Roles of the endoplasmic reticulum-resident, collagen-specific molecular chaperone Hsp47 in vertebrate cells and human disease.
FKBP65
IRE1alpha
Osteogenesis imperfecta
TANGO1
collagen
endoplasmic reticulum (ER)
fibrosis
heat shock protein (HSP)
molecular chaperone
serpin
thrombosis
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:
08 02 2019
08 02 2019
Historique:
pubmed:
14
12
2018
medline:
27
6
2019
entrez:
14
12
2018
Statut:
ppublish
Résumé
Heat shock protein 47 (Hsp47) is an endoplasmic reticulum (ER)-resident molecular chaperone essential for correct folding of procollagen in mammalian cells. In this Review, we discuss the role and function of Hsp47 in vertebrate cells and its role in connective tissue disorders. Hsp47 binds to collagenous (Gly-Xaa-Arg) repeats within triple-helical procollagen in the ER and can prevent its local unfolding or aggregate formation, resulting in accelerating triple-helix formation of procollagen. Hsp47 pH-dependently dissociates from procollagen in the
Identifiants
pubmed: 30541925
pii: S0021-9258(20)36857-5
doi: 10.1074/jbc.TM118.002812
pmc: PMC6369284
doi:
Substances chimiques
HSP47 Heat-Shock Proteins
0
HSP70 Heat-Shock Proteins
0
HSP90 Heat-Shock Proteins
0
SERPINH1 protein, human
0
Serpinh1 protein, mouse
0
Collagen
9007-34-5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
2133-2141Informations de copyright
© 2019 Ito and Nagata.
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