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Keyword
- collagen3
- molecular chaperone2
- protein-protein interaction2
- biosynthesis1
- chaperone1
- decorin1
- extracellular matrix1
- fibromodulin1
- heat shock protein (HSP)1
- Hsp471
- lumican1
- post-translational modification (PM)1
- prolyl isomerase1
- protein folding1
- protein secretion1
- small leucine-rich protein1
- small leucine-rich proteoglycan (SLRP)1
Glycobiology and Extracellular Matrices
3 Results
- Glycobiology and Extracellular MatricesOpen Access
The endoplasmic reticulum–resident collagen chaperone Hsp47 interacts with and promotes the secretion of decorin, fibromodulin, and lumican
Journal of Biological ChemistryVol. 293Issue 35p13707–13716Published online: July 12, 2018- Yoshihiro Ishikawa
- Kristofer Rubin
- Hans Peter Bächinger
- Sebastian Kalamajski
Cited in Scopus: 15The build-up of diversified and tissue-specific assemblies of extracellular matrix (ECM) proteins depends on secreted and cell surface–located molecular arrays that coordinate ECM proteins into discrete designs. The family of small leucine-rich proteins (SLRPs) associates with and dictates the structure of fibrillar collagens, which form the backbone of most ECM types. However, whether SLRPs form complexes with proteins other than collagens is unclear. Here, we demonstrate that heat shock protein 47 (Hsp47), a well-established endoplasmic reticulum–resident collagen chaperone, also binds the SLRPs decorin, lumican, and fibromodulin with affinities comparable with that in the Hsp47–type I collagen interaction. - Glycobiology and Extracellular MatricesOpen Access
Heat shock protein 47 and 65-kDa FK506-binding protein weakly but synergistically interact during collagen folding in the endoplasmic reticulum
Journal of Biological ChemistryVol. 292Issue 42p17216–17224Published online: August 31, 2017- Yoshihiro Ishikawa
- Paul Holden
- Hans Peter Bächinger
Cited in Scopus: 19Collagen is the most abundant protein in the extracellular matrix in humans and is critical to the integrity and function of many musculoskeletal tissues. A molecular ensemble comprising more than 20 molecules is involved in collagen biosynthesis in the rough endoplasmic reticulum. Two proteins, heat shock protein 47 (Hsp47/SERPINH1) and 65-kDa FK506-binding protein (FKBP65/FKBP10), have been shown to play important roles in this ensemble. In humans, autosomal recessive mutations in both genes cause similar osteogenesis imperfecta phenotypes. - Glycobiology and Extracellular MatricesOpen Access
Ziploc-ing the structure 2.0: Endoplasmic reticulum-resident peptidyl prolyl isomerases show different activities toward hydroxyproline
Journal of Biological ChemistryVol. 292Issue 22p9273–9282Published online: April 6, 2017- Yoshihiro Ishikawa
- Kazunori Mizuno
- Hans Peter Bächinger
Cited in Scopus: 12Extracellular matrix proteins are biosynthesized in the rough endoplasmic reticulum (rER), and the triple-helical protein collagen is the most abundant extracellular matrix component in the human body. Many enzymes, molecular chaperones, and post-translational modifiers facilitate collagen biosynthesis. Collagen contains a large number of proline residues, so the cis/trans isomerization of proline peptide bonds is the rate-limiting step during triple-helix formation. Accordingly, the rER-resident peptidyl prolyl cis/trans isomerases (PPIases) play an important role in the zipper-like triple-helix formation in collagen.