scholarly journals Rapid Isolation of Extracellular Vesicles from Cell Culture and Biological Fluids Using a Synthetic Peptide with Specific Affinity for Heat Shock Proteins

PLoS ONE ◽  
2014 ◽  
Vol 9 (10) ◽  
pp. e110443 ◽  
Author(s):  
Anirban Ghosh ◽  
Michelle Davey ◽  
Ian C. Chute ◽  
Steven G. Griffiths ◽  
Scott Lewis ◽  
...  
2017 ◽  
Vol 373 (1738) ◽  
pp. 20160522 ◽  
Author(s):  
A. Graham Pockley ◽  
Brian Henderson

Extracellular cell stress proteins are highly conserved phylogenetically and have been shown to act as powerful signalling agonists and receptors for selected ligands in several different settings. They also act as immunostimulatory ‘danger signals’ for the innate and adaptive immune systems. Other studies have shown that cell stress proteins and the induction of immune reactivity to self-cell stress proteins can attenuate disease processes. Some proteins (e.g. Hsp60, Hsp70, gp96) exhibit both inflammatory and anti-inflammatory properties, depending on the context in which they encounter responding immune cells. The burgeoning literature reporting the presence of stress proteins in a range of biological fluids in healthy individuals/non-diseased settings, the association of extracellular stress protein levels with a plethora of clinical and pathological conditions and the selective expression of a membrane form of Hsp70 on cancer cells now supports the concept that extracellular cell stress proteins are involved in maintaining/regulating organismal homeostasis and in disease processes and phenotype. Cell stress proteins, therefore, form a biologically complex extracellular cell stress protein network having diverse biological, homeostatic and immunomodulatory properties, the understanding of which offers exciting opportunities for delivering novel approaches to predict, identify, diagnose, manage and treat disease. This article is part of the theme issue ‘Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective’.


2006 ◽  
Vol 411 (1) ◽  
pp. 369-372
Author(s):  
D. A. Mavletova ◽  
V. P. Reutov ◽  
V. V. Ryapolov ◽  
G. A. Dvorkin

2021 ◽  
Vol 2021 ◽  
pp. 1-15
Author(s):  
Mona G. Alharbi ◽  
Seok Hee Lee ◽  
Aaser M. Abdelazim ◽  
Islam M. Saadeldin ◽  
Mosleh M. Abomughaid

Extracellular vesicles (EVs), like exosomes, are nanosized membrane-enveloped vesicles containing different bioactive cargo, such as proteins, lipids, mRNA, miRNA, and other small regulatory RNAs. Cell-derived EVs, including EVs originating from stem cells, may capture components from damaged cells or cells impacted by therapeutic treatments. Interestingly, EVs derived from stem cells can be preconditioned to produce and secrete EVs with different therapeutic properties, particularly with respect to heat-shock proteins and other molecular cargo contents. This behavior is consistent with stem cells that also respond differently to various microenvironments. Heat-shock proteins play roles in cellular protection and mediate cellular resistance to radiotherapy, chemotherapy, and heat shock. This review highlights the possible roles EVs play in mediating cellular plasticity and survival when exposed to different physical and chemical stressors, with a special focus on the respiratory distress due to the air pollution.


1998 ◽  
Vol 66 (6) ◽  
pp. 3024-3027 ◽  
Author(s):  
M. Walid Qoronfleh ◽  
Carol A. Bortner ◽  
Paul Schwartzberg ◽  
Brian J. Wilkinson

ABSTRACT Antibodies to Staphylococcus aureus heat shock proteins (Hsps) are present in the sera of patients with S. aureus endocarditis (M. W. Qoronfleh, W. Weraarchakul, and B. J. Wilkinson, Infect. Immun. 61:1567–1570, 1993). Although these proteins are immunogenic, their role in infection has not been established. We developed a cell culture system as a model to examine the potential involvement of staphylococcal Hsps in the initial events of infection. This study supports a model in which a clinical endocarditis isolate responds to host cell signals by selectively regulating the synthesis of numerous proteins, including the stress proteins Hsp60 (GroEL homolog) and Hsp70 (DnaK homolog) and a unique 58-kDa protein.


1990 ◽  
Vol 80 (2) ◽  
pp. 301-306
Author(s):  
Tiina Vahala ◽  
Tage Eriksson ◽  
Peter Engstrom

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