Progressing neurobiological strategies against proteostasis failure: Challenges in neurodegeneration. (December 2017)
- Record Type:
- Journal Article
- Title:
- Progressing neurobiological strategies against proteostasis failure: Challenges in neurodegeneration. (December 2017)
- Main Title:
- Progressing neurobiological strategies against proteostasis failure: Challenges in neurodegeneration
- Authors:
- Amanullah, Ayeman
Upadhyay, Arun
Joshi, Vibhuti
Mishra, Ribhav
Jana, Nihar Ranjan
Mishra, Amit - Abstract:
- Graphical abstract: Highlights: Detailed analysis of proteome is crucial to understand the problem of aging and neurodegeneration. Proteome imbalance can lead to widespread aberrant protein aggregation and decline proteostasis. Systematic understanding of proteostasis can open opportunities and may diminish challenges of misfolded proteins accumulation. Natural and pharmaceutical compounds: A promising approach to repair compromised cellular proteostasis. Abstract: Proteins are ordered useful cellular entities, required for normal health and organism's survival. The proteome is the absolute set of cellular expressed proteins, which regulates a wide range of physiological functions linked with all domains of life. In aging cells or under unfavorable cellular conditions, misfolding of proteins generates common pathological events linked with neurodegenerative diseases and aging. Current advances of proteome studies systematically generates some progress in our knowledge that how misfolding of proteins or their accumulation can contribute to the impairment or depletion of proteome functions. Still, the underlying causes of this unrecoverable loss are not clear that how such unsolved transitions give rise to multifactorial challengeable degenerative pathological conditions in neurodegeneration. In this review, we specifically focus and systematically summarize various molecular mechanisms of proteostasis maintenance, as well as discuss progressing neurobiological strategies,Graphical abstract: Highlights: Detailed analysis of proteome is crucial to understand the problem of aging and neurodegeneration. Proteome imbalance can lead to widespread aberrant protein aggregation and decline proteostasis. Systematic understanding of proteostasis can open opportunities and may diminish challenges of misfolded proteins accumulation. Natural and pharmaceutical compounds: A promising approach to repair compromised cellular proteostasis. Abstract: Proteins are ordered useful cellular entities, required for normal health and organism's survival. The proteome is the absolute set of cellular expressed proteins, which regulates a wide range of physiological functions linked with all domains of life. In aging cells or under unfavorable cellular conditions, misfolding of proteins generates common pathological events linked with neurodegenerative diseases and aging. Current advances of proteome studies systematically generates some progress in our knowledge that how misfolding of proteins or their accumulation can contribute to the impairment or depletion of proteome functions. Still, the underlying causes of this unrecoverable loss are not clear that how such unsolved transitions give rise to multifactorial challengeable degenerative pathological conditions in neurodegeneration. In this review, we specifically focus and systematically summarize various molecular mechanisms of proteostasis maintenance, as well as discuss progressing neurobiological strategies, promising natural and pharmacological candidates, which can be useful to counteract the problem of proteopathies. Our article emphasizes an urgent need that now it is important for us to recognize the fundamentals of proteostasis to design a new molecular framework and fruitful strategies to uncover how the proteome defects are associated with aging and neurodegenerative diseases. A enhance understanding of progress link with proteome and neurobiological challenges may provide new basic concepts in the near future, based on pharmacological agents, linked with impaired proteostasis and neurodegenerative diseases. … (more)
- Is Part Of:
- Progress in neurobiology. Volume 159(2017:Dec.)
- Journal:
- Progress in neurobiology
- Issue:
- Volume 159(2017:Dec.)
- Issue Display:
- Volume 159 (2017)
- Year:
- 2017
- Volume:
- 159
- Issue Sort Value:
- 2017-0159-0000-0000
- Page Start:
- 1
- Page End:
- 38
- Publication Date:
- 2017-12
- Subjects:
- AAA ATPases associated with diverse cellular activities -- 17-AAG 17-N-allylamino-17-demethoxygeldanamycin -- ABC ATP-binding cassette -- ABCE1 ATP binding cassette subfamily E member 1 -- AD Alzheimer's disease -- AIF apoptosis inducing factor -- Akt Alpha serine/threonine-protein kinase -- ALS amyotrophic lateral sclerosis -- AMFR Autocrine motility factor receptor -- AMPK AMP-activated protein kinase -- Aβ Amyloid beta -- APP Amyloid precursor protein -- AQUA Absolute quantification -- ATG autophagy related gene -- Atg8 Autophagy-related protein 8 -- ATM Ataxia-telangiectasia mutated -- BAD Bcl 2 associated death -- BAG3 B-cell lymphoma 2-associated anthogene 3 -- Bax Bcl-2 associated X protein -- Bcr-Abl Breast cancer-Abelson murine leukemia viral oncogene homolog 1 -- BiP Binding immunoglobulin protein -- CAP Chaperone assisted proteasomal degradation -- cAMP Cyclic adenosine monophosphate -- CASA Chaperone-assisted selective autophagy -- Cbl-b Casitas B-lineage lymphoma B cells -- Cdc Cell division cycle -- Cdc48 cell-division cycle 48 -- CFTR Cystic fibrosis transmembrane conductance regulator -- CHIP Carboxyl terminus of Hsc70-interacting protein -- CHOP CCAAT-enhancer-binding protein homologous protein -- CLpP Clp protease proteolytic subunit -- CMA Chaperone mediated autophagy -- CpdA 3′, 5′-cyclic AMP phosphodiesterase -- CRBN cereblon -- Cue1 Coupling of ubiquitin conjugation to ER degradation protein 1 -- Derlin-1 Degradation in endoplasmic reticulum protein 1 -- DHA Docosahexaenoic acid -- DIGE Difference gel electrophoresis -- DIP Database of interacting proteins -- DNA-PK DNA-dependent protein kinase -- Doa10 degradation of alpha2-10 -- DUBs Deubiquitinating enzymes -- eIF2alpha Eukaryotic translation initiation factor -- ER Endoplasmic reticulum -- ERAD Endoplasmic reticulum associated degradation -- ERKs Extracellular signal–regulated kinases -- ETC Electron transport chain -- FAD Flavin adenine dinucleotide -- FOXO forkhead Box O -- GABA γ-aminobutyric acid -- GPCR G-protein-coupled receptor -- GRP78 Glucose regulated protein 78 -- GRP94 Glucose-regulated protein 94 -- Gp78 Glycoprotein 78 -- HD Huntington's disease -- HDAC6 histone deacetylase 6 -- hDJ-1 Human DJ-1 -- HDM2 Human Mdm2 -- HIV Human immunodeficiency virus -- Hel2 Histone E3 ligase -- HEWL Hen egg white lysozyme -- Hrd1 HMG-CoA reductase degradation protein 1 -- Hsc70 Heat shock cognate 70 -- HspB8 Heat shock protein B8 -- Hsp40 Heat shock protein 40 -- Hsp70 Heat shock protein 70 -- Hsp90 Heat shock protein 90 -- Hsp26 Heat shock protein 26 -- Hsp100 Heat shock protein 100 -- HSF1 Heat shock transcription factor 1 -- HSR heat shock response -- HSV-1 Herpes simplex virus-1 -- HTRA2 High temperature requirement protease alpha 2 -- IGF-1 insulin/insulin growth factor 1 -- IRE1 Inositol-requiring enzyme 1 -- IM Intermembrane -- Inpp5a Inositol polyphosphate-5-phosphatase A -- IPOD Insoluble protein deposit -- iTRAQ Isobaric tag for relative and absolute quantification -- JUNQ/INQ Juxtanuclear quality control compartment LAMP-2A Lysosome-associated membrane protein type 2A -- LC3 Light chain 3 -- LONP Lon protease homologue -- MA Macroautophagy -- MALDI-TOF Matrix-assisted laser desorption ionization time-of-flight -- MAPK Mitogen-activated protein kinase -- Mcl-1 Myeloid cell leukemia 1 -- MEK MAPK/ERK kinase -- MGRN1 Mahogunin ring finger 1 -- MIPS Munich information centre for protein sequences -- mRNA messenger RNA -- MS mass spectrometry -- Mtb Mycobacterium tuberculosis -- mTOR mammalian target of rapapmycin -- mtQC mitochondrial quality control -- MAO-B Monoamine oxidase B -- MuRF1 Muscle ring finger 1 -- MUTHY mutY Homolog -- NAC Nascent polypeptide-associated complex -- NADPH Nicotinamide adenine dinucleotide phosphate -- NBD2 Nucleotide binding domain 2 -- NDDs Neurodegenerative diseases -- NF-κβ Nuclear factor kappa B -- Nox4 NADPH Oxidase 4 -- NSAIDs Nonsteroidal anti-inflammatory drug -- OA Oleic acid -- OGG1 8-Oxoguanine DNA Glycosylase -- OMM Outer mitochondrial membrane -- PA Palmitic acid -- PARP1 Protein poly (ADP-ribose) polymerase 1 -- PEDRo Proteomics experiment data repository -- PERK Protein kinase-like endoplasmic reticulum kinase -- PD Parkinson's disease -- PDI Protein disulfide isomerase -- PINK1 PTEN-induced putative kinase 1 -- PI3K Phosphatidylinositol-3-kinase -- PQC Protein quality control -- Protacs Proteolysis Targeting Chimeras -- QC Quality control -- RAC Ribosome-associated complex -- RES Resveratrol -- RNPs Ribonucleoproteins -- RML Rocky Mountain Laboratory -- ROS Reactive oxygen species -- SCF Skp1-cullins-f-box proteins -- Sch9/Akt serine/threonine-protein kinase -- SELDI-MS Surface-Enhanced Laser Desorption–Ionization Mass Spectrometry -- sHSPs small heat shock proteins -- Siah2 Seven in absentia homolog protein 2 -- SILAC Stable isotope labeling by amino acids in cell culture -- SIRT1 Sirutin 1 -- SOD1 Superoxide dismutase 1 -- SUMO Small ubiquitin like modifiers -- TDP43 TAR DNA binding protein 43 -- TOR target of rapamycin -- TRAF6 TNF receptor associated factor 6 -- TSC2 Tuberous sclerosis protein 2 -- TTR Transthyretin -- Ubc1/7 Ubiquitin conjugating enzyme 1/7 -- UCHL5 Ubiquitin carboxyl-terminal hydrolase isozyme L5 -- Uev1a Ubiquitin-conjugating enzyme E2 variant 1A -- UPR Unfolded protein response -- UPRER and UPRmt unfolded protein response of endoplasmic reticulum and mitochondria -- UPS Ubiquitin proteasome system -- USP Ubiquitin specific protease -- XBP-1 X-box binding protein 1
Proteostasis -- Neurodegeneration -- Aging -- Natural products -- Pharmacological agents
Neurobiology -- Periodicals
Neurology -- Periodicals
Neurology -- Periodicals
Neurobiologie -- Périodiques
612.8 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03010082 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.pneurobio.2017.08.005 ↗
- Languages:
- English
- ISSNs:
- 0301-0082
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6870.300000
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