ArticleScientific reports2019
Lowering the culture temperature corrects collagen abnormalities caused by HSP47 gene knockout.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 31 citations in OpenAlex.
- THSD4 promotes hair growth by facilitating dermal papilla and hair matrix interactions.Theranostics · 2025Article
- HSP47 at the Crossroads of Thrombosis and Collagen Dynamics: Unlocking Therapeutic Horizons and Debates.TH open : companion journal to thrombosis and haemostasis · 2025Review
- Is Exon Skipping a Viable Therapeutic Approach for Vascular Ehlers-Danlos Syndrome with Mutations inInternational journal of molecular sciences · 2024Article
- A model for collagen secretion by intercompartmental continuities.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Expression of mammalian proteins for diagnostics and therapeutics: a review.Molecular biology reports · 2022Review
- The Thermal Stability of the Collagen Triple Helix Is Tuned According to the Environmental Temperature.International journal of molecular sciences · 2022Article
- Collagen's primary structure determines collagen:HSP47 complex stoichiometry.The Journal of biological chemistry · 2021Article
- The CAG promoter maintains high-level transgene expression in HEK293 cells.FEBS open bio · 2021Article
- Mechanisms of procollagen and HSP47 sorting during ER-to-Golgi trafficking.Matrix biology : journal of the International Society for Matrix Biology · 2020Article
- Exogenous supply of Hsp47 triggers fibrillar collagen deposition in skin cell cultures in vitro.BMC molecular and cell biology · 2020Article
- Role of Glycosyltransferase 25 Domain 1 in Type I Collagen Glycosylation and Molecular Phenotypes.Biochemistry · 2019Article
- 4-Phenylbutyric acid enhances the mineralization of osteogenesis imperfecta iPSC-derived osteoblasts.The Journal of biological chemistryArticle
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7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat shock protein 47 (HSP47) is an endoplasmic reticulum (ER)-resident molecular chaperone that specifically recognizes triple helical portions of procollagens. The chaperone function of HSP47 is indispensable in mammals, and hsp47-null mice show an embryonic lethal phenotype accompanied by severe abnormalities in collagen-based tissue structures. Two leading hypotheses are currently accepted for the molecular function of HSP47 as a procollagen-specific chaperone. One is facilitation of procollagen folding by stabilizing thermally unstable triple helical folding intermediates, and the other is inhibition of procollagen aggregation or lateral association in the ER. The aim of this study was to elucidate the functional essence of this unique chaperone using fibroblasts established from hsp47-/- mouse embryos. When the cells were cultured at 37 °C, various defects in procollagen biosynthesis were observed, such as accumulation in the ER, over-modifications including prolyl hydroxylation, lysyl hydroxylation, and further glycosylation, and unusual secretion of type I collagen homotrimer. All defects were corrected by culturing the cells at a lower temperature of 33 °C. These results indicated that lowering the culture temperature compensated for the loss of HSP47. This study elucidated that HSP47 stabilizes the elongating triple helix of procollagens, which is otherwise unstable at the body temperature of mammals.
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