PUBLICATION
Synergistic effect of PCPE1 and sFRP2 on the processing of procollagens via BMP1
- Authors
- Zhu, Q., Guo, W., Zhang, S., Feng, Y., Wang, X., Greenspan, D.S., Zhou, L., Huang, G.R.
- ID
- ZDB-PUB-181110-9
- Date
- 2018
- Source
- FEBS letters 593(1): 119-127 (Journal)
- Registered Authors
- Keywords
- Bone morphogenetic protein 1, Dorsalized, Procollagen C-proteinase enhancer 1, Procollagen processing, Secreted frizzled related protein 2
- MeSH Terms
-
- Animals
- Binding Sites
- Body Patterning
- Bone Morphogenetic Protein 1/metabolism*
- Cells, Cultured
- Extracellular Matrix Proteins/chemistry
- Extracellular Matrix Proteins/genetics
- Extracellular Matrix Proteins/metabolism
- Fibroblasts/cytology
- Fibroblasts/metabolism
- Gene Knockdown Techniques
- Glycoproteins/chemistry
- Glycoproteins/genetics
- Glycoproteins/metabolism*
- Membrane Proteins/genetics
- Membrane Proteins/metabolism*
- Mice
- Zebrafish/embryology
- Zebrafish/growth & development*
- Zebrafish/metabolism
- Zebrafish Proteins/chemistry
- Zebrafish Proteins/genetics
- Zebrafish Proteins/metabolism
- PubMed
- 30411347 Full text @ FEBS Lett.
Citation
Zhu, Q., Guo, W., Zhang, S., Feng, Y., Wang, X., Greenspan, D.S., Zhou, L., Huang, G.R. (2018) Synergistic effect of PCPE1 and sFRP2 on the processing of procollagens via BMP1. FEBS letters. 593(1):119-127.
Abstract
Procollagen processing is essential for organ development and tissue functions. Both procollagen C-proteinase enhancer 1 (PCPE1) and secreted frizzled-related protein 2 (sFRP2) play vital roles in collagen formation via regulating the procollagen C-proteinase (pCP) activity of bone morphogenetic protein 1 (BMP1). However, whether the two proteins exert a synergistic effect on BMP1 activity remains unclear. Here, simultaneous knockdown of sFRP2 and PCPE1 led to less collagen formation in mouse embryonic fibroblasts and dorsalized phenotypes in zebrafish embryos. Further studies revealed a direct interaction between the Frizzled domain of sFRP2 and the CUB domain of PCPE1, which enhances the cleavage activity of BMP1 on procollagen. These results suggest that double silencing of sFRP2 and PCPE1 may provide a strategy for treating fibrosis diseases caused by collagen deposition. This article is protected by copyright. All rights reserved.
Errata / Notes
This article is corrected by ZDB-PUB-220906-146 .
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping