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Related Experiment Video

Updated: May 31, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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Published on: June 7, 2018

Hsp47 as a collagen-specific molecular chaperone.

Yoshihito Ishida¹, Kazuhiro Nagata

¹Laboratory of Molecular and Cellular Biology, Department of Molecular Biosciences, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan.

Methods in Enzymology

|June 21, 2011

Summary

Heat shock protein 47 (Hsp47) is crucial for collagen maturation and embryonic development. Targeting Hsp47 offers a potential therapeutic strategy for collagen-related diseases like fibrosis and osteogenesis imperfecta.

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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Published on: September 2, 2019

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Heat shock protein 47 (Hsp47) is a collagen-binding glycoprotein in the endoplasmic reticulum.
Hsp47 expression is regulated by heat shock elements and correlates with collagen expression.
It belongs to the serpin family but lacks serine protease inhibitory activity.

Purpose of the Study:

To elucidate the role of Hsp47 in collagen maturation and its implications in disease.
To investigate Hsp47 as a potential therapeutic target for collagen-related disorders.

Main Methods:

Gene ablation studies in mice.
Analysis of Hsp47-deficient cells.
Investigation of Hsp47's role in fibrosis mouse models.

Main Results:

Hsp47 is essential for embryonic development and collagen maturation.
Hsp47 binds procollagen, inhibiting aggregation and facilitating triple helix formation.
Misfolded procollagen in Hsp47-deficient cells is degraded via autophagy-lysosome pathway.
Hsp47 knockdown reduced collagen accumulation in fibrosis models.
Mutations in Hsp47 cause genetic disorders like osteogenesis imperfecta.

Conclusions:

Hsp47 is an indispensable collagen-specific molecular chaperone.
Hsp47 plays a critical role in collagen homeostasis and is implicated in major human diseases.
Hsp47 represents a promising therapeutic target for fibrosis and other collagenopathies.