Biomaterial Database

Molecular chaperones and neuronal proteostasis. 2015

Heather L Smith, and Wenwen Li, and Michael E Cheetham

UCL Institute of Ophthalmology, 11-43 Bath Street, London EC1V 9EL, UK.

Protein homeostasis (proteostasis) is essential for maintaining the functionality of the proteome. The disruption of proteostasis, due to genetic mutations or an age-related decline, leads to aberrantly folded proteins that typically lose their function. The accumulation of misfolded and aggregated protein is also cytotoxic and has been implicated in the pathogenesis of neurodegenerative diseases. Neurons have developed an intrinsic protein quality control network, of which molecular chaperones are an essential component. Molecular chaperones function to promote efficient folding and target misfolded proteins for refolding or degradation. Increasing molecular chaperone expression can suppress protein aggregation and toxicity in numerous models of neurodegenerative disease; therefore, molecular chaperones are considered exciting therapeutic targets. Furthermore, mutations in several chaperones cause inherited neurodegenerative diseases. In this review, we focus on the importance of molecular chaperones in neurodegenerative diseases, and discuss the advances in understanding their protective mechanisms.

UI	MeSH Term	Description	Entries
D011506	Proteins	Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.	Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D006360	Heat-Shock Proteins	Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other environmental stresses. They increase thermal tolerance and perform functions essential to cell survival under these conditions.	Stress Protein,Stress Proteins,Heat-Shock Protein,Heat Shock Protein,Heat Shock Proteins,Protein, Stress
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D018832	Molecular Chaperones	A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.	Chaperones, Molecular,Chaperone, Molecular,Molecular Chaperone
D019636	Neurodegenerative Diseases	Hereditary and sporadic conditions which are characterized by progressive nervous system dysfunction. These disorders are often associated with atrophy of the affected central or peripheral nervous system structures.	Degenerative Diseases, Nervous System,Degenerative Diseases, Central Nervous System,Degenerative Diseases, Neurologic,Degenerative Diseases, Spinal Cord,Degenerative Neurologic Diseases,Degenerative Neurologic Disorders,Nervous System Degenerative Diseases,Neurodegenerative Disorders,Neurologic Degenerative Conditions,Neurologic Degenerative Diseases,Neurologic Diseases, Degenerative,Degenerative Condition, Neurologic,Degenerative Conditions, Neurologic,Degenerative Neurologic Disease,Degenerative Neurologic Disorder,Neurodegenerative Disease,Neurodegenerative Disorder,Neurologic Degenerative Condition,Neurologic Degenerative Disease,Neurologic Disease, Degenerative,Neurologic Disorder, Degenerative,Neurologic Disorders, Degenerative
D066263	Protein Aggregation, Pathological	A biochemical phenomenon in which misfolded proteins aggregate either intra- or extracellularly. Triggered by factors such as MUTATION; POST-TRANSLATIONAL MODIFICATIONS, and environmental stress, it is generally associated with ALZHEIMER DISEASE; PARKINSON DISEASE; HUNTINGTON DISEASE; and TYPE 2 DIABETES MELLITUS.	Aggregation, Pathological Protein,Pathological Protein Aggregation