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Decorin is processed by three isoforms of bone morphogenetic protein-1 (BMP1)
Zofia von Marschall1, Larry W Fisher
1Craniofacial and Skeletal Diseases Branch, NIDCR, NIH, DHHS, Bethesda, MD, USA.
Biochemical and Biophysical Research Communications
|December 23, 2009
Summary
Bone morphogenetic protein-1 (BMP1) isoforms cleave propeptides from decorin and biglycan, activating these small leucine-rich proteoglycans. This BMP1-mediated processing is a key characteristic of Class I SLRPs.
Area of Science:
- Biochemistry
- Molecular Biology
- Extracellular Matrix Biology
Background:
- Decorin, a secreted small proteoglycan, regulates collagen formation and TGF-beta superfamily bioactivity.
- Recombinant prodecorin is explored in gene therapy for fibrosis, but its propeptide processing in vivo is unclear.
- The specific protease responsible for removing decorin's conserved propeptide remains unidentified.
Purpose of the Study:
- To identify the protease responsible for removing the propeptide from human prodecorin.
- To investigate the role of bone morphogenetic protein-1 (BMP1) isoforms in prodecorin processing.
- To determine if propeptide removal is essential for decorin's glycosaminoglycan chain addition.
Main Methods:
- In vitro assays using recombinant human prodecorin and biglycan.
- Analysis of propeptide cleavage by three different BMP1 isoforms (classic BMP1, mTLD, BMP1-5).
- Assessment of glycosaminoglycan chain addition in relation to propeptide removal.
Main Results:
- Three BMP1 isoforms (BMP1, mTLD, BMP1-5) efficiently removed propeptides from human prodecorin and murine probiglycan.
- Propeptide removal by BMP1 was not required for the addition of decorin's glycosaminoglycan chain.
- These findings position decorin among matrix molecules processed by the BMP1/Tolloid family.
Conclusions:
- Members of the BMP1/Tolloid family, including three distinct isoforms, process and activate decorin and biglycan by removing their propeptides.
- Propeptide cleavage by BMP1 is not a prerequisite for decorin glycosaminoglycanation.
- The processing of Class I small leucine-rich proteoglycans (SLRPs) by BMP1 represents a conserved mechanism, likely extending to asporin.
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