HSF1 Protects Neurons through a Novel Trimerization- and HSP-Independent Mechanism

• Published in: The Journal of neuroscience Vol. 34; no. 5; pp. 1599 - 1612
• Main Authors: Verma, Pragya, Pfister, Jason A., Mallick, Sathi, D'Mello, Santosh R.
• Format: Journal Article
• Language: English
• Published: United States Society for Neuroscience 29.01.2014
• Subjects: Animals; Animals, Newborn; Apoptosis - drug effects; Apoptosis - genetics; Brain - cytology; Cells, Cultured; Chromatin Immunoprecipitation; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; Enzyme Inhibitors - pharmacology; Female; Gene Expression Regulation - drug effects; Gene Expression Regulation - genetics; Heat Shock Transcription Factors; Heat-Shock Proteins - genetics; Heat-Shock Proteins - metabolism; Humans; Male; Mice; Neurons - drug effects; Neurons - metabolism; Neuroprotective Agents - metabolism; Neuroprotective Agents - pharmacology; Niacinamide - pharmacology; Protein Multimerization - drug effects; Protein Structure, Tertiary - drug effects; Protein Structure, Tertiary - genetics; Rats; Rats, Wistar; Signal Transduction - drug effects; Signal Transduction - genetics; Time Factors; Transcription Factors - genetics; Transcription Factors - metabolism; Vitamin B Complex - pharmacology

Heat shock factor 1 (HSF1) protects neurons from death caused by the accumulation of misfolded proteins. It is believed that this protective effect is mediated by the transcriptional stimulation of genes encoding heat shock proteins (HSPs), a family of chaperones that refold or degrade misfolded pro...