Heat shock proteins (HSPs) are induced in response to many injuries including stroke, neurodegenerative disease, epilepsy, andtrauma. The overexpression of one HSP in particular, Hsp70, serves a protective role in several different models of nervoussystem injury, but has also been linked to a deleterious role in some diseases. Hsp70 functions as a chaperone and protectsneurons from protein aggregation and toxicity (Parkinson disease, Alzheimer disease, polyglutamine diseases, and amyotrophiclateral sclerosis), protects cells from apoptosis (Parkinson disease), is a stress marker (temporal lobe epilepsy), protects cells frominflammation (cerebral ischemic injury), has an adjuvant role in antigen presentation and is involved in the immune response inautoimmune disease (multiple sclerosis). The worldwide incidence of neurodegenerative diseases is high. As neurodegenerativediseases disproportionately affect older individuals, disease-related morbidity has increased along with the general increase inlongevity. An understanding of the underlying mechanisms that lead to neurodegeneration is key to identifying methods ofprevention and treatment. Investigators have observed protective effects of HSPs induced by preconditioning, overexpression,or drugs in a variety of models of brain disease. Experimental data suggest that manipulation of the cellular stress response mayoffer strategies to protect the brain during progression of neurodegenerative disease.
|Numero di pagine||18|
|Rivista||Biochemistry Research International|
|Stato di pubblicazione||Published - 2011|
All Science Journal Classification (ASJC) codes