Welcome to cider

Field	Query

Alzheimer disease
Amyotrophic lateral sclerosis
Autism
Bipolar disorder
COXPD
Cancer
Cardiovascular diseases
Diabetes mellitus, type II
Epilepsy
Farber lipogranulomatosis
Inflammatory bowel disease
Lung disease
Major depressive disorder
Multiple sclerosis
Muscular atrophy
Neutropenia, severe congenital
Other
Parkinson disease
Post-traumatic stress disorder
Postpartum depression
Rare disease
Schizophrenia

	Field	Term

General Information:

Id:	479 (click here to show other Interactions for entry)
Diseases:	Parkinson disease
Organism:	Homo sapiens
Tissue/Cell line:	BTO:0001009 PC-12 cell
Publication type:	article
Reference:	Cuervo AM et al.(2004) Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 305: 1292-1295 [PMID: 15333840]

Interaction Information:

Comment	In PC-12 cells serum removal activates both macroautophagy and chaperone-mediated autophagy (CMA).
Formal Description Interaction-ID: 2249	process response to starvation increases_activity of process macroautophagy

Comment	In PC-12 cells serum removal activates both macroautophagy and chaperone-mediated autophagy (CMA).
Formal Description Interaction-ID: 2250	process response to starvation increases_activity of process autophagy

Comment	Wild-type alpha-synuclein is internalized and degraded in lysosomes by CMA.
Formal Description Interaction-ID: 2257	process autophagy decreases_quantity of gene/protein SNCA

Comment	Both A30P and A53T mutant alpha-synucleins bound intact lysosomes more strongly than did the wild-type protein, but the mutants were poorly internalized, thus impairing the degradation of other CMA substrates.
Formal Description Interaction-ID: 2266	gene/protein mutant SNCA-p.A30P decreases_activity of process autophagy

Comment	Both A30P and A53T mutant alpha-synucleins bound intact lysosomes more strongly than did the wild-type protein, but the mutants were poorly internalized, thus impairing the degradation of other CMA substrates.
Formal Description Interaction-ID: 2267	gene/protein mutant SNCA-p.A53T decreases_activity of process autophagy

Comment	Wild-type alpha-synuclein is internalized and degraded in lysosomes by CMA, but the pathogenic alpha-synuclein mutations are poorly degraded by CMA despite a high affinity for the CMA receptor LAMPB.
Formal Description Interaction-ID: 2268	process autophagy NOT decreases_quantity of gene/protein mutant SNCA-p.A30P

Comment	Wild-type alpha-synuclein is internalized and degraded in lysosomes by CMA, but the pathogenic alpha-synuclein mutations are poorly degraded by CMA despite a high affinity for the CMA receptor LAMPB.
Formal Description Interaction-ID: 2269	process autophagy NOT decreases_quantity of gene/protein mutant SNCA-p.A53T

Home
Contact

The Helmholtz Zentrum München Imprint and Privacy Policy apply.

© 2013 - Helmholtz Zentrum München - German Research Center for Environmental Health (GmbH) Ingolstädter Landstraße 1, D-85764 Neuherberg, Germany

Disclaimer: IBIS Databases and associated information are protected by copyright. This server and its associated data and services are for academic, non-commercial use only. The Helmholtz Zentrum München has no liability for the use of results, data or information which have been provided through this server. Neither the use for commercial purposes, nor the redistribution of IBIS database files to third parties nor the distribution of parts of files or derivative products to any third parties is permitted. Commercial users shall contact the Helmholtz Zentrum München for a separate users license.