Dysfunction of constitutive and inducible ubiquitin-proteasome system in amyotrophic lateral sclerosis: Implication for protein aggregation and immune response

Article ID	Journal	Published Year	Pages	File Type
6286592	Progress in Neurobiology	2012	26 Pages	PDF

Abstract

âº Degenerating motoneuron in ALS accumulate abnormal protein aggregates. âº Ubiquitin-proteasome system (UPS) is altered by mutant SOD1-linked familial ALS. âº Possible link between UPS alterations in motoneuron and immune reactions in ALS.

Keywords

VCP Cys SFN EAE NMJ IFN-γ HSPs NSC34 cells Optineurin SOD1 FTLD TDP-43 TNFα SLI RHI OPTN SALS MHC I PDTC UCHL1 DUB D3T UBQLN2 Nrf2 ERAD TLS SUMO FUs Astrocyte deubiquitinating enzyme experimental autoimmune encephalomyelitis Neuromuscular junction amyotrophic lateral sclerosis Sporadic amyotrophic lateral sclerosis translocated in liposarcoma Alzheimer's disease ALS Huntington's disease Parkinson's disease endoplasmic reticulum-associated degradation Oxidative stress Neurodegeneration tumor necrosis factor alpha fALS fused in sarcoma Immune system CNS pyrrolidine dithiocarbamate Sulforaphane superoxide dismutase 1 Superoxide dismutase Cysteine Ubiquitin-proteasome system central nervous system endoplasmic reticulum Spinal cord Nuclear factor-erythroid 2-related factor 2 skein-like inclusion T lymphocytes Lysine LYS Transgenic mice Microglia Motor neuron wild type ARE Valosin-containing protein tar DNA-binding protein 43 Heat shock proteins CHiP Major histocompatibility complex class I small ubiquitin-like modifier Interferon gamma Gly Glycine UPS