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HSPs - Ambiguous Mediators of Immunity

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Book Series: Frontiers Research Topics ISSN: 16648714 ISBN: 9782889451524 Year: Pages: 92 DOI: 10.3389/978-2-88945-152-4 Language: English
Publisher: Frontiers Media SA
Subject: Allergy and Immunology --- Medicine (General)
Added to DOAB on : 2017-08-28 14:01:09
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Heat shock proteins (HSPs) were discovered as polypeptides induced by stress that can be found in all kingdoms of cellular organisms. Their functions were, a first enigmatic and these proteins were thus classified by molecular weight, as in—Hsp27, Hsp70, Hsp90, Hsp110. More recently, each of these size-classified molecules has attributed a role in protein folding, and they thus came to be known, as a class, as molecular chaperones. However, the they possess properties beyond chaperoning. Indeed, their discovery in the extracellular spaces suggested roles in regulation of the immune responses.

The immunology of cellular stress proteins

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Book Series: Frontiers Research Topics ISSN: 16648714 ISBN: 9782889193257 Year: Pages: 89 DOI: 10.3389/978-2-88919-325-7 Language: English
Publisher: Frontiers Media SA
Subject: Allergy and Immunology --- Medicine (General)
Added to DOAB on : 2016-03-10 08:14:32
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Stress proteins or heat-shock proteins (HSP) are evolutionary conserved proteins present in every prokaryotic and eukaryotic cell. Their main function is to protect cells and proteins from damage under stressful circumstances. The latter circumstances do include the cell and protein damaging effects of inflammation. The discovery of mycobacterial HSP60 being a critical antigen in the model of adjuvant arthritis, has led to studies that showed the immuno-dominance of microbial HSP60 and the potential of the microbial HSP induced repertoire of antibodies and T cells to cross-recognize the self-HSP homologues of stressed cells. Since then, the research in the immunology of stress proteins started to comprise a widening spectrum of topics with potential medical relevance. Interestingly, since stress proteins have their activities in both innate and adaptive immunity, they are key elements in the cross-roads between both arms of the immune system. Stress proteins or HSP can be considered as functional 'biomarkers' of inflammation. They are up-regulated locally during inflammation and interestingly, they seem to function as targets for anti-inflammatory regulatory T cells. In experimental models of autoimmunity, mainly arthritis, administration of HSP peptides have been shown to suppress disease. First clinical trials have shown the anti-inflammatory nature of T cell responses to Hsp. In type I diabetes and in rheumatoid arthritis, parenteral and oral administration of Hsp peptides were shown to induce a bias in pro-inflammatory T cells, switching them in the direction of regulatory cytokine production (IL4, IL5 and IL10). In addition a raised level of a marker of natural T regulatory cells, the transcription factor FoxP3, was noted in the RA trial. Other inflammatory diseases or diseases with inflammatory components which feature the immune imprint of the up-regulated Hsp are atherosclerosis, inflammatory bowel diseases, multiple sclerosis and atopic diseases such atopic dermatitis and allergic asthma.

The HSP70 Molecular Chaperone Machines

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Book Series: Frontiers Research Topics ISSN: 16648714 ISBN: 9782889451258 Year: Pages: 69 DOI: 10.3389/978-2-88945-125-8 Language: English
Publisher: Frontiers Media SA
Subject: Science (General)
Added to DOAB on : 2017-07-06 13:27:36
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Members of the HSP70 family form a central hub of the molecular chaperone network, controlling protein homeostasis in prokaryotes and in the ATP-containing compartments of the eukaryotic cells. The heat-inducible form HSPA1A (HSP70), its constitutive cytosolic cognate HSPA8 (Hsc70), its endoplasmic reticulum form HSPA5 (BiP), and its mitochondrial form HSPA9 (Mortalin), as well as the more distantly related HSPHs (HSP110s), make up 1-2 % of the total mass of proteins in human cells. They use the energy of ATP-hydrolysis to prevent and forcefully revert the process of protein misfolding and aggregation during and following various stresses, presumably by working as unfoldases to lift aberrant conformers out of kinetic traps. As such, HSP70s, in cooperation with their J-domain co-chaperones and nucleotide exchange factors (NEFs) and co-disaggregases, form an efficient network of cellular defenses against the accumulation of cytotoxic misfolded protein conformers, which may cause degenerative diseases such as Parkinson's and Alzheimer's disease, diabetes, and aging in general. In addition to their function in repair of stress-induced damage, HSP70s fulfill many housekeeping functions, including assisting the de novo folding and maturation of proteins, driving the translocation of protein precursors across narrow membrane pores into organelles, and by controlling the oligomeric state of key regulator protein complexes involved in signal transduction and vesicular trafficking. For reasons not well understood, HSP70s are also found on the surface of some animal cells, in particular cancer cells where they may serve as specific targets for cancer immunotherapy. Here, we gathered seven mini reviews, each presenting a complementary aspect of HSP70’s structure and function in bacteria and eukaryotes, under physiological and stressful conditions. These articles highlight how, the various members of this conserved family of molecular chaperones, assisted by their various J-domain and NEF cochaperones and co-disaggregases, harness ATP hydrolysis to perform a great diversity of life-sustaining cellular functions using a similar molecular mechanism.

Protein Quality Controlling Systems in Plant Responses to Environmental Stresses

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Book Series: Frontiers Research Topics ISSN: 16648714 ISBN: 9782889455584 Year: Pages: 214 DOI: 10.3389/978-2-88945-558-4 Language: English
Publisher: Frontiers Media SA
Subject: Science (General) --- Botany
Added to DOAB on : 2019-01-23 14:53:42
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Environmental stress factors negatively affect plant growth by inducing proteins dysfunction. As coping strategies, plant have developed a comprehensive protein quality controlling system (PQCS) to keep proteins homeostasis. In this research topic of “Protein Quality Controlling Systems in Plant Responses to Environmental Stresses”, some latest researches and opinions in this field, including heat shock proteins (HSPs), unfolded protein response (UPR), ubiquitin-proteasome system (UPS) and autophagy, were reported, aiming to provide novel insights for increasing crop production under environmental challenges.

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