The collagen-specific molecular chaperone HSP47: is there a role in fibrosis?

Trends Mol Med. 2007 Feb;13(2):45-53. doi: 10.1016/j.molmed.2006.12.001. Epub 2006 Dec 13.


Heat shock protein 47 (HSP47) is a collagen-specific molecular chaperone that is required for molecular maturation of various types of collagens. Recent studies have shown a close association between increased expression of HSP47 and excessive accumulation of collagens in scar tissues of various human and experimental fibrotic diseases. It is presumed that the increased levels of HSP47 in fibrotic diseases assist in excessive assembly and intracellular processing of procollagen molecules and, thereby, contribute to the formation of fibrotic lesions. Studies have also shown that suppression of HSP47 expression can reduce accumulation of collagens to delay the progression of fibrotic diseases in experimental animal models. Because HSP47 is a specific chaperone for collagen synthesis, it provides a selective target to manipulate collagen production, a phenomenon that might have enormous clinical impact in controlling a wide range of fibrotic diseases. Here, we outline the fibrogenic role of HSP47 and discuss the potential usefulness of HSP47 as an anti-fibrotic therapeutic target.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Collagen / metabolism*
  • Fibrosis / etiology*
  • Fibrosis / metabolism*
  • Fibrosis / therapy
  • HSP47 Heat-Shock Proteins / metabolism*
  • Humans
  • Models, Biological
  • Protein Processing, Post-Translational


  • HSP47 Heat-Shock Proteins
  • Collagen