Heat shock proteins and immunity (CROSBI ID 37580)
Prilog u knjizi | izvorni znanstveni rad
Podaci o odgovornosti
Barišić, Karmela
engleski
Heat shock proteins and immunity
Heat shock response is a universal biological phenomenon of cellular defence under various types of stress. It consists of rapid induction of a specific set of genes encoding cytoprotective proteins named stress proteins or heat shock proteins (HSPs). Hsps are highly conserved proteins found in all prokaryotes and eukaryotes. In normal physiological conditions, Hsps are expressed at a low level. They are increased under a wide variety of stressful stimuli, including heat, toxic chemicals, heavy metals and inhibitors of energy metabolism, viral and bacterial pathogens, oxidant injury, ischemia, aging, and cancer. The heat shock response to stress serves to protect the cell from the effects of abnormally folded proteins and protein aggregation. Various Hsps act as molecular chaperons helping the other cellular proteins achieve their correct folding, reach their final destination and resist denaturing by stressors. Being involved in protein folding, translocation and assembly, they have emerged as important players in diverse biological processes, such as regulation of cytoskeletal structure, cell adhesion, migration, proliferation, cell death and cell signalling. In a pathological situation, such as necrotic cell death, Hsps can be released into the extracellular environment complexed with cellular proteins. Hsp-cellular protein complexes can induce autoimmunity by receptor-mediated activation of the innate immune response and by participation in the presentation of autoantigens for adaptive immune response. Conservation of Hsps through prokaryotes and eukaryotes and increased production of host and microbial Hsps at the site of infection provide a link between infection and autoimmunity. According to their roles in antigen processing and presentation, Hsps have also the ability to carry tumour antigens and generate protective immunity against live tumour challenge. Hsp induction could be beneficial in overcoming immunosuppressive mechanisms of the tumour and in breaking tolerance to tumour antigens. This has offered new possibilities of tumour vaccine development. Moreover, it was reported that tumur derived Hsp-peptide complexes induced a powerful immune response, and could be used as effective prophylactic and therapeutic agents, even in poorly immunogenic cancer. This review summarizes the Hsp involvement in signal transduction pathways and immunological processes by focusing on Hsps as challenging targets and/or effectors of immune system-based therapy against autoimmune and cancer diseases.
Heat shock protein (Hsp), chaperon, stress, immunity
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Podaci o prilogu
29-36.
objavljeno
Podaci o knjizi
Biochemistry and Immunology Intersections
Markotić, Anita ; Glavaš-Obrovac, Ljubica ; Varljen, Jadranka ; Žanić-Grubišić, Tihana
Lahti: Research Signpost
2008.
978-81-308-0265-7