HSP47, a molecular chaperone which interacts with procollagens in the endoplasmic reticulum

Takaki Koide, K. Nagata

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

HSP47 is an endoplasmic reticulum(ER)-resident glycoprotein with an ER- retention signal, Arg-Asp-Glu-Leu, at its C-terminus. This protein belongs to serine protease inhibitor (serpin) family, although the protease-inhibitory activity has not yet been detected. The expression of HSP47 under stress conditions is regulated by the heat shock transcription factor (HSF) system, and that under non-stress condition is well correlated with collagen expression in various cell lines and tissues. In the collagen producing cells, HSP47 tentatively interacts with procollagen during its translation, folding and/or modification steps, and releases procollagen at cis-Golgi. HSP47 shows the affinity to all types of collagen tested as well as simple collagen model peptides (Pro-Pro-Gly)n (n≥7) in vitro. Recent studies have suggested that chaperone proteins including HSP47 would facilitate or control the collagen biosynthesis in the ER.

Original languageEnglish
Pages (from-to)307-312
Number of pages6
JournalConnective Tissue
Volume30
Issue number4
Publication statusPublished - 1998
Externally publishedYes

Fingerprint

Procollagen
Molecular Chaperones
Endoplasmic Reticulum
Collagen
prolyl-prolyl-glycine
Serine Proteinase Inhibitors
Glycoproteins
Proteins
Peptide Hydrolases
Cell Line
Peptides

Keywords

  • Collagen
  • Endoplasmic reticulum
  • Fibrosis
  • HSP47
  • Procollagen
  • Prolyl-4- hydroxylation

ASJC Scopus subject areas

  • Rheumatology

Cite this

HSP47, a molecular chaperone which interacts with procollagens in the endoplasmic reticulum. / Koide, Takaki; Nagata, K.

In: Connective Tissue, Vol. 30, No. 4, 1998, p. 307-312.

Research output: Contribution to journalArticle

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