Blood-brain and blood-cerebrospinal fluid passage of BRICHOS domains from two molecular chaperones in mice.
Adaptor Proteins, Signal Transducing
Amyloid beta-Peptides
/ metabolism
Animals
Blood-Brain Barrier
/ metabolism
Brain
/ metabolism
Cell Membrane Permeability
Intercellular Signaling Peptides and Proteins
Male
Membrane Proteins
/ administration & dosage
Mice
Mice, Inbred C57BL
Peptides
/ administration & dosage
Protein Domains
Pulmonary Surfactant-Associated Protein C
protein assembly
protein domain
protein misfolding
neuroscience
neurodegenerative disease
protein aggregation
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
22 02 2019
22 02 2019
Historique:
received:
20
06
2018
revised:
19
12
2018
pubmed:
2
1
2019
medline:
21
5
2019
entrez:
2
1
2019
Statut:
ppublish
Résumé
Targeting toxicity associated with β-amyloid (Aβ) misfolding and aggregation is a promising therapeutic strategy for preventing or managing Alzheimer's disease. The BRICHOS domains from human prosurfactant protein C (proSP-C) and integral membrane protein 2B (Bri2) efficiently reduce neurotoxicity associated with Aβ42 fibril formation both
Identifiants
pubmed: 30598503
pii: S0021-9258(20)39361-3
doi: 10.1074/jbc.RA118.004538
pmc: PMC6393622
doi:
Substances chimiques
Adaptor Proteins, Signal Transducing
0
Amyloid beta-Peptides
0
Intercellular Signaling Peptides and Proteins
0
Itm2b protein, mouse
0
Membrane Proteins
0
Peptides
0
Pulmonary Surfactant-Associated Protein C
0
Sftpc protein, mouse
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2606-2615Informations de copyright
© 2019 Tambaro et al.
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