Journal
MATRIX BIOLOGY
Volume 63, Issue -, Pages 91-105Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.matbio.2017.02.001
Keywords
Cell-matrix-interactions; Mechanoreception; Suprastructure; Adaptor proteins
Categories
Funding
- Deutsche Forschungsgemeinschaft [BR1497/4-1, EB177/9-1]
- BBSRC UK [BB/I011226/1]
- Biotechnology and Biological Sciences Research Council [BB/I011226/1] Funding Source: researchfish
- Cancer Foundation Finland sr [140104, 160072] Funding Source: researchfish
- BBSRC [BB/I011226/1] Funding Source: UKRI
Ask authors/readers for more resources
Interactions of cells with supramolecular aggregates of the extracellular matrix (ECM) are mediated, in part, by cell surface receptors of the integrin family. These are important molecular components of cell surface-suprastructures regulating cellular activities in general. A subfamily of beta 1-integrins with von Willebrand-factor A-like domains (I-domains) in their alpha-chains can bind to collagen molecules and, therefore, are considered as important cellular mechano-receptors. Here we show that chondrocytes strongly bind to cartilage collagens in the form of individual triple helical molecules but very weakly to fibrils formed by the same molecules. We also find that chondrocyte integrins alpha 1 beta 1-, alpha 2 beta 1- and alpha 10 beta 1-integrins and their I-domains have the same characteristics. Nevertheless we find integrin binding to mechanically generated cartilage fibril fragments, which also comprise peripheral non-collagenous material. We conclude that cell adhesion results from binding of integrin-containing adhesion suprastructures to the non-collagenous fibril periphery but not to the collagenous fibril cores. The biological importance of the well-investigated recognition of collagen molecules by integrins is unknown. Possible scenarios may include fibrillogenesis, fibril degradation and/or phagocytosis, recruitment of cells to remodeling sites, or molecular signaling across cytoplasmic membranes. In these circumstances, collagen molecules may lack a fibrillar organization. However, other processes requiring robust biomechanical functions, such as fibril organization in tissues, cell division, adhesion, or migration, do not involve direct integrin-collagen interactions. (C) 2017 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available