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The Scar-in-a-Jar: studying potential antifibrotic compounds from the epigenetic to extracellular level in a single
C Z C Chen1, Y X Peng, Z B Wang
1Division of Bioengineering, Faculty of Engineering, National University of Singapore, Singapore.
Background And Purpose:
Fibrosis, a pathological accumulation of collagen in tissues, represents a major global disease burden. Effective characterization of potential antifibrotic drugs has been constrained by poor formation of the extracellular matrix in vitro, due to tardy procollagen processing by collagen C-proteinase/BMP-1, and difficulties in relating this matrix to cell numbers in experimental samples.
Experimental Approach:
The Scar-in-a-Jar model provided, in vitro, the complete biosynthetic cascade of collagen matrix formation including complete conversion of procollagen by C-proteinase/BMP-1, its subsequent extracellular deposition and lysyl oxidase-mediated cross-linking, achieved by applying the biophysical principle of macromolecular 'crowding'. Collagen matrix deposition, velocity and morphology can be controlled using negatively charged 'crowders' in a rapid (2 days) mode or a mixture of neutral 'crowders' in an accelerated (6 days) mode. Combined with quantitative optical bioimaging, this novel system allows for in situ assessment of the area of deposited collagen(s) per cell.
Key Results:
Optical evaluation of known and novel antifibrotic compounds effective at the epigenetic, post-transcriptional/translational/secretional level correlated excellently with corresponding biochemical analyses. Focusing on quantitation of deposited collagen, the Scar-in-a-Jar was most effective in assessing novel inhibitors that may have multiple targets, such as microRNA29c, found to be a promising antifibrotic agent.
Conclusions And Implications:
This novel screening system supersedes current in vitro fibroplasia models, as a fast, quantitative and non-destructive technique. This method distinguishes a reduction in collagen I deposition, excluding collagen cross-linking, and allows full evaluation of inhibitors of C-proteinase/BMP-1 and other matrix metalloproteinases.
Insights
A novel Scar-in-a-Jar model rapidly quantifies antifibrotic drug efficacy by measuring collagen deposition per cell. This advanced in vitro system accelerates drug discovery for fibrosis, a major global health concern.
Area of Science:
- Biochemistry
- Drug Discovery
- Cell Biology
Background:
- Fibrosis, characterized by excessive collagen accumulation, poses a significant global health challenge.
- Current in vitro models struggle to accurately mimic extracellular matrix formation for antifibrotic drug screening.
- Limitations include slow procollagen processing and difficulty in relating matrix deposition to cell counts.
Purpose of the Study:
- To develop a novel in vitro model for efficient and quantitative assessment of antifibrotic compounds.
- To overcome limitations in current models regarding extracellular matrix formation and analysis.
- To enable rapid screening of potential antifibrotic drugs targeting collagen processing and deposition.
Main Methods:
- The Scar-in-a-Jar model utilizes macromolecular crowding to recapitulate the complete collagen biosynthetic cascade in vitro.
- It enables controlled collagen matrix deposition, velocity, and morphology within 2-6 days.
- Quantitative optical bioimaging allows for in situ assessment of deposited collagen area per cell.
Main Results:
- The model accurately correlated optical evaluation of antifibrotic compounds with biochemical analyses.
- It proved effective in assessing novel inhibitors, including microRNA29c, a promising antifibrotic agent.
- The system quantifies deposited collagen, distinguishing effects on collagen I deposition from cross-linking.
Conclusions:
- The Scar-in-a-Jar system offers a superior alternative to existing in vitro fibrosis models.
- It provides a fast, quantitative, and non-destructive method for antifibrotic drug screening.
- This technique facilitates the evaluation of inhibitors targeting collagen C-proteinase/BMP-1 and other matrix metalloproteinases.
