Stress Proteins: Their Detection and Uses in Biomonitoring

2009 ◽  
pp. 338-338-10 ◽  
Author(s):  
BP Bradley
Keyword(s):  
Stress Proteins

A comparison of three cryotechniques (freeze-drying, cryosubstitution, cryosectioning) of specimen preparation for immunolabelling of bacterial antigens of Coxiella burnetii

1994 ◽  
Vol 52 ◽  
pp. 140-141
Author(s):  
T. F. McCaul ◽  
R. J. Gould
Keyword(s):  
Coxiella Burnetii ◽  
Freeze Drying ◽  
Stress Proteins ◽  
Cultured Cells ◽  
High Specificity ◽  
Specimen Preparation ◽  
Bacterial Antigens ◽  
Structural Preservation ◽  
Nuclear Ribonucleoprotein ◽  
Cellular Components

Immuno-electron microscopy has allowed the selective localisation of molecules with high resolution and high specificity. Cryopreparatory methods have provided better retention of antigenicity suitable for precise immunolabelling together with optimal structural preservation of cellular components. Cryosubstitution and cryoultramicrotomy have widely been exploited for immunolabelling. Molecular Distillation Dryer (MDD), a form of freeze-drying technique, has recently been used for immunolabelling of Plasmodium falciparum stress proteins and nuclear ribonucleoprotein particles in cultured cells. In the present study, we report the comparison of all three cryotechniques in the immunolabelling of bacterial antigens of Coxiella burnetii.The highly infectious C. burnetii was prefixed in 3% glutaraldehyde (66 mM cacodylate buffer, pH 6.8 ). The cells were then pre-embedded in 2% low-temperature agarose on Durapore hydrophilic membrane prior to cryofixation using a LifeCell CF100 metal-mirror system. A 1% glutaraldehyde in 100% methanol was used as a medium for cryosubstitution in a Reichert CS Auto Cryosubstitution apparatus.

Chaperonin as the normal controls and pathological anti-stress response in the human reproductive system

2016 ◽  
pp. 126-129
Author(s):  
M. Makarenko ◽  
◽  
D. Hovsyeyev ◽  
L. Sydoryk ◽  
◽  
...  
Keyword(s):  
Reproductive System ◽  
Stress Proteins ◽  
Physiological Stress ◽  
Protein Complexes ◽  
Reproductive Function ◽  
Intercellular Signaling ◽  
Toll Like Receptors ◽  
Wide Range ◽  
Protein Functions ◽  
And Function

Different kinds of physiological stress cause mass changes in the cells, including the changes in the structure and function of the protein complexes and in separate molecules. The protein functions is determined by its folding (the spatial conclusion), which depends on the functioning of proteins of thermal shock- molecular chaperons (HSPs) or depends on the stress proteins, that are high-conservative; specialized proteins that are responsible for the correct proteinaceous folding. The family of the molecular chaperones/ chaperonins/ Hsp60 has a special place due to the its unique properties of activating the signaling cascades through the system of Toll-like receptors; it also stimulates the cells to produce anti- inflammatory cytokines, defensins, molecules of cell adhesion and the molecules of MHC; it functions as the intercellular signaling molecule. The pathological role of Hsp60 is established in a wide range of illnesses, from diabetes to atherosclerosis, where Hsp60 takes part in the regulation of both apoptosis and the autoimmune processes. The presence of the HSPs was found in different tissues that are related to the reproductive system. Key words: molecular chaperons (HSPs), Toll-like receptors, reproductive function, natural auto antibody.

Simultaneous Overexpression of Two Stress Proteins in Rat Cardiomyocytes and Myogenic Cells Confers Protection Against Ischemia-Induced Injury

Circulation ◽  
1997 ◽  
Vol 96 (7) ◽  
pp. 2287-2294 ◽  
Author(s):  
Sandy Lau ◽  
Nandita Patnaik ◽  
M. Richard Sayen ◽  
Ruben Mestril
Keyword(s):  
Stress Proteins ◽  
Myogenic Cells ◽  
Rat Cardiomyocytes

Effect of glutamine on heat-shock-induced mRNA and stress proteins

1993 ◽  
Vol 157 (2) ◽  
pp. 313-318 ◽  
Author(s):  
Itzhak Nissim ◽  
Beatrice States ◽  
Mattie Hardy ◽  
Jeanette Pleasure ◽  
Ilana Nissim
Keyword(s):  
Heat Shock ◽  
Stress Proteins

The Novel Vascular Disrupting Agent ANG501 Induces Cell Cycle Arrest and Enhances Endothelial Cell Sensitivity to Radiation

2009 ◽  
Vol 2 ◽  
pp. CGM.S2596 ◽  
Author(s):  
Shona T. Dougherty ◽  
Sean E. Walker ◽  
Peter D. Davis ◽  
Graeme J. Dougherty
Keyword(s):  
Cell Cycle ◽  
Endothelial Cells ◽  
Normal Cell ◽  
Cell Cycle Progression ◽  
Stress Proteins ◽  
Vascular Disrupting Agent ◽  
Heat Shock Stress ◽  
Cell Cycling ◽  
Vascular Disrupting

The efficacy of approaches in which vascular disrupting agents (VDA) are used in combination with conventional chemotherapy and/or radiation therapy in the treatment of cancer might be improved if there were a better understanding of the cellular and molecular changes induced in normal and malignant cells as a result of VD A exposure. Toward this goal, murine endothelial cells were treated in vitro with ANG501, a novel stilbene VDA developed in our laboratory, and alterations in gene expression determined by genome-wide microarray analysis and subsequently confirmed by Western blot analysis. Among the genes that were shown to be induced upon brief exposure to non-cytotoxic doses of ANG501 were several involved in the control of cell cycle progression and apoptosis, including p21Wafl and the heat shock/stress proteins hsp25, hsp70 and anti-B-crystallin. Reflecting such induction, functional studies confirmed that normal cell cycling is temporarily inhibited following treatment with ANG501 such that the majority of cells accumulate at the radiation-sensitive G2/M phase of the cell cycle at 6 hr. The effects were transient and by 24 hr normal cell cycling had largely resumed. Combination experiments confirmed that endothelial cells treated 6 hr previously with ANG501 were more readily killed by radiation. Importantly, significant effects were evident at clinically relevant radiation doses. Taken together these findings emphasize the need to consider the radiosensitizing activity of VD As when developing therapies in which these promising compounds are used in combination with radiation.

scholarly journals Activation of endoplasmic reticulum stress response during the development of ischemic heart disease

2006 ◽  
Vol 291 (3) ◽  
pp. H1411-H1420 ◽  
Author(s):  
Asim Azfer ◽  
Jianli Niu ◽  
Linda M. Rogers ◽  
Frances M. Adamski ◽  
Pappachan E. Kolattukudy
Keyword(s):  
Endoplasmic Reticulum ◽  
Heart Disease ◽  
Stress Response ◽  
Transgenic Mice ◽  
Ischemic Heart Disease ◽  
Er Stress ◽  
Stress Proteins ◽  
Gene Array ◽  
Ischemic Heart ◽  
Endoplasmic Reticulum Stress Response

Endoplasmic reticulum (ER) stress has been found to be associated with neurodegenerative diseases and diabetes mellitus. Whether ER stress is involved in the development of heart disease is not known. Cardiac-specific expression of monocyte chemoattractant protein-1 (MCP-1) in mice causes the development of ischemic heart disease. Here we report that microarray analysis of gene expression changes in the heart of these transgenic mice revealed that a cluster of ER stress-related genes was transcriptionally activated in the heart during the development of ischemic heart disease. The gene array results were verified by quantitative real-time PCR that showed highly elevated transcript levels of genes involved in unfolded protein response such as ER and cytoplasmic chaperones, oxidoreductases, protein disulfide isomerase (PDI) family, and ER-associated degradation system such as ubiquitin. Immunoblot analysis confirmed the expression of chaperones, PDI, and ubiquitin. Immunohistochemical analyses showed that ER stress proteins were associated mainly with the degenerating cardiomyocytes. A novel ubiquitin fold modifier (Ufm1) that has not been previously associated with ER stress and not found to be induced under any condition was also found to be upregulated in the hearts of MCP mice (transgenic mice that express MCP-1 specifically in the heart). The present results strongly suggest that activation of ER stress response is involved in the development of ischemic heart disease in this murine model.

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