ArticleThe Journal of biological chemistry2012
Direct in vitro and in vivo evidence for interaction between Hsp47 protein and collagen triple helix.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed, 51 citations in OpenAlex.
- Collagen IV in Gould syndrome and Alport syndrome.Nature reviews. Nephrology · 2025Review
- The life cycle of type IV collagen.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- Decoding collagen's thermally induced unfolding and refolding pathways.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Photothermal driven BMSCs osteogenesis and M2 macrophage polarization on polydopamine-coated TiMaterials today. Bio · 2024Article
- HSP47 in human diseases: Navigating pathophysiology, diagnosis and therapy.Clinical and translational medicine · 2024Review
- Article
- Local Net Charge State of Collagen Triple Helix Is a Determinant of FKBP22 Binding to Collagen III.International journal of molecular sciences · 2023Article
- Profiling extra cellular matrix associated proteome of human fetal nucleus pulposus in search for regenerative targets.Scientific reports · 2021Article
- Aberrant binding of mutant HSP47 affects posttranslational modification of type I collagen and leads to osteogenesis imperfecta.PLoS genetics · 2021Article
- Silencing Heat Shock Protein 47 (HSP47) in Fibrogenic Precision-Cut Lung Slices: A Surprising Lack of Effects on Fibrogenesis?Frontiers in medicine · 2021Article
- SERPINH1 is a Potential Prognostic Biomarker and Correlated With Immune Infiltration: A Pan-Cancer Analysis.Frontiers in genetics · 2021Article
- Cryptic collagen elements as signaling hubs in the regulation of tumor growth and metastasis.Journal of cellular physiology · 2020Review
- A BRET-based assay reveals collagen-Hsp47 interaction dynamics in the endoplasmic reticulum and small-molecule inhibition of this interaction.The Journal of biological chemistry · 2019Article
- Reversal of Vocal Fold Mucosal Fibrosis Using siRNA against the Collagen-Specific Chaperone Serpinh1.Molecular therapy. Nucleic acids · 2019Article
- ER-to-Golgi trafficking of procollagen in the absence of large carriers.The Journal of cell biology · 2019Article
- A small-molecule compound inhibits a collagen-specific molecular chaperone and could represent a potential remedy for fibrosis.The Journal of biological chemistry · 2017Article
- Matrix metalloproteinase collagenolysis in health and disease.Biochimica et biophysica acta. Molecular cell research · 2017Review
- COPII-coated membranes function as transport carriers of intracellular procollagen I.The Journal of cell biology · 2017Article
- Endoplasmic reticulum stress in chondrodysplasias caused by mutations in collagen types II and X.Cell stress & chaperones · 2016Review
- The pH-dependent Client Release from the Collagen-specific Chaperone HSP47 Is Triggered by a Tandem Histidine Pair.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hsp47 (heat shock protein 47), a collagen-specific molecular chaperone, is essential for the maturation of various types of procollagens. Previous studies have suggested that Hsp47 may preferentially recognize the triple-helix form of procollagen rather than unfolded procollagen chains in the endoplasmic reticulum. However, the underlying mechanism has remained unclear because of limitations in the available methods for detecting in vitro and in vivo interactions between Hsp47 and collagen. In this study, we established novel methods for this purpose by adopting a time-resolved FRET technique in vitro and a bimolecular fluorescence complementation technique in vivo. Using these methods, we provide direct evidence that Hsp47 binds to collagen triple helices but not to the monomer form in vitro. We also demonstrate that Hsp47 binds a collagen model peptide in the trimer conformation in vivo. Hsp47 did not bind collagen peptides that had been modified to block their ability to form triple helices in vivo. These results conclusively indicate that Hsp47 recognizes the triple-helix form of procollagen in vitro and in vivo.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.