scholarly journals Molecular mechanisms of heat shock proteins (HSPs) involved in neoplasm development

2019 ◽  
Vol 34 (2) ◽  
pp. 455-474
Author(s):  
Rafael Guerrero-Rojas ◽  
Carlos Guerrero-Fonsecaz
2003 ◽  
Vol 66 (11) ◽  
pp. 2045-2050 ◽  
Author(s):  
YI ZHANG ◽  
MANSEL W. GRIFFITHS

Heat shock proteins play an important role in protecting bacterial cells against several stresses, including starvation. In this study, the promoters for two genes encoding heat shock proteins involved in many stress responses, UspA and GrpE, were fused with the green fluorescent protein (gfp) gene. Thus, the expression of the two genes could be quantified by measuring the fluorescence emitted by the cells under different environmental conditions. The heat resistance levels of starved and nonstarved cells during storage at 5, 10, and 37°C were compared with the levels of expression of the uspA and grpE genes. D52-values (times required for decimal reductions in count at 52°C) increased by 11.5, 14.6, and 18.5 min when cells were starved for 3 h at 37°C, for 24 h at 10°C, and for 2 days at 5°C, respectively. In all cases, these increases were significant (P < 0.01), indicating that the stress imposed by starvation altered the ability of E. coli O157:H7 to survive subsequent heat treatments. Thermal tolerance was correlative with the induction of UspA and GrpE. At 5°C, the change in the thermal tolerance of the pathogen was positively linked to the induced expression of the grpE gene but negatively related to the expression of the uspA gene. The results obtained in this study indicate that UspA plays an important role in starvation-induced thermal tolerance at 37°C but that GrpE may be more involved in regulating this response at lower temperatures. An improvement in our understanding of the molecular mechanisms involved in these cross-protection responses may make it possible to devise strategies to limit their effects.


2018 ◽  
Vol 21 (5) ◽  
pp. 364-375 ◽  
Author(s):  
Ivan I. Dedov ◽  
Vsevolod A. Tkachuk ◽  
Nikolai B. Gusev ◽  
Vladimir P. Shirinsky ◽  
Aleksandr V. Vorotnikov ◽  
...  

Type 2 diabetes mellitus (T2DM) is a socially important disease with only symptomatic therapy developed due to lack of knowledge about its pathogenesis and underlying mechanism. Insulin resistance (IR) is the first link of T2DM pathogenesis and results in decrease of ability of insulin to stimulate glucose uptake by target cells. Development of IR involves genetic predisposition, excessive nutrition, stress, obesity or chronic inflammation due to disruption of insulin signaling within cells. Molecular mechanisms and markers of IR are characterized rather poorly, which prevents early diagnosis and creation of preventive therapy. Euglycemic clamp test is still a golden standard for IR diagnosis in clinic. Hyperglycemia is a distant consequence of IR in which damaging effect of oxidative and carbonyl stress is realized and diagnosis of T2DM is stipulated. Molecular chaperones and small heat-shock proteins have a protective effect at the early stages of T2DM pathogenesis, preventing development of reticulum stress and apoptosis. Endothelial dysfunction is related to T2DM and its cardiovascular complications, however, it is unknown on which stage of pathogenesis these changes occur and what are their molecular inductors. Finally, transcriptional activity and adipogenic differentiation play an important role in formation of new fat depots from predecessor cells and activation of brown and beige fat demonstrating hypolipidemic and hypoglycemic properties. The aim of this study was investigation of pathophysiological mechanisms of development of IR and endothelial dysfunction, role of transcription factor Prep1 and small heat shock proteins, evaluation of novel methods of diagnostics of IR and therapeutic potential of brown and beige fat, determination of biotargets for new antidiabetic drugs.


Author(s):  
Maria Kidwai ◽  
Puja Singh ◽  
Prasanna Dutta ◽  
Khushboo Chawda ◽  
Debasis Chakrabarty

1983 ◽  
Vol 61 (6) ◽  
pp. 387-394 ◽  
Author(s):  
R. M. Tanguay

The induction by thermal stress of certain specific genes (heat-shock genes) first described in Drosophila has recently been observed in a wide variety of unicellular and multicellular organisms, emphasizing the basic importance of this ubiquitous response. Recent data dealing with the molecular mechanisms involved in the intensive transcriptional and posttranscriptional regulation during heat shock is reviewed with emphasis on the induction of the response and the putative function of the heat-shock proteins. A model showing the various interactions of cellular regulatory mechanisms operating in the heat-shocked cell is presented. While the list of agents or treatments inducing heat-shock proteins (hsp's) in various organisms is increasing, the identification of a hypothetical common inducing factor is elusive. The recently described reorganization of some cytoskeletal elements upon heat shock is discussed both in terms of its potential involvement in transcriptional and (or) translational regulation and of its putative relation with the cellular localization of the hsp's. Studies on the cellular localization of hsp's in various organisms do not show a clear uniform pattern which could help in elucidating the function of hsp's. On the other hand, studies on the thermal resistance of various cells types show a strong correlation between the induction of hsp's and the development of transitory thermotolerance. Such a protective function for hsp's can probably be extended to other types of cellular aggression.


2010 ◽  
Vol 92 (2) ◽  
pp. 184-211 ◽  
Author(s):  
R. Anne Stetler ◽  
Yu Gan ◽  
Wenting Zhang ◽  
Anthony K. Liou ◽  
Yanqin Gao ◽  
...  

2014 ◽  
Vol 13 (1) ◽  
pp. 116 ◽  
Author(s):  
Ingvild Haaland ◽  
Jill A Opsahl ◽  
Frode S Berven ◽  
Håkon Reikvam ◽  
Hanne K Fredly ◽  
...  

2019 ◽  
Vol 46 (5) ◽  
pp. 417 ◽  
Author(s):  
Dan He ◽  
Xue-Yuan Lou ◽  
Song-Lin He ◽  
Ya-Kai Lei ◽  
Bo-Va Lv ◽  
...  

Interspecific hybridisation is the main method for improvement and breeding of tree peony (Paeonia ostii T.Hong & J.X.Zhang), but cross-incompatibility as the major factor restricting the rapid development of interspecific hybridisation. To better understand the molecular mechanisms involved in cross-incompatibility between tree peony (Paeonia ostii cv. Fengdanbai) and herbaceous peony (Paeonia lactiflora Pall. cv. Fenyunu), a quantitative proteomic analysis using isobaric tags for relative and absolute quantitation (iTRAQ) technology was performed on the stigma 24h after pollination. Of the 2900 proteins whose levels were quantitated, 685 proteins were differentially expressed in the stigma after hybrid pollination, in contrast to self-pollination. Functional annotation analysis showed that dysregulated proteins involved in RNA degradation, the Ca signalling pathway, the phosphatidylinositol signalling system and the mitogen-activated protein kinase (MAPK) signalling pathway may have made contributions to cross-incompatibility. The downregulated expression of enolase, DnaK (Heat Shock Proteins, HSP70), GroEL (Heat Shock Proteins, HSP60), calmodulin and glyoxalase I, and the upregulated expression of adenine nucleotide translocator indicated that the energy synthesis required by pollen tube growth, the signal pathway and the metabolic pathway related to the growth polarity of the pollen tube were blocked after hybrid pollination. Eight genes were selected to confirm their expression by quantitative real-time PCR. Compared with the STRING database, a protein–protein interaction network of the chosen proteins was constructed. These results provide fundamental and important information for research into the molecular mechanisms of cross-incompatibility in peony and should facilitate interspecific hybridisation in agricultural practice.


2016 ◽  
Vol 66 (3-4) ◽  
pp. 321-333 ◽  
Author(s):  
Yunyun Cheng ◽  
Songcai Liu ◽  
Ying Zhang ◽  
Dan Su ◽  
Gang Wang ◽  
...  

Heat stress dramatically decreases bull sperm quality and has recently received more attention due to the warmer global climate and more intensive production. However, no data exist regarding sperm quality or the related molecular mechanisms under heat stress. Recent studies showed that inducible heat shock proteins (HSPs) play an important role in the dairy heat stress regulation. In this article, to investigate the impacts of heat stress on sperm quality and the associated molecular mechanisms, sperm quality and enzyme activities concerning acrosome reaction were assessed in Simmental, Limousin and Yanbian bulls under heat stress. Subsequently, changes in heat shock protein expression profiles of Simmental bulls were observed, because we observed that sperm quality of these bulls was most sensitive to heat stress. Finally, the relationship between sperm quality and heat shock protein expression under heat stress was analyzed. The results show that summer heat stress decreased the sperm quality of the three bull breeds significantly. Moreover, different levels of heat stimulation induced various enzyme activity changes, among which the activity change in acrosomal enzyme was the most remarkable. Furthermore, the expression of heat shock proteins in the sperm was influenced by the imposed heat stress, among which the expression levels of HSP60 and HSP70 were increased while HSP90 decreased. In summary, our data show that heat stress seriously affects sperm quality and that HSP90 was most sensitive, although it should be noted that seasonal effects may confound these results. This change in heat shock protein expression may be the major factor that affected the sperm quality of the bulls. The findings may provide a new hypothesis for how heat stress impacts reproduction mechanistically.


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