limitation by demonstrating a substantial improvement in HSPS efficiency via large-scale time multiplexing. Using an ultra-low loss, adjustable optical delay to multiplex 40 conventional HSPS photon generation processes into each operation cycle, we have observed a factor of 9.7(5) enhancement in efficiency, yielding a 66.7(24)% probability of collecting a single photon with high indistinguishability (90%) into a single-mode fiber per cycle. We also experimentally investigate the trade-off between a high single-photon probability and unwanted multiphoton emission. Upgrading our time-multiplexed source with state-of-the-art HSPS and single-photon detector technologies will enable the generation of >30 coincident photons with unprecedented efficiency.
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Tower, John. "Hsps and aging." Trends in Endocrinology & Metabolism 20, no. 5 (July 2009): 216–22. http://dx.doi.org/10.1016/j.tem.2008.12.005.
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Chen, Wei, Pengmian Feng, Tao Liu, and Dianchuan Jin. "Recent Advances in Machine Learning Methods for Predicting Heat Shock Proteins." Current Drug Metabolism 20, no. 3 (May 22, 2019): 224–28. http://dx.doi.org/10.2174/1389200219666181031105916.
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Background:As molecular chaperones, Heat Shock Proteins (HSPs) not only play key roles in protein folding and maintaining protein stabilities, but are also linked with multiple kinds of diseases. Therefore, HSPs have been regarded as the focus of drug design. Since HSPs from different families play distinct functions, accurately classifying the families of HSPs is the key step to clearly understand their biological functions. In contrast to laborintensive and cost-ineffective experimental methods, computational classification of HSP families has emerged to be an alternative approach.Methods:We reviewed the paper that described the existing datasets of HSPs and the representative computational approaches developed for the identification and classification of HSPs.Results:The two benchmark datasets of HSPs, namely HSPIR and sHSPdb were introduced, which provided invaluable resources for computationally identifying HSPs. The gold standard dataset and sequence encoding schemes for building computational methods of classifying HSPs were also introduced. The three representative web-servers for identifying HSPs and their families were described.Conclusion:The existing machine learning methods for identifying the different families of HSPs indeed yielded quite encouraging results and did play a role in promoting the research on HSPs. However, the number of HSPs with known structures is very limited. Therefore, determining the structure of the HSPs is also urgent, which will be helpful in revealing their functions.
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Baszczynski, Chris L. "Immunochemical analysis of heat-shock protein synthesis in maize (Zea mays L.)." Canadian Journal of Genetics and Cytology 28, no. 6 (December 1, 1986): 1076–87. http://dx.doi.org/10.1139/g86-151.
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Polyclonal antibodies to 18-kilodalton (kDa) heat-shock proteins (HSPs) and to the high molecular weight (73 000 – 89 000) HSPs from 5- day-old maize plumules have been produced in rabbits. The antisera to high molecular weight HSPs show minor cross-reactivity to proteins of similar molecular mass in not heat-shocked tissues, while antisera to 18-kDa HSPs react only with this 18-kDa HSP class. HSPs of similar molecular mass and isoelectric points in maize plumules, mesocotyls, radicles, and young leaves also have similar antigenic determinants based on positive reactions with antisera to plumule HSPs. Among 13 maize inbreds and genetic stocks tested, differences were noted in the amount of immunoprecipitable 18-kDa HSPs. Antisera to maize plumule HSPs also showed cross-reactivity with similar-sized HSPs from pea epicotyls and soybean hypocotyls but not with HSPs from several animal tissues.Key words: polyclonal antibodies, maize, heat-shock.
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Song, Xueming, Zhiqiang Chen, Chunbo Wu, and Shiguang Zhao. "Abrogating HSP Response Augments Cell Death Induced by As2O3 in Glioma Cell Lines." Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 37, no. 4 (July 2010): 504–11. http://dx.doi.org/10.1017/s0317167100010544.
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Objectives:We previously reported that Arsenic trioxide (ATO) can inhibit glioma growth both in vitro and in vivo. While the use of ATO alone for solid tumor treatment sometimes was found to be ineffective which may be due to the protective pathways including heat shock proteins (HSPs) response induced by ATO. In this study, we modified HSPs expression to investigate whether HSPs had some effect on ATO induced glioma cell death.Methods:Trypan bule exclusion assay, mitochondrial membrane potential (MMP) Assay, and SubG1 detection were used to evaluate cell viability and western-blot was employed to detect HSPs and some apoptosis markers expression induced by ATO. Heat pre-treatment, HSPs inhibitor, or Heat Shock factor-1 (HSF1) knockdown by SiRNA was employed to modify HSPs levels.Results:It was showed that KNK437 (HSPs inhibitor) or HSF1 knockdown significantly enhanced cell death, MMP disruption, JNK phosphorylation and caspase-3 cleavage induced by ATO, which was accompanied by abrogation of HSPs induction, while heat pre-treatment with clear HSPs induction had strong protection on the effects mentioned above.Conclusion:Those data suggested that HSPs play protective roles on ATO induced cell death in glioma. Inhibition of HSPs may have a synergistic effect with ATO on glioma treatment.
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Vierling, Elizabeth. "MOLECULAR ANALYSIS OF HEAT STRESS PROTEINS IN HIGHER PLANTS." HortScience 25, no. 9 (September 1990): 1175e—1175. http://dx.doi.org/10.21273/hortsci.25.9.1175e.
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When plants experience high temperature stress, they respond by synthesizing a discrete set of proteins called heat shock proteins (HSPs). This response is not unique to plants, but is observed in all other eukaryotes. It is now known that the HSPs are evolutionarily conserved proteins, and furthermore, that HSPs function not only during stress, but also during normal growth and development. My laboratory has characterized several of the major groups of HSPs in higher plants. We have cloned genes encoding plant HSP70 proteins and low molecular weight (LMW) HSPs (17-23 kDa). Using this information we have investigated the expression of HSPs both in the field, and under laboratory conditions which mimic field situations. We have determined the temperature limits for expression of HSPs in vegetative tissues, and have also found that HSPs are frequently produced in plant reproductive structures, even in the absence of stress. As a first step toward understanding HSP function, we have characterized the intracellular localization of HSPs. Results show that there are unique HSPs in the cytoplasm, chloroplast and endomembrane system. These ubiquitous proteins appear to play essential roles in many cellular processes.
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Rodríguez-Iturbe, B., and RJ Johnson. "Heat shock proteins and cardiovascular disease." Physiology International 105, no. 1 (March 2018): 19–37. http://dx.doi.org/10.1556/2060.105.2018.1.4.
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The development of stress drives a host of biological responses that include the overproduction of a family of proteins named heat shock proteins (HSPs), because they were initially studied after heat exposure. HSPs are evolutionarily preserved proteins with a high degree of interspecies homology. HSPs are intracellular proteins that also have extracellular expression. The primary role of HSPs is to protect cell function by preventing irreversible protein damage and facilitating molecular traffic through intracellular pathways. However, in addition to their chaperone role, HSPs are immunodominant molecules that stimulate natural as well as disease-related immune reactivity. The latter may be a consequence of molecular mimicry, generating cross-reactivity between human HSPs and the HSPs of infectious agents. Autoimmune reactivity driven by HSPs could also be the result of enhancement of the immune response to peptides generated during cellular injury and of their role in the delivery of peptides to the major histocompatibility complex in antigen-presenting cells. In humans, HSPs have been found to participate in the pathogenesis of a large number of diseases. This review is focused on the role of HSPs in atherosclerosis and essential hypertension.
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Xu, Qingbo, Bernhard Metzler, Marjan Jahangiri, and Kaushik Mandal. "Molecular chaperones and heat shock proteins in atherosclerosis." American Journal of Physiology-Heart and Circulatory Physiology 302, no. 3 (February 2012): H506—H514. http://dx.doi.org/10.1152/ajpheart.00646.2011.
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In response to stress stimuli, mammalian cells activate an ancient signaling pathway leading to the transient expression of heat shock proteins (HSPs). HSPs are a family of proteins serving as molecular chaperones that prevent the formation of nonspecific protein aggregates and assist proteins in the acquisition of their native structures. Physiologically, HSPs play a protective role in the homeostasis of the vessel wall but have an impact on immunoinflammatory processes in pathological conditions involved in the development of atherosclerosis. For instance, some members of HSPs have been shown to have immunoregulatory properties and modification of innate and adaptive response to HSPs, and can protect the vessel wall from the disease. On the other hand, a high degree of sequence homology between microbial and mammalian HSPs, due to evolutionary conservation, carries a risk of misdirected autoimmunity against HSPs expressed on the stressed cells of vascular endothelium. Furthermore, HSPs and anti-HSP antibodies have been shown to elicit production of proinflammatory cytokines. Potential therapeutic use of HSP in prevention of atherosclerosis involves achieving optimal balance between protective and immunogenic effects of HSPs and in the progress of research on vaccination. In this review, we update the progress of studies on HSPs and the integrity of the vessel wall, discuss the mechanism by which HSPs exert their role in the disease development, and highlight the potential clinic translation in the research field.
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Das, Jugal Kishore, Xiaofang Xiong, Xingcong Ren, Jin-Ming Yang, and Jianxun Song. "Heat Shock Proteins in Cancer Immunotherapy." Journal of Oncology 2019 (December 11, 2019): 1–9. http://dx.doi.org/10.1155/2019/3267207.
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Heat shock proteins (HSPs) are highly conserved molecular chaperones with divergent roles in various cellular processes. The HSPs are classified according to their molecular size as HSP27, HSP40, HSP60, HSP70, and HSP90. The HSPs prevent nonspecific cellular aggregation of proteins by maintaining their native folding energetics. The disruption of this vital cellular process, driven by the aberrant expression of HSPs, is implicated in the progression of several different carcinomas. Many HSPs are also actively involved in promoting the proliferation and differentiation of tumor cells, contributing to their metastatic phenotype. Upregulation of these HSPs is associated with the poor outcome of anticancer therapy in clinical settings. On the other hand, these highly expressed HSPs may be exploited as viable immunotherapeutic targets for different types of cancers. This review discusses recent advances and perspectives on the research of HSP-based cancer immunotherapy.
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Paul, Catherine, Florence Manero, Sandrine Gonin, Carole Kretz-Remy, Vesna Ljubic-Thibal, Cécile Ducasse, Chantal Diaz-Latoud, and Andre-Patrick Arrigo. "Small Hsps as regulators of apoptosis." Biology of the Cell 91, no. 7 (September 1999): 545. http://dx.doi.org/10.1016/s0248-4900(99)90250-2.
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Fang, Bingliang, and Wei Guo. "Enhancing antitumor immune response by HSPs." Cancer Biology & Therapy 7, no. 2 (February 4, 2008): 196–97. http://dx.doi.org/10.4161/cbt.7.2.5578.
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Kilic, Arman, and Kaushik Mandal. "Heat Shock Proteins: Pathogenic Role in Atherosclerosis and Potential Therapeutic Implications." Autoimmune Diseases 2012 (2012): 1–9. http://dx.doi.org/10.1155/2012/502813.
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Heat shock proteins (HSPs) are a highly conserved group of proteins that are constitutively expressed and function as molecular chaperones, aiding in protein folding and preventing the accumulation of misfolded proteins. In the arterial wall, HSPs have a protective role under normal physiologic conditions. In disease states, however, HSPs expressed on the vascular endothelial cell surface can act as targets for detrimental autoimmunity due to their highly conserved sequences. Developing therapeutic strategies for atherosclerosis based on HSPs is challenged by the need to balance such physiologic and pathologic roles of these proteins. This paper summarizes the role of HSPs in normal vascular wall processes as well as in the development and progression of atherosclerosis. The potential implications of HSPs in clinical therapies for atherosclerosis are also discussed.
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Yun, Chul Won, Hyung Joo Kim, Ji Ho Lim, and Sang Hun Lee. "Heat Shock Proteins: Agents of Cancer Development and Therapeutic Targets in Anti-Cancer Therapy." Cells 9, no. 1 (December 24, 2019): 60. http://dx.doi.org/10.3390/cells9010060.
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Heat shock proteins (HSPs) constitute a large family of molecular chaperones classified by their molecular weights, and they include HSP27, HSP40, HSP60, HSP70, and HSP90. HSPs function in diverse physiological and protective processes to assist in maintaining cellular homeostasis. In particular, HSPs participate in protein folding and maturation processes under diverse stressors such as heat shock, hypoxia, and degradation. Notably, HSPs also play essential roles across cancers as they are implicated in a variety of cancer-related activities such as cell proliferation, metastasis, and anti-cancer drug resistance. In this review, we comprehensively discuss the functions of HSPs in association with cancer initiation, progression, and metastasis and anti-cancer therapy resistance. Moreover, the potential utilization of HSPs to enhance the effects of chemo-, radio-, and immunotherapy is explored. Taken together, HSPs have multiple clinical usages as biomarkers for cancer diagnosis and prognosis as well as the potential therapeutic targets for anti-cancer treatment.
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Zininga, Tawanda, Lebogang Ramatsui, and Addmore Shonhai. "Heat Shock Proteins as Immunomodulants." Molecules 23, no. 11 (November 1, 2018): 2846. http://dx.doi.org/10.3390/molecules23112846.
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Heat shock proteins (Hsps) are conserved molecules whose main role is to facilitate folding of other proteins. Most Hsps are generally stress-inducible as they play a particularly important cytoprotective role in cells exposed to stressful conditions. Initially, Hsps were generally thought to occur intracellulary. However, recent work has shown that some Hsps are secreted to the cell exterior particularly in response to stress. For this reason, they are generally regarded as danger signaling biomarkers. In this way, they prompt the immune system to react to prevailing adverse cellular conditions. For example, their enhanced secretion by cancer cells facilitate targeting of these cells by natural killer cells. Notably, Hsps are implicated in both pro-inflammatory and anti-inflammatory responses. Their effects on immune cells depends on a number of aspects such as concentration of the respective Hsp species. In addition, various Hsp species exert unique effects on immune cells. Because of their conservation, Hsps are implicated in auto-immune diseases. Here we discuss the various metabolic pathways in which various Hsps manifest immune modulation. In addition, we discuss possible experimental variations that may account for contradictory reports on the immunomodulatory function of some Hsps.
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Abi Zamer, Batoul, Waseem El-Huneidi, Mohamed Ahmed Eladl, and Jibran Sualeh Muhammad. "Ins and Outs of Heat Shock Proteins in Colorectal Carcinoma: Its Role in Carcinogenesis and Therapeutic Perspectives." Cells 10, no. 11 (October 24, 2021): 2862. http://dx.doi.org/10.3390/cells10112862.
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Cancer cells can reprogram their metabolic activities and undergo uncontrolled proliferation by utilizing the power of heat shock proteins (HSPs). HSPs are highly conserved chaperones that facilitate the folding of intracellular proteins under stress. Constitutively, HSPs are expressed at low levels, but their expression upregulates in response to a wide variety of insults, including anticancer drugs, allowing cancer cells to develop chemoresistance. In recent years, several researchers have reported that HSPs could be an important therapeutic target in difficult-to-treat cancers such as colorectal carcinoma (CRC). Worldwide, CRC is the second most common type of cancer and the second leading cause of cancer-related deaths. The molecular complexity of CRC and the coexisting inflammatory conditions present a significant obstacle to developing effective treatment. Recently, considerable progress has been made in enhancing our understanding of the role of HSPs in CRC pathogenesis. Moreover, novel therapeutic strategies targeting HSPs, either alone or in combination with other anticancer agents, have been reported. Herein, we present an overview of the functional mechanisms and the diagnostic and prognostic potential of HSPs in CRC. We also discuss emerging anti-CRC strategies based on targeting HSPs.
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Liu, Daiqi, Xuyao Han, Zhiwei Zhang, Gary Tse, Qingmiao Shao, and Tong Liu. "Role of Heat Shock Proteins in Atrial Fibrillation: From Molecular Mechanisms to Diagnostic and Therapeutic Opportunities." Cells 12, no. 1 (December 30, 2022): 151. http://dx.doi.org/10.3390/cells12010151.
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Heat shock proteins (HSPs) are endogenous protective proteins and biomarkers of cell stress response, of which examples are HSP70, HSP60, HSP90, and small HSPs (HSPB). HSPs protect cells and organs, especially the cardiovascular system, against harmful and cytotoxic conditions. More recent attention has focused on the roles of HSPs in the irreversible remodeling of atrial fibrillation (AF), which is the most common arrhythmia in clinical practice and a significant contributor to mortality. In this review, we investigated the relationship between HSPs and atrial remodeling mechanisms in AF. PubMed was searched for studies using the terms “Heat Shock Proteins” and “Atrial Fibrillation” and their relevant abbreviations up to 10 July 2022. The results showed that HSPs have cytoprotective roles in atrial cardiomyocytes during AF by promoting reverse electrical and structural remodeling. Heat shock response (HSR) exhaustion, followed by low levels of HSPs, causes proteostasis derailment in cardiomyocytes, which is the basis of AF. Furthermore, potential implications of HSPs in the management of AF are discussed in detail. HSPs represent reliable biomarkers for predicting and staging AF. HSP inducers may serve as novel therapeutic modalities in postoperative AF. HSP induction, either by geranylgeranylacetone (GGA) or by other compounds presently in development, may therefore be an interesting new approach for upstream therapy for AF, a strategy that aims to prevent AF whilst minimizing the ventricular proarrhythmic risks of traditional anti-arrhythmic agents.
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Chiba, Tsuyoshi, Nanae Tanemura, and Chiharu Nishijima. "Determination of the Awareness about and Need for Health Support Pharmacies as the Provider of Consultation Service about Nutrition Education and Diet-Related Health Promotion by Health Professionals in Japan." Nutrients 14, no. 1 (December 30, 2021): 165. http://dx.doi.org/10.3390/nu14010165.
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Health support pharmacies (HSPs) have been established as a new category of pharmacies in Japan. In addition to prescriptions, HSPs provide several health services, including consultations on diet/nutrition, health foods, and nursing care. Therefore, not only individuals receiving medications but also community residents should have access to HSPs. However, it is unclear whether people are aware of HSPs. Thus, the purpose of this study was to assess the awareness about HSPs and determine the need for their services. To this end, we conducted an online cross-sectional questionnaire survey in 10,000 Japanese adults. Approximately 60.2% of the participants were aware of family pharmacies/pharmacists, and 21.8% of these participants had a family pharmacy/pharmacist. Meanwhile, 2.6% of the participants were aware of HSPs, while 9.2% of the participants had only heard of HSPs. Awareness of HSPs was higher among men and younger individuals than among women and older generations. In addition, only 7.2% of the participants were aware of the location of the HSP in their area of residence. At the time at which this survey was conducted, only 3.5% of the participants were using HSP services, and half of them did not perceive the merits of using these services. However, 44.4% of the participants wished to avail themselves of HSP services in the future, and this desire increased with age. Half of the participants wished to use services that were associated with drugs, and the need for other services, such as consultations on diet/nutrition or health foods, was low. In conclusion, there was low awareness about HSPs among the survey participants. However, from our findings, we gathered that if individuals are aware of HSPs, they will wish to use HSP services. To improve healthy life expectancy, it is important to increase awareness about HSPs and their number.
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Goulhen, Florence, Daniel Grenier, and Denis Mayrand. "Oral Microbial Heat-shock Proteins and Their Potential Contributions to Infections." Critical Reviews in Oral Biology & Medicine 14, no. 6 (November 2003): 399–412. http://dx.doi.org/10.1177/154411130301400603.
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The oral cavity is a complex ecosystem in which several hundred microbial species normally cohabit harmoniously. However, under certain special conditions, the growth of some micro-organisms with a pathogenic potential is promoted, leading to infections such as dental caries, periodontal disease, and stomatitis. The physiology and pathogenic properties of micro-organisms are influenced by modifications in environmental conditions that lead to the synthesis of specific proteins known as the heat-shock proteins (HSPs). HSPs are families of highly conserved proteins whose main role is to allow micro-organisms to survive under stress conditions. HSPs act as molecular chaperones in the assembly and folding of proteins, and as proteases when damaged or toxic proteins have to be degraded. Several pathological functions have been associated with these proteins. Many HSPs of oral micro-organisms, particularly periodontopathogens, have been identified, and some of their properties—including location, cytotoxicity, and amino acid sequence homology with other HSPs—have been reported. Since these proteins are immunodominant antigens in many human pathogens, studies have recently focused on the potential contributions of HSPs to oral diseases. The cytotoxicity of some bacterial HSPs may contribute to tissue destruction, whereas the presence of common epitopes in host proteins and microbial HSPs may lead to autoimmune responses. Here, we review the current knowledge regarding HSPs produced by oral micro-organisms and discuss their possible contributions to the pathogenesis of oral infections.
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Edmison, Daisy, Luyu Wang, and Swetha Gowrishankar. "Lysosome Function and Dysfunction in Hereditary Spastic Paraplegias." Brain Sciences 11, no. 2 (January 24, 2021): 152. http://dx.doi.org/10.3390/brainsci11020152.
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Hereditary Spastic Paraplegias (HSPs) are a genetically diverse group of inherited neurological diseases with over 80 associated gene loci. Over the last decade, research into mechanisms underlying HSPs has led to an emerging interest in lysosome dysfunction. In this review, we highlight the different classes of HSPs that have been linked to lysosome defects: (1) a subset of complex HSPs where mutations in lysosomal genes are causally linked to the diseases, (2) other complex HSPs where mutation in genes encoding membrane trafficking adaptors lead to lysosomal defects, and (3) a subset of HSPs where mutations affect genes encoding proteins whose function is primarily linked to a different cellular component or organelle such as microtubule severing and Endoplasmic Reticulum-shaping, while also altering to lysosomes. Interestingly, aberrant axonal lysosomes, associated with the latter two subsets of HSPs, are a key feature observed in other neurodegenerative diseases such as Alzheimer’s disease. We discuss how altered lysosome function and trafficking may be a critical contributor to HSP pathology and highlight the need for examining these features in the cortico-spinal motor neurons of HSP mutant models.
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Voegeli, Tracy S., Amanda J. Wintink, Yu Chen, and R. William Currie. "Heat shock proteins 27 and 70 regulating angiotensin II-induced NF-κB: a possible connection to blood pressure control?" Applied Physiology, Nutrition, and Metabolism 33, no. 5 (October 2008): 1042–49. http://dx.doi.org/10.1139/h08-068.
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Heat shock proteins (HSPs) are critical for cell survival and have several mechanisms of action. HSPs regulate protein folding, suppress apoptosis, and regulate anti-oxidative activity. In addition, HSPs are involved in the regulation of the pro-inflammatory transcription factor nuclear factor (NF)-κB. When angiotensin (Ang) II is infused into rats, there is a significant increase in systolic blood pressure, and NF-κB is activated in the heart. If rats are heat shocked to induce the heat shock response and HSPs before Ang II infusion, there is a significant suppression of both the Ang II-induced increase in blood pressure and NF-κB activation in the heart. Although the role of specific HSPs in the regulation of NF-κB is unclear, several HSPs, including Hsp27 and Hsp70, are thought to be involved in the regulation of Ang II-induced NF-κB. The role of Hsp27 and Hsp70 in NF-κB activation is reviewed here, along with evidence suggesting that HSPs regulate Ang II-induced blood pressure through the regulation of NF-κB.
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Arnold-Schild, Danièle, Daniel Hanau, Danièle Spehner, Claudia Schmid, Hans-Georg Rammensee, Henri de la Salle, and Hansjörg Schild. "Cutting Edge: Receptor-Mediated Endocytosis of Heat Shock Proteins by Professional Antigen-Presenting Cells." Journal of Immunology 162, no. 7 (April 1, 1999): 3757–60. http://dx.doi.org/10.4049/jimmunol.162.7.3757.
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Abstract Immunization with heat shock proteins (HSPs) induces Ag-specific CTL responses. The specificity of the immune response is based on peptides associated with HSPs. To investigate how exogenous HSP/peptide complexes gain access to the MHC class I-restricted Ag presentation pathway, we incubated the monocytic cell line P388D1 and the dendritic cell line D2SC/1 with gold-labeled HSPs gp96 and HSC70. We show that HSPs bind specifically to the surface of these APCs and are internalized spontaneously by receptor-mediated endocytosis, demonstrating the existence of specific receptors for HSPs on these cells. In addition, we observe colocalization of internalized HSPs and surface MHC class I molecules in early and late endosomal structures. These findings provide possible explanations for the immunogenicity of HSP/peptide complexes and for the transfer of HSP-associated peptides onto MHC class I molecules.
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Yakovenko, L. F., O. V. Romashchenko, and I. V. Kroupskaya. "Heat shock proteins in the diagnosis and prognosis of reproductive disorders in women." HEALTH OF WOMAN, no. 7(133) (September 30, 2018): 77–83. http://dx.doi.org/10.15574/hw.2018.133.77.
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Heat shock proteins are structurally highly conserved and abundantly expressed by prokaryotic and eukaryotic cells under stressful conditions. HSPs are immunodominant antigens for many microbes. They are overexpressed at sites of acute and chronic inflammation and involved in the patogenesis of various diseases. Clinical studies and results of own investigations provided evidence that HSPs and anti-HSPs antibodies can be biomarkers for the diagnosis and prognosis of reproductive disorders in women. The involvement of HSPs and anti-HSPs antibodies in pathogenesis of tubal infertility, ovarian failure, pregnancy loss is discussed. Key words: heat shock proteins, antibodies against heat shock proteins, infertility, pregnancy loss, in vitro fertilisation.
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Sediqi, Khwaja Zubair, Lars Prehn, and Oliver Gasser. "Hyper-specific prefixes." ACM SIGCOMM Computer Communication Review 52, no. 2 (April 30, 2022): 20–34. http://dx.doi.org/10.1145/3544912.3544916.
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Autonomous Systems (ASes) exchange reachability information between each other using BGP---the de-facto standard inter-AS routing protocol. While IPv4 (IPv6) routes more specific than /24 (/48) are commonly filtered (and hence not propagated), route collectors still observe many of them. In this work, we take a closer look at those "hyper-specific" prefixes (HSPs). In particular, we analyze their prevalence, use cases, and whether operators use them intentionally or accidentally. While their total number increases over time, most HSPs can only be seen by route collector peers. Nonetheless, some HSPs can be seen constantly throughout an entire year and propagate widely. We find that most HSPs represent (internal) routes to peering infrastructure or are related to address block relocations or blackholing. While hundreds of operators intentionally add HSPs to well-known routing databases, we observe that many HSPs are possibly accidentally leaked routes.
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Brenu, E. W., D. R. Staines, L. Tajouri, T. Huth, K. J. Ashton, and S. M. Marshall-Gradisnik. "Heat Shock Proteins and Regulatory T Cells." Autoimmune Diseases 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/813256.
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Heat shock proteins (HSPs) are important molecules required for ideal protein function. Extensive research on the functional properties of HSPs indicates that HSPs may be implicated in a wide range of physiological functions including immune function. In the immune system, HSPs are involved in cell proliferation, differentiation, cytokine release, and apoptosis. Therefore, the ability of the immune system, in particular immune cells, to function optimally and in unison with other physiological systems is in part dependent on signaling transduction processes, including bidirectional communication with HSPs. Regulatory T cells (Tregs) are important T cells with suppressive functions and impairments in their function have been associated with a number of autoimmune disorders. The purpose of this paper is to examine the relationship between HSPs and Tregs. The interrelationship between cells and proteins may be important in cellular functions necessary for cell survival and expansion during diseased state.
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Tytell, M. "Release of heat shock proteins (Hsps) and the effects of extracellular Hsps on neural cells and tissues." International Journal of Hyperthermia 21, no. 5 (August 2005): 445–55. http://dx.doi.org/10.1080/02656730500041921.
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Larson, Brent K., Julie M. Hess, and Jeffrey M. Williams. "PROCEDURE FOR ESTIMATING OIL THREE-DIMENSIONAL SOLUBILITY PARAMETERS." Rubber Chemistry and Technology 90, no. 4 (October 1, 2017): 621–32. http://dx.doi.org/10.5254/rct.82.83733.
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ABSTRACT Process oils make important contributions to nearly every compound in a tire, and oil–polymer interactions have effects on compound processing and performance. One way to predict oil–polymer interactions is to determine the three-dimensional (3-D) Hansen solubility parameters (HSPs) for both oil and polymer, and the polymer solubility sphere (PSS) radius. Favorable oil–polymer interactions occur when an oil's HSPs are located within a PSS. Interactions are stronger when an oil's HSPs are located closer to the center of the PSS. If an oil's HSPs are located outside a polymer's solubility sphere, then the polymer is not soluble in the oil as a result of insufficient favorable interactions. A polymer characterization technique for determining the HSPs is the bitumen solubility model. However, no simple procedure has previously been documented for estimating the 3-D HSPs for an oil. A labor-intensive method has been described by Levin and Redelius. The oil solubility parameters estimation procedure (OSPEP) has been developed to meet the need for a relatively simple characterization technique. This procedure can provide an estimation of oil HSPs by running two titrations and a dynamic scanning calorimetry test. Analysis involves an iterative procedure to estimate the three HSPs for the oil. OSPEP represents a step forward to easily obtain insight into oil–polymer interactions.
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Son, Ok-Sun, and Jinsook Kim. "Revalidation of the Korean Version of the Highly Sensitive Person Scale (K-HSPS-18)." KOREAN JOURNAL OF COUNSELING AND PSYCHOTHERAPY 33, no. 3 (August 31, 2021): 1049–75. http://dx.doi.org/10.23844/kjcp.2021.08.33.3.1049.
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Noble, Earl G., Kevin J. Milne, and C. W. James Melling. "Heat shock proteins and exercise: a primer." Applied Physiology, Nutrition, and Metabolism 33, no. 5 (October 2008): 1050–75. http://dx.doi.org/10.1139/h08-069.
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Heat shock proteins (HSPs) are, in general, prosurvival molecules within the cellular environment, and the overexpression of even just 1 family of HSPs can lead to protection against and improvements after a variety of stressors. Not surprisingly, a fertile area of study has grown out of effors to exploit the innate biologic behaviour of HSPs. Exercise, because of the inherent physiologic stresses associated with it, is but 1 stimulus that can result in a robust increase in various HSPs in several tissues, not the least of which happen to be the heart and skeletal muscle. The purpose of this review is to introduce the reader to the major HSP families, the control of their expression, and some of their biologic functions, specifically with respect to the influence of exercise. Moreover, as the first in a series of reviews from a common symposium, we will briefly introduce the concepts presented by the other authors, which include the effects of different exercise paradigms on skeletal muscle HSPs in the adult and aged systems, HSPs as regulators of inflammation, and the ion channel stabilizing effects of HSPs.
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Nandan, Monica, Archana Singh, and Gokul Mandayam. "Social Value Creation and Social Innovation by Human Service Professionals: Evidence from Missouri, USA." Administrative Sciences 9, no. 4 (November 8, 2019): 86. http://dx.doi.org/10.3390/admsci9040086.
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Owing to the contextual challenges, human service professionals (HSP) are creating social value (SV) for diverse vulnerable population groups through social innovation. This qualitative exploratory study investigates the nature of SV created by 14 HSPs, representing a diverse range of human service organizations (HSOs), and examines ‘why’ and ‘how’ they innovate. In addition, the study examines HSPs’ current understanding and practices related to social entrepreneurship (SE). The study findings highlight that increased accountability and new funding opportunities challenged HSPs to innovate. HSPs created SV by addressing new unmet needs, developing new collaborations, and employing alternative marketing strategies, thereby ensuring the financial sustainability of their programs and organizations, and promoting social and economic justice. Different understandings of SE were voiced based on the educational backgrounds of HSPs. Without formal training in SE, HSPs trained in social work appeared to use various components of the SE process, though in a haphazard fashion compared to those with a non-social work academic training. We suggest that the graduate curriculum across various disciplines should formally include principles and behaviors related to social innovation and entrepreneurship. Finally, more research is needed to understand and describe how HSPs create SV in HSOs.
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EINSLA, BRIAN, ETHAN GLOR, JOHN ROPER, JEFF LEITINGER, NICK NICHOLAS, and SAMANTHA WOODFIN. "The use of hollow sphere pigments as strength additives in paper and paperboard coatings—Part 2: Optimization in paperboard formulations for opacity and strength." November 2020 19, no. 11 (December 1, 2020): 597–604. http://dx.doi.org/10.32964/tj19.11.597.
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This report aims to summarize the efforts in testing the properties of coatings for paperboard utilizing hollow sphere pigments (HSPs). HSPs are known to effectively scatter light and replace titanium dioxide (TiO2) in architectural coating formulations. The effect of the particle size and void fraction was evaluated, along with many coating parameters, including level of addition, binder chemistry, and blends of two HSPs. The small HSPs that have optimized voids for scattering light showed equivalent strength to the TiO2-containing control. The strength data was surprising, particularly the improvement in strength for coatings containing large particle size HSPs. Because of this increase in strength, four parts of binder could be removed, which allowed for higher brightness while not compromising other properties, including hot melt glueability. These trends held true using different binder chemistries (styrene acrylic, vinyl acrylic, and styrene butadiene). Upon refining the formulations further, blends of two HSPs showed further benefit.
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Buttacavoli, Miriam, Gianluca Di Cara, Cesare D’Amico, Fabiana Geraci, Ida Pucci-Minafra, Salvatore Feo, and Patrizia Cancemi. "Prognostic and Functional Significant of Heat Shock Proteins (HSPs) in Breast Cancer Unveiled by Multi-Omics Approaches." Biology 10, no. 3 (March 22, 2021): 247. http://dx.doi.org/10.3390/biology10030247.
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Heat shock proteins (HSPs) are a well-characterized molecular chaperones protein family, classified into six major families, according to their molecular size. A wide range of tumors have been shown to express atypical levels of one or more HSPs, suggesting that they could be used as biomarkers. However, the collective role and the possible coordination of HSP members, as well as the prognostic significance and the functional implications of their deregulated expression in breast cancer (BC) are poorly investigated. Here, we used a systematic multi-omics approach to assess the HSPs expression, the prognostic value, and the underlying mechanisms of tumorigenesis in BC. By using data mining, we showed that several HSPs were deregulated in BC and significantly correlated with a poor or good prognosis. Functional network analysis of HSPs co-expressed genes and miRNAs highlighted their regulatory effects on several biological pathways involved in cancer progression. In particular, these pathways concerned cell cycle and DNA replication for the HSPs co-expressed genes, and miRNAs up-regulated in poor prognosis and Epithelial to Mesenchymal Transition (ETM), as well as receptors-mediated signaling for the HSPs co-expressed genes up-regulated in good prognosis. Furthermore, the proteomic expression of HSPs in a large sample-set of breast cancer tissues revealed much more complexity in their roles in BC and showed that their expression is quite variable among patients and confined into different cellular compartments. In conclusion, integrative analysis of multi-omics data revealed the distinct impact of several HSPs members in BC progression and indicate that collectively they could be useful as biomarkers and therapeutic targets for BC management.
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Dahl, Heather, Tina Vo, and Margarita Huerta. " Using a Science Literary Lens to Conceptualize Anxiety Around COVID-19: Strategies for Human Services Professionals." Journal of Human Services 40, no. 1 (March 2021): 48–63. http://dx.doi.org/10.52678/2021.4.
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Amid the COVID-19 global pandemic, Human Services Professionals (HSPs) are faced with clients experiencing increased anxiety. HSPs again must broaden their scope of competency to approach this novel, natural phenomenon. Science literacy is the understanding and application of scientific knowledge toward decisions and sensemaking. Although science literacy has many facets, one area, Crosscutting Concepts (CCCs), prioritizes individuals’ funds of knowledge to engage with new phenomena such as COVID-19. This paper describes the role of HSPs responding to COVID-19; provides a conceptual framework through the Ecological Systems Theory, which centers on clients and science literacy; and proposes an integration of science concepts with HSPs’ work. Finally, this paper ends with a vignette collection offering CCCs and resource pathways HSPs can utilize with their clients.
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Stephanou, Anastasis, and David S. Latchman. "Transcriptional Modulation of Heat-Shock Protein Gene Expression." Biochemistry Research International 2011 (2011): 1–8. http://dx.doi.org/10.1155/2011/238601.
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Heat-shock proteins (Hsps) are molecular chaperones that are ubiquitously expressed but are also induced in cells exposed to stressful stimuli. Hsps have been implicated in the induction and propagation of several diseases. This paper focuses on regulatory factors that control the transcription of the genes encoding Hsps. We also highlight how distinct transcription factors are able to interact and modulate Hsps in different pathological states. Thus, a better understanding of the complex signaling pathways regulating Hsp expression may lead to novel therapeutic targets.
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Zheng, Hao-Yuan, Peng-Hao Qin, Kun Yang, Tong-Xian Liu, You-Jun Zhang, and Dong Chu. "Genome-Wide Identification and Analysis of the Heat-Shock Protein Gene Superfamily in Bemisia tabaci and Expression Pattern Analysis under Heat Shock." Insects 13, no. 7 (June 23, 2022): 570. http://dx.doi.org/10.3390/insects13070570.
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The thermal tolerance of Bemisia tabaci MED, an invasive whitefly species with worldwide distribution, plays an important role in its ecological adaptation during the invasion process. Heat-shock proteins (HSPs) are closely related to heat resistance. In this study, 33 Hsps (BtaHsps) were identified based on sequenced genome of B. tabaci MED belonging to six HSP families, among which 22 Hsps were newly identified. The secondary structures of a further 22 BtaHsps were also predicted. The results of RT-qPCR showed that heat shock could affect the expression of 14 of the 22 Hsps newly identified in this study. Among them, the expression level of six Hsps increased under 42 °C treatment. As the unstudied gene, BtaHsp90A3 had the highest increase rate. Therefore, BtaHsp90A3 was chosen for the RNAi test, and silencing BtaHsp90A3 by RNAi decreased the survival rate of adult B. tabaci at 42 °C. The results indicated that only a few Hsps were involved in the thermal tolerance of host whitefly although many Hsps would response under heat stress. This study conducted a more in-depth and comprehensive identification that demonstrates the evolutionary relationship of BtaHsps and illustrates the response of BtaHsps under the influence of thermal stress in B. tabaci MED.
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Rees, C. A. B., N. C. Hogan, D. B. Walden, and B. G. Atkinson. "Identification of mRNAs encoding low molecular mass heat-shock proteins in maize (Zea mays L.)." Canadian Journal of Genetics and Cytology 28, no. 6 (December 1, 1986): 1106–14. http://dx.doi.org/10.1139/g86-154.
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Subjecting 5-day-old maize seedlings to a rapid elevation in growth temperature (heat shock; 25–42 °C) results in a shift in the pattern of protein synthesis in maize plumules from the production of a broad spectrum of proteins to the new and (or) enhanced synthesis of a small number of heat-shock proteins (HSPs). The low relative molecular mass (Mr) HSPs, and more specifically an 18-kDa HSP with four major isoelectric variants, represent the majority of HSP synthesis following cell-free translation of total cellular poly (A)+ RNAs and polyribosomal RNAs extracted from heat-shocked plumules. Immunochemical studies, using polyclonal antibodies raised against the 18-kDa HSPs, show that the 18-kDa HSPs synthesized in vitro share immunochemical properties with HSPs of the same Mr synthesized in vivo by heat-shocked plumules. Furthermore, size fractionation and translation analyses of total cellular poly(A)+ RNAs extracted from heat-shocked plumules demonstrate that poly(A)+ RNAs encoding an 18-kDa HSP(s) have an estimated size of 0.6–0.95 kilobases. The observation that 18-kDa HSPs are absent among the translation products and immunoprecipitates of proteins synthesized in vitro by RNAs extracted from control plumules (25 °C) suggests that the mRNAs encoding 18-kDa HSPs are heat-shock induced.Key words: mRNA, maize, heat shock.
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Moseley, Pope L. "Heat shock proteins and heat adaptation of the whole organism." Journal of Applied Physiology 83, no. 5 (November 1, 1997): 1413–17. http://dx.doi.org/10.1152/jappl.1997.83.5.1413.
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Moseley, Pope L. Heat shock proteins and heat adaptation of the whole organism. J. Appl. Physiol. 83(5): 1413–1417, 1997.—Adaptation to heat may occur through acclimatization or thermotolerance; however, the linkage of these phenomena is poorly understood. The importance of heat shock proteins (HSPs) in thermotolerance and differences in their accumulation in organisms adapted to the heat suggest a role for HSPs in acclimatization as well. The role of HSPs in heat adaptation of the whole organism and the interrelationships among heat adaptation, endotoxin tolerance, and cytokine resistance through HSPs are reviewed.
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Zhang, Haifeng, Jiubo Cui, Weiwei Pei, and Dongfang Wang. "A CASSCF/CSAPT2 Study on the Reaction Pathways From HOSS to HSSO Radicals." E3S Web of Conferences 165 (2020): 05025. http://dx.doi.org/10.1051/e3sconf/202016505025.
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In this paper, we used the CASSCF/CASPT2 method to study the low-lying electronic states of the HOSS and HSSO radicals. Based on the Cs and C1 symmetries, the geometrical parameters, total energies, configurations, oscillator strengths, excitation energies, oscillator strengths and harmonic vibrational frequencies of the HOSS and HSSO radicals were calculated. We found that the ground state of HSSO radical with C1 symmetry has multi-configurational character, which leads to a significant difference of dihedral angles of HSSO radical among at our work and at References. Moreover, a transition state was given out in the pathway for the reaction from HOSS to HSSO. This transition state produces relatively high-energy barrier of 30.5 Kcal/mol corresponding to the gradual changes of the S2-H-O angle.
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Hoter, Rizk, and Naim. "The Multiple Roles and Therapeutic Potential of Molecular Chaperones in Prostate Cancer." Cancers 11, no. 8 (August 16, 2019): 1194. http://dx.doi.org/10.3390/cancers11081194.
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Prostate cancer (PCa) is one of the most common cancer types in men worldwide. Heat shock proteins (HSPs) are molecular chaperones that are widely implicated in the pathogenesis, diagnosis, prognosis, and treatment of many cancers. The role of HSPs in PCa is complex and their expression has been linked to the progression and aggressiveness of the tumor. Prominent chaperones, including HSP90 and HSP70, are involved in the folding and trafficking of critical cancer-related proteins. Other members of HSPs, including HSP27 and HSP60, have been considered as promising biomarkers, similar to prostate-specific membrane antigen (PSMA), for PCa screening in order to evaluate and monitor the progression or recurrence of the disease. Moreover, expression level of chaperones like clusterin has been shown to correlate directly with the prostate tumor grade. Hence, targeting HSPs in PCa has been suggested as a promising strategy for cancer therapy. In the current review, we discuss the functions as well as the role of HSPs in PCa progression and further evaluate the approach of inhibiting HSPs as a cancer treatment strategy.
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Qazi, Khaleda Rahman, Mousumi Rahman Qazi, Esther Julián, Mahavir Singh, Manuchehr Abedi-Valugerdi, and Carmen Fernández. "Exposure to Mycobacteria Primes the Immune System for Evolutionarily Diverse Heat Shock Proteins." Infection and Immunity 73, no. 11 (November 2005): 7687–96. http://dx.doi.org/10.1128/iai.73.11.7687-7696.2005.
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ABSTRACT During stress conditions, such as infection, the synthesis of heat shock proteins (HSPs) in microorganisms is upregulated. Since a high degree of homology exists within each HSP family, we postulated that exposure to microorganisms could prime the immune system for evolutionarily diverse HSPs. We tested this hypothesis by priming mice with three microorganisms, namely, Mycobacterium bovis BCG, Mycobacterium vaccae, and Chlamydia pneumoniae. After this, mice received a dose of the various HSPs. We found that BCG and M. vaccae but not C. pneumoniae primed the immune system for the induction of secondary immunoglobulin G (IgG) responses to most of the HSPs tested. Analysis of the IgG1 and IgG2a profile and gamma interferon production induced against the HSPs revealed the induction of a mixture of responses. We also observed that sera from mice treated with M. vaccae and HSP70 were cross-reactive, but no antibody complexes were observed in their kidneys, which frequently are targets for autoantibody reactions. Our findings add further support for the use of HSPs as effective vaccine adjuvants.
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Beck, Franz-X., Wolfgang Neuhofer, and Eva Müller. "Molecular chaperones in the kidney: distribution, putative roles, and regulation." American Journal of Physiology-Renal Physiology 279, no. 2 (August 1, 2000): F203—F215. http://dx.doi.org/10.1152/ajprenal.2000.279.2.f203.
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Molecular chaperones are intracellular proteins that prevent inappropriate intra- and intermolecular interactions of polypetide chains. A specific group of highly conserved molecular chaperones are the heat shock proteins (HSPs), many of which are constitutively expressed but most of which are inducible by diverse (in some cases specific) stress factors. HSPs, either alone or in cooperation with “partner” chaperones, are involved in cellular processes as disparate as correct folding and assembly of proteins, transport of proteins to specific intracellular locations, protein degradation, and preservation and restructuring of the cytoskeleton. The characteristic distribution of individual HSPs in the kidney, and their response to different challenges, suggests that a number of HSPs may fulfill specific, kidney-related functions. HSP72 and the osmotic stress protein 94 (Osp94) appear to participate in the adaptation of medullary cells to high extracellular salt and urea concentrations; the small HSPs (HSP25/27 and crystallins) may be involved in the function of mesangial cells and podocytes and contribute to the volume-regulatory remodeling of the cytoskeleton in medullary cells during changes in extracellular tonicity. HSP90 contributes critically to the maturation of steroid hormone receptors and may thus be a critical determinant of the aldosterone sensitivity of specific renal epithelial cells. Certain HSPs are also induced in various pathological states of the kidney. The observation that the expression of individual HSPs in specific kidney diseases often displays characteristic time courses and intrarenal distribution patterns supports the idea that HSPs are involved in the recovery but possibly also in the initiation and/or maintenance phases of these disturbances.
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Pandita, Tej K. "Role of HSPs and telomerase in radiotherapy." International Journal of Hyperthermia 21, no. 8 (December 2005): 689–94. http://dx.doi.org/10.1080/02656730500271700.
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A. Meenakshi, Martin, and Erik G. Seth. "Protective role of TAT-HSP70 after myocardial I/R injury." American Journal of BioMedicine 5, no. 3 (September 22, 2017): 279–84. http://dx.doi.org/10.18081/2333-5106/015-04/289-294.
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Myocardial ischemia reperfusion injury I/R adversely affects cardiac function. Heat shock proteins (HSPs) are a highly conserved family of proteins with diverse functions expressed by all cells exposed to environmental stress including myocardila injury. We investigated release of small constitutive heat shock proteins (HSPs) from mouse myocardium and the effects of TAT-HSP70 after myocardial I/R via occluding the left coronary artery (LAD). The results support the hypothesis that elevated HSPs in myocardium after ischemia and reperfusion and contributes to the inflammatory mechanism of myocardial functional injury. Further investigation of the significance of HSPs accumulation to the evolution of myocardial injury.
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Robins, Lauren, Kaprea Johnson, Alexandra Gantt, Dana Brookover, Brittany Suggs, Janelle Jones, and Megan Cannedy. " The Role of Human Services Providers in Addressing Social Determinants of Health." Journal of Human Services 40, no. 1 (March 2021): 83–101. http://dx.doi.org/10.52678/2021.6.
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Social determinants of health (SDOH) are circumstances in which people grow, live, work, and play. Unmet SDOH needs can adversely affect mental and physical health; however, to date, there are no comprehensive publications that highlight human services providers’ (HSPs’) role in addressing SDOH. This article defines SDOH, delineates HSPs’ role in addressing SDOH, and provides conceptual frameworks that can be used by HSPs to promote SDOH in practice. Special consideration is given for a collective approach that incorporates multiple frameworks to promote holistic practice and health equity. The article concludes with implications for HSPs, administrators, and educators.
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Finlayson-Trick, Emma, Jessica Connors, Andrew Stadnyk, and Johan Van Limbergen. "Regulation of Antimicrobial Pathways by Endogenous Heat Shock Proteins in Gastrointestinal Disorders." Gastrointestinal Disorders 1, no. 1 (September 28, 2018): 39–56. http://dx.doi.org/10.3390/gidisord1010005.
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Heat shock proteins (HSPs) are essential mediators of cellular homeostasis by maintaining protein functionality and stability, and activating appropriate immune cells. HSP activity is influenced by a variety of factors including diet, microbial stimuli, environment and host immunity. The overexpression and down-regulation of HSPs is associated with various disease phenotypes, including the inflammatory bowel diseases (IBD) such as Crohn’s disease (CD). While the precise etiology of CD remains unclear, many of the putative triggers also influence HSP activity. The development of different CD phenotypes therefore may be a result of the disease-modifying behavior of the environmentally-regulated HSPs. Understanding the role of bacterial and endogenous HSPs in host homeostasis and disease will help elucidate the complex interplay of factors. Furthermore, discerning the function of HSPs in CD may lead to therapeutic developments that better reflect and respond to the gut environment.
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Kregel, Kevin C. "Invited Review: Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance." Journal of Applied Physiology 92, no. 5 (May 1, 2002): 2177–86. http://dx.doi.org/10.1152/japplphysiol.01267.2001.
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Cells from virtually all organisms respond to a variety of stresses by the rapid synthesis of a highly conserved set of polypeptides termed heat shock proteins (HSPs). The precise functions of HSPs are unknown, but there is considerable evidence that these stress proteins are essential for survival at both normal and elevated temperatures. HSPs also appear to play a critical role in the development of thermotolerance and protection from cellular damage associated with stresses such as ischemia, cytokines, and energy depletion. These observations suggest that HSPs play an important role in both normal cellular homeostasis and the stress response. This mini-review examines recent evidence and hypotheses suggesting that the HSPs may be important modifying factors in cellular responses to a variety of physiologically relevant conditions such as hyperthermia, exercise, oxidative stress, metabolic challenge, and aging.
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Harrington, HM, S. Dash, N. Dharmasiri, and S. Dharmasiri. "Heat-Shock Proteins: a Search for Functions." Functional Plant Biology 21, no. 6 (1994): 843. http://dx.doi.org/10.1071/pp9940843.
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Heat-shock proteins (hsps) are synthesised in response to increased growing temperature and are thought to result in the acquisition of thermotolerance to otherwise nonpermissive temperatures. This phenomenon, called the heat-shock response (HSR), is conserved among all biological organisms. While much information is available on the regulation of heat-shock genes and the synthesis of hsps, comparatively little is known of hsp functions in cells. The current thinking is that hsps provide the molecular basis for thermotolerance although there is limited evidence to support this view. Research in our laboratory is focused on the characterisation of hsps that function in signal transduction including protein kinases and heat-shock-induced calmodulin-binding proteins. Such enzymes and proteins are likely to be involved in key regulatory mechanisms that operate during the HSR and may help to identify specific functions for HSPs.
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Waterson, Patrick, Eva-Maria Carman, Tanja Manser, and Antje Hammer. "Hospital Survey on Patient Safety Culture (HSPSC): a systematic review of the psychometric properties of 62 international studies." BMJ Open 9, no. 9 (September 2019): e026896. http://dx.doi.org/10.1136/bmjopen-2018-026896.
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ObjectiveTo carry out a systematic review of the psychometric properties of international studies that have used the Hospital Survey on Patient Safety Culture (HSPSC).DesignLiterature review and an analysis framework to review studies.SettingHospitals and other healthcare settings in North and South America, Europe, the Near East, the Middle East and the Far East.Data sourcesA total of 62 studies and 67 datasets made up of journal papers, book chapters and PhD theses were included in the review.Primary and secondary outcome measuresPsychometric properties (eg, internal consistency) and sample characteristics (eg, country of use, participant job roles and changes made to the original version of the HSPSC).ResultsJust over half (52%) of the studies in our sample reported internal reliabilities lower than 0.7 for at least six HSPSC dimensions. The dimensions ‘staffing’, ‘communication openness’, ‘non-punitive response to error’, ‘organisational learning’ and ‘overall perceptions of safety’ resulted in low internal consistencies in a majority of studies. The outcomes from assessing construct validity were reported in 60% of the studies. Most studies took place in a hospital setting (84%); the majority of survey participants (62%) were drawn from nursing and technical staff. Forty-two per cent of the studies did not state what modifications, if any, were made to the original US version of the instrument.ConclusionsWhile there is evidence of a growing worldwide trend in the use of the HSPSC, particularly within Europe and the Near/Middle East, our review underlines the need for caution in using the instrument. Future use of the HSPSC needs to be sensitive to the demands of care settings, the target population and other aspects of the national and local healthcare contexts. There is a need to develop guidelines covering procedures for using, adapting and translating the HSPSC, as well as reporting findings based on its use.