Collagen Type I as a Ligand for Receptor-Mediated Signaling
Collagens form the fibrous component of the extracellular matrix in all multi-cellular animals. Collagen type I is the most abundant collagen present in skin, tendons, vasculature, as well as the organic portion of the calcified tissue of bone and teeth. This review focuses on numerous receptors for...
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Format: | Article |
Language: | English |
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Frontiers Media S.A.
2017-05-01
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Series: | Frontiers in Physics |
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Online Access: | http://journal.frontiersin.org/article/10.3389/fphy.2017.00012/full |
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author | Iris Boraschi-Diaz Iris Boraschi-Diaz Jennifer Wang John S. Mort Svetlana V. Komarova Svetlana V. Komarova |
author_facet | Iris Boraschi-Diaz Iris Boraschi-Diaz Jennifer Wang John S. Mort Svetlana V. Komarova Svetlana V. Komarova |
author_sort | Iris Boraschi-Diaz |
collection | DOAJ |
description | Collagens form the fibrous component of the extracellular matrix in all multi-cellular animals. Collagen type I is the most abundant collagen present in skin, tendons, vasculature, as well as the organic portion of the calcified tissue of bone and teeth. This review focuses on numerous receptors for which collagen acts as a ligand, including integrins, discoidin domain receptors DDR1 and 2, OSCAR, GPVI, G6b-B, and LAIR-1 of the leukocyte receptor complex (LRC) and mannose family receptor uPARAP/Endo180. We explore the process of collagen production and self-assembly, as well as its degradation by collagenases and gelatinases in order to predict potential temporal and spatial sites of action of different collagen receptors. While the interactions of the mature collagen matrix with integrins and DDR are well-appreciated, potential signals from immature matrix as well as collagen degradation products are possible but not yet described. The role of multiple collagen receptors in physiological processes and their contribution to pathophysiology of diseases affecting collagen homeostasis require further studies. |
first_indexed | 2024-04-12T19:13:07Z |
format | Article |
id | doaj.art-03334fee3f6a4d8abf2f56603ab8f0b3 |
institution | Directory Open Access Journal |
issn | 2296-424X |
language | English |
last_indexed | 2024-04-12T19:13:07Z |
publishDate | 2017-05-01 |
publisher | Frontiers Media S.A. |
record_format | Article |
series | Frontiers in Physics |
spelling | doaj.art-03334fee3f6a4d8abf2f56603ab8f0b32022-12-22T03:19:49ZengFrontiers Media S.A.Frontiers in Physics2296-424X2017-05-01510.3389/fphy.2017.00012249703Collagen Type I as a Ligand for Receptor-Mediated SignalingIris Boraschi-Diaz0Iris Boraschi-Diaz1Jennifer Wang2John S. Mort3Svetlana V. Komarova4Svetlana V. Komarova5Faculty of Dentistry, McGill UniversityMontreal, QC, CanadaShriners Hospitals for Children - CanadaMontreal, QC, CanadaShriners Hospitals for Children - CanadaMontreal, QC, CanadaShriners Hospitals for Children - CanadaMontreal, QC, CanadaFaculty of Dentistry, McGill UniversityMontreal, QC, CanadaShriners Hospitals for Children - CanadaMontreal, QC, CanadaCollagens form the fibrous component of the extracellular matrix in all multi-cellular animals. Collagen type I is the most abundant collagen present in skin, tendons, vasculature, as well as the organic portion of the calcified tissue of bone and teeth. This review focuses on numerous receptors for which collagen acts as a ligand, including integrins, discoidin domain receptors DDR1 and 2, OSCAR, GPVI, G6b-B, and LAIR-1 of the leukocyte receptor complex (LRC) and mannose family receptor uPARAP/Endo180. We explore the process of collagen production and self-assembly, as well as its degradation by collagenases and gelatinases in order to predict potential temporal and spatial sites of action of different collagen receptors. While the interactions of the mature collagen matrix with integrins and DDR are well-appreciated, potential signals from immature matrix as well as collagen degradation products are possible but not yet described. The role of multiple collagen receptors in physiological processes and their contribution to pathophysiology of diseases affecting collagen homeostasis require further studies.http://journal.frontiersin.org/article/10.3389/fphy.2017.00012/fullbonecathepsin Kcollagen type Idiscoidin domain receptorsintegrinsleukocyte immunoglobulin-like receptor complex |
spellingShingle | Iris Boraschi-Diaz Iris Boraschi-Diaz Jennifer Wang John S. Mort Svetlana V. Komarova Svetlana V. Komarova Collagen Type I as a Ligand for Receptor-Mediated Signaling Frontiers in Physics bone cathepsin K collagen type I discoidin domain receptors integrins leukocyte immunoglobulin-like receptor complex |
title | Collagen Type I as a Ligand for Receptor-Mediated Signaling |
title_full | Collagen Type I as a Ligand for Receptor-Mediated Signaling |
title_fullStr | Collagen Type I as a Ligand for Receptor-Mediated Signaling |
title_full_unstemmed | Collagen Type I as a Ligand for Receptor-Mediated Signaling |
title_short | Collagen Type I as a Ligand for Receptor-Mediated Signaling |
title_sort | collagen type i as a ligand for receptor mediated signaling |
topic | bone cathepsin K collagen type I discoidin domain receptors integrins leukocyte immunoglobulin-like receptor complex |
url | http://journal.frontiersin.org/article/10.3389/fphy.2017.00012/full |
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