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Journal article
Distinct effects of different matrix proteoglycans on collagen fibrillogenesis and cell-mediated collagen reorganization
Scientific reports, v 10(1), pp 19065-19065
04 Nov 2020
PMID: 33149218
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The extracellular matrix (ECM) is a complex mixture composed of fibrillar collagens as well as additional protein and carbohydrate components. Proteoglycans (PGs) contribute to the heterogeneity of the ECM and play an important role in its structure and function. While the small leucine rich proteoglycans (SLRPs), including decorin and lumican, have been studied extensively as mediators of collagen fibrillogenesis and organization, the function of large matrix PGs in collagen matrices is less well known. In this study, we showed that different matrix PGs have distinct roles in regulating collagen behaviors. We found that versican, a large chondroitin sulfate PG, promotes collagen fibrillogenesis in a turbidity assay and upregulates cell-mediated collagen compaction and reorganization, whereas aggrecan, a structurally-similar large PG, has different and often opposing effects on collagen. Compared to versican, decorin and lumican also have distinct functions in regulating collagen behaviors. The different ways in which matrix PGs interact with collagen have important implications for understanding the role of the ECM in diseases such as fibrosis and cancer, and suggest that matrix PGs are potential therapeutic targets.
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Details
- Title
- Distinct effects of different matrix proteoglycans on collagen fibrillogenesis and cell-mediated collagen reorganization
- Creators
- Dongning Chen - University of PennsylvaniaLucas R. Smith - University of PennsylvaniaGauri Khandekar - University of PennsylvaniaPavan Patel - Drexel UniversityChristopher K. Yu - University of PennsylvaniaKehan Zhang - Boston UniversityChristopher S. Chen - National Science FoundationLin Han - Drexel Univ, Sch Biomed Engn Sci & Hlth Syst, Philadelphia, PA 19104 USARebecca G. Wells - University of Pennsylvania
- Publication Details
- Scientific reports, v 10(1), pp 19065-19065
- Publisher
- NATURE PORTFOLIO
- Number of pages
- 13
- Grant note
- DMR-1720530 / UPenn National Science Foundation MRSEC CMMI:15-48571 / Center for Engineering MechanoBiology (CEMB), a National Science Foundation Science and Technology Center P30 DK050306 / NIH; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- School of Biomedical Engineering, Science, and Health Systems
- Web of Science ID
- WOS:000587638900020
- Scopus ID
- 2-s2.0-85094952334
- Other Identifier
- 991019168279904721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology