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Association of Hsp47, Grp78, and Grp94 with procollagen supports the successive or coupled action of molecular chaperones
- Source :
- Journal of Cellular Biochemistry. 56:518-526
- Publication Year :
- 1994
- Publisher :
- Wiley, 1994.
-
Abstract
- Hsp47, Grp78, and Grp94 have been implicated with procollagen maturation events. In particular, Hsp47 has been shown to nascent procollagen alpha 1(I) chains in the course of synthesis and/or translocation into the endoplasmic reticulum (ER). Although, Hsp47 binding to gelatin and collagen has previously been suggested to be independent of ATP. Grp78 and Grp94 are known to dissociate from its substrates by an ATP-dependent release mechanism. The early association of Hsp47 with procollagen and its relatively late release suggested that other chaperones, Grp78 and Grp94, interact successively or concurrently with Hsp47. Herein, we examined how these events occur in cells metabolically stressed by depletion of ATP. In cells depleted of ATP, the release of Hsp47, Grp78, and Grp94 from maturing procollagen is delayed. Thus, in cells experiencing metabolic stress, newly synthesized procollagen unable to properly fold became stably bound to a complex of molecular chaperones. In that Hsp47, Grp78, and Grp94 could be recovered with nascent procollagen and as oligomers in ATP depleted cells suggests that these chaperones function in a series of coupled or successive reactions.
- Subjects :
- Carbonyl Cyanide m-Chlorophenyl Hydrazone
animal structures
Proline
Protein Disulfide-Isomerases
Chromosomal translocation
Deoxyglucose
Biology
Hydroxylation
Biochemistry
Mice
2,2'-Dipyridyl
Adenosine Triphosphate
Animals
HSP70 Heat-Shock Proteins
Metabolic Stress
Isomerases
Endoplasmic Reticulum Chaperone BiP
HSP47 Heat-Shock Proteins
Molecular Biology
Cells, Cultured
Heat-Shock Proteins
Lysine
Endoplasmic reticulum
Membrane Proteins
Cell Biology
Chromatography, Agarose
Embryo, Mammalian
Precipitin Tests
Cell biology
Procollagen peptidase
embryonic structures
Carrier Proteins
Procollagen
Molecular Chaperones
Subjects
Details
- ISSN :
- 10974644 and 07302312
- Volume :
- 56
- Database :
- OpenAIRE
- Journal :
- Journal of Cellular Biochemistry
- Accession number :
- edsair.doi.dedup.....3e9130598a0ce1fa358fbce156729d0d
- Full Text :
- https://doi.org/10.1002/jcb.240560412