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- Glycobiology and Extracellular Matrices
- Bächinger, Hans PeterRemove Bächinger, Hans Peter filter
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Glycobiology and Extracellular Matrices
2 Results
- Research ArticleOpen Access
Type I and type V procollagen triple helix uses different subsets of the molecular ensemble for lysine posttranslational modifications in the rER
Journal of Biological ChemistryVol. 296100453Published online: February 22, 2021- Yoshihiro Ishikawa
- Yuki Taga
- Keith Zientek
- Nobuyo Mizuno
- Antti M. Salo
- Olesya Semenova
- and others
Cited in Scopus: 9Collagen is the most abundant protein in humans. It has a characteristic triple-helix structure and is heavily posttranslationally modified. The complex biosynthesis of collagen involves processing by many enzymes and chaperones in the rough endoplasmic reticulum. Lysyl hydroxylase 1 (LH1) is required to hydroxylate lysine for cross-linking and carbohydrate attachment within collagen triple helical sequences. Additionally, a recent study of prolyl 3-hydroxylase 3 (P3H3) demonstrated that this enzyme may be critical for LH1 activity; however, the details surrounding its involvement remain unclear. - 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.