In-Depth Analysis of the Pancreatic Extracellular Matrix during Development for Next-Generation Tissue Engineering
The pancreas is a complex organ consisting of differentiated cells and extracellular matrix (ECM) organized adequately to enable its endocrine and exocrine functions. Although much is known about the intrinsic factors that control pancreas development, very few studies have focused on the microenvir...
Main Authors: | , , , , , , , , , , , , , , , , |
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MDPI AG
2023-06-01
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Online Access: | https://www.mdpi.com/1422-0067/24/12/10268 |
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author | Laura Glorieux Laura Vandooren Sylvie Derclaye Sébastien Pyr dit Ruys Paloma Oncina-Gil Anna Salowka Gaëtan Herinckx Elias Aajja Pascale Lemoine Catherine Spourquet Hélène Lefort Patrick Henriet Donatienne Tyteca Francesca M. Spagnoli David Alsteens Didier Vertommen Christophe E. Pierreux |
author_facet | Laura Glorieux Laura Vandooren Sylvie Derclaye Sébastien Pyr dit Ruys Paloma Oncina-Gil Anna Salowka Gaëtan Herinckx Elias Aajja Pascale Lemoine Catherine Spourquet Hélène Lefort Patrick Henriet Donatienne Tyteca Francesca M. Spagnoli David Alsteens Didier Vertommen Christophe E. Pierreux |
author_sort | Laura Glorieux |
collection | DOAJ |
description | The pancreas is a complex organ consisting of differentiated cells and extracellular matrix (ECM) organized adequately to enable its endocrine and exocrine functions. Although much is known about the intrinsic factors that control pancreas development, very few studies have focused on the microenvironment surrounding pancreatic cells. This environment is composed of various cells and ECM components, which play a critical role in maintaining tissue organization and homeostasis. In this study, we applied mass spectrometry to identify and quantify the ECM composition of the developing pancreas at the embryonic (E) day 14.5 and postnatal (P) day 1 stages. Our proteomic analysis identified 160 ECM proteins that displayed a dynamic expression profile with a shift in collagens and proteoglycans. Furthermore, we used atomic force microscopy to measure the biomechanical properties and found that the pancreatic ECM was soft (≤400 Pa) with no significant change during pancreas maturation. Lastly, we optimized a decellularization protocol for P1 pancreatic tissues, incorporating a preliminary crosslinking step, which effectively preserved the 3D organization of the ECM. The resulting ECM scaffold proved suitable for recellularization studies. Our findings provide insights into the composition and biomechanics of the pancreatic embryonic and perinatal ECM, offering a foundation for future studies investigating the dynamic interactions between the ECM and pancreatic cells. |
first_indexed | 2024-03-11T02:20:45Z |
format | Article |
id | doaj.art-d382c5adc80b4bd09962e1eff532acb7 |
institution | Directory Open Access Journal |
issn | 1661-6596 1422-0067 |
language | English |
last_indexed | 2024-03-11T02:20:45Z |
publishDate | 2023-06-01 |
publisher | MDPI AG |
record_format | Article |
series | International Journal of Molecular Sciences |
spelling | doaj.art-d382c5adc80b4bd09962e1eff532acb72023-11-18T10:51:08ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-06-0124121026810.3390/ijms241210268In-Depth Analysis of the Pancreatic Extracellular Matrix during Development for Next-Generation Tissue EngineeringLaura Glorieux0Laura Vandooren1Sylvie Derclaye2Sébastien Pyr dit Ruys3Paloma Oncina-Gil4Anna Salowka5Gaëtan Herinckx6Elias Aajja7Pascale Lemoine8Catherine Spourquet9Hélène Lefort10Patrick Henriet11Donatienne Tyteca12Francesca M. Spagnoli13David Alsteens14Didier Vertommen15Christophe E. Pierreux16Cell Biology Unit, de Duve Institute, UCLouvain, 1200 Brussels, BelgiumCell Biology Unit, de Duve Institute, UCLouvain, 1200 Brussels, BelgiumNanobiophysics Lab, Louvain Institute of Biomolecular Science and Technology, UCLouvain, 1348 Louvain-la-Neuve, BelgiumLouvain Drug Research Institute, UCLouvain, 1200 Brussels, BelgiumNanobiophysics Lab, Louvain Institute of Biomolecular Science and Technology, UCLouvain, 1348 Louvain-la-Neuve, BelgiumCentre for Gene Therapy and Regenerative Medicine, King’s College London, Great Maze Pond, London SE1 9RT, UKde Duve Institute and MASSPROT Platform, UCLouvain, 1200 Brussels, BelgiumCell Biology Unit, de Duve Institute, UCLouvain, 1200 Brussels, BelgiumCell Biology Unit, de Duve Institute, UCLouvain, 1200 Brussels, BelgiumCell Biology Unit, de Duve Institute, UCLouvain, 1200 Brussels, BelgiumCell Biology Unit, de Duve Institute, UCLouvain, 1200 Brussels, BelgiumCell Biology Unit, de Duve Institute, UCLouvain, 1200 Brussels, BelgiumCell Biology Unit, de Duve Institute, UCLouvain, 1200 Brussels, BelgiumCentre for Gene Therapy and Regenerative Medicine, King’s College London, Great Maze Pond, London SE1 9RT, UKNanobiophysics Lab, Louvain Institute of Biomolecular Science and Technology, UCLouvain, 1348 Louvain-la-Neuve, Belgiumde Duve Institute and MASSPROT Platform, UCLouvain, 1200 Brussels, BelgiumCell Biology Unit, de Duve Institute, UCLouvain, 1200 Brussels, BelgiumThe pancreas is a complex organ consisting of differentiated cells and extracellular matrix (ECM) organized adequately to enable its endocrine and exocrine functions. Although much is known about the intrinsic factors that control pancreas development, very few studies have focused on the microenvironment surrounding pancreatic cells. This environment is composed of various cells and ECM components, which play a critical role in maintaining tissue organization and homeostasis. In this study, we applied mass spectrometry to identify and quantify the ECM composition of the developing pancreas at the embryonic (E) day 14.5 and postnatal (P) day 1 stages. Our proteomic analysis identified 160 ECM proteins that displayed a dynamic expression profile with a shift in collagens and proteoglycans. Furthermore, we used atomic force microscopy to measure the biomechanical properties and found that the pancreatic ECM was soft (≤400 Pa) with no significant change during pancreas maturation. Lastly, we optimized a decellularization protocol for P1 pancreatic tissues, incorporating a preliminary crosslinking step, which effectively preserved the 3D organization of the ECM. The resulting ECM scaffold proved suitable for recellularization studies. Our findings provide insights into the composition and biomechanics of the pancreatic embryonic and perinatal ECM, offering a foundation for future studies investigating the dynamic interactions between the ECM and pancreatic cells.https://www.mdpi.com/1422-0067/24/12/10268pancreasextracellular matrixdevelopmentdecellularizationproteomicsatomic force microscopy |
spellingShingle | Laura Glorieux Laura Vandooren Sylvie Derclaye Sébastien Pyr dit Ruys Paloma Oncina-Gil Anna Salowka Gaëtan Herinckx Elias Aajja Pascale Lemoine Catherine Spourquet Hélène Lefort Patrick Henriet Donatienne Tyteca Francesca M. Spagnoli David Alsteens Didier Vertommen Christophe E. Pierreux In-Depth Analysis of the Pancreatic Extracellular Matrix during Development for Next-Generation Tissue Engineering International Journal of Molecular Sciences pancreas extracellular matrix development decellularization proteomics atomic force microscopy |
title | In-Depth Analysis of the Pancreatic Extracellular Matrix during Development for Next-Generation Tissue Engineering |
title_full | In-Depth Analysis of the Pancreatic Extracellular Matrix during Development for Next-Generation Tissue Engineering |
title_fullStr | In-Depth Analysis of the Pancreatic Extracellular Matrix during Development for Next-Generation Tissue Engineering |
title_full_unstemmed | In-Depth Analysis of the Pancreatic Extracellular Matrix during Development for Next-Generation Tissue Engineering |
title_short | In-Depth Analysis of the Pancreatic Extracellular Matrix during Development for Next-Generation Tissue Engineering |
title_sort | in depth analysis of the pancreatic extracellular matrix during development for next generation tissue engineering |
topic | pancreas extracellular matrix development decellularization proteomics atomic force microscopy |
url | https://www.mdpi.com/1422-0067/24/12/10268 |
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