Unique charge-dependent constraint on collagen recognition by integrin α10β1

Hamaia, Samir; Luff, Daisy H; Hunter, Emma J.; Malcor, Jean‐Daniel; Bihan, Dominique; Gullberg, Donald; Farndale, Richard W.

doi:10.1016/j.matbio.2016.08.010

Cited by 18 publications

(15 citation statements)

References 42 publications

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“…3 for α2β1-integrin. In conclusion, these results confirm and extend previous observations [24,[39][40][41] that monomolecular cartilage collagens were good binding substrates for all collagen-binding integrins expressed by chondrocytes.…”

Section: Binding Of Soluble Integrins To Collagens II Ix and Xisupporting

confidence: 91%

The binding capacity of α1β1-, α2β1- and α10β1-integrins depends on non-collagenous surface macromolecules rather than the collagens in cartilage fibrils

et al. 2017

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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 surfacesuprastructures regulating cellular activities in general. A subfamily of β1-integrins with von Willebrand-factor A-like domains (I-domains) in their α-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 α1β1-, α2 β1-and α10β1-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/orphagocytosis, 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.

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Section: Binding Of Soluble Integrins To Collagens II Ix and Xisupporting

confidence: 91%

The binding capacity of α1β1-, α2β1- and α10β1-integrins depends on non-collagenous surface macromolecules rather than the collagens in cartilage fibrils

et al. 2017

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“…The former chain is encoded by COL1A1 gene, while the latter chain is encoded by COL1A2 gene [51]. Adhesion of type I collagen and ACs is mediated by integrin: strongly by a 2 b 1 integrin and weakly by a 10 b 1 integrin [52,53]. Type I collagen possess multiple binding sites, such as GFOGER and GROGER (amino acid sequences with single letter amino acid nomenclature), capable to be recognized by a 2 I and a 10 I domains of integrin [52,53], respectively.…”

Section: Interaction Of Articular Chondrocytes (Acs)mentioning

confidence: 99%

Collagen Scaffolds in Cartilage Tissue Engineering and Relevant Approaches for Future Development

Irawan

Sung

Higuchi

et al. 2018

Tissue Eng Regen Med

169

127

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BACKGROUND: Cartilage tissue engineering (CTE) aims to obtain a structure mimicking native cartilage tissue through the combination of relevant cells, three-dimensional scaffolds, and extraneous signals. Implantation of 'matured' constructs is thus expected to provide solution for treating large injury of articular cartilage. Type I collagen is widely used as scaffolds for CTE products undergoing clinical trial, owing to its ubiquitous biocompatibility and vast clinical approval. However, the long-term performance of pure type I collagen scaffolds would suffer from its limited chondrogenic capacity and inferior mechanical properties. This paper aims to provide insights necessary for advancing type I collagen scaffolds in the CTE applications. METHODS: Initially, the interactions of type I/II collagen with CTE-relevant cells [i.e., articular chondrocytes (ACs) and mesenchymal stem cells (MSCs)] are discussed. Next, the physical features and chemical composition of the scaffolds crucial to support chondrogenic activities of AC and MSC are highlighted. Attempts to optimize the collagen scaffolds by blending with natural/synthetic polymers are described. Hybrid strategy in which collagen and structural polymers are combined in non-blending manner is detailed. RESULTS: Type I collagen is sufficient to support cellular activities of ACs and MSCs; however it shows limited chondrogenic performance than type II collagen. Nonetheless, type I collagen is the clinically feasible option since type II collagen shows arthritogenic potency. Physical features of scaffolds such as internal structure, pore size, stiffness, etc. are shown to be crucial in influencing the differentiation fate and secreting extracellular matrixes from ACs and MSCs. Collagen can be blended with native or synthetic polymer to improve the mechanical and bioactivities of final composites. However, the versatility of blending strategy is limited due to denaturation of type I collagen at harsh processing condition. Hybrid strategy is successful in maximizing bioactivity of collagen scaffolds and mechanical robustness of structural polymer. CONCLUSION: Considering the previous improvements of physical and compositional properties of collagen scaffolds and recent manufacturing developments of structural polymer, it is concluded that hybrid strategy is a promising approach to advance further collagen-based scaffolds in CTE. Keywords Cartilage tissue engineering Á Type I collagen Á Articular chondrocytes Á Mesenchymal stem cells Á Hybrid scaffolds

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“…Collagen plays an important structural role in the extracellular matrix of many different tissues. It is also capable of interacting with the following integrins: α1β1, α2β1, α10β1, and α11β1 (Langholz et al, 1995;Zhang et al, 2003;Hamaia et al, 2017). Furthermore, collagen can efficiently attract platelets to damaged blood vessels to prevent extravascular bleeding.…”

Section: A C Bmentioning

confidence: 99%

Integrin-Ligand Interactions in Inflammation, Cancer, and Metabolic Disease: Insights Into the Multifaceted Roles of an Emerging Ligand Irisin

Park

Myint

Ito

et al. 2020

Front. Cell Dev. Biol.

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Integrins are transmembrane proteins that mediate cellular adhesion and migration to neighboring cells or the extracellular matrix, which is essential for cells to undertake diverse physiological and pathological pathways. For integrin activation and ligand binding, bidirectional signaling across the cell membrane is needed. Integrins aberrantly activated under pathologic conditions facilitate cellular infiltration into tissues, thereby causing inflammatory or tumorigenic progressions. Thus, integrins have emerged to the forefront as promising targets for developing therapeutics to treat autoimmune and cancer diseases. In contrast, it remains a fact that integrin-ligand interactions are beneficial for improving the health status of different tissues. Among these ligands, irisin, a myokine produced mainly by skeletal muscles in an exercise-dependent manner, has been shown to bind to integrin αVβ5, alleviating symptoms under unfavorable conditions. These findings may provide insights into some of the underlying mechanisms by which exercise improves quality of life. This review will discuss the current understanding of integrin-ligand interactions in both health and disease. Likewise, we not only explain how diverse ligands play different roles in mediating cellular functions under both conditions via their interactions with integrins, but also specifically highlight the potential roles of the emerging ligand irisin in inflammation, cancer, and metabolic disease.

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Unique charge-dependent constraint on collagen recognition by integrin α10β1

Cited by 18 publications

References 42 publications

The binding capacity of α1β1-, α2β1- and α10β1-integrins depends on non-collagenous surface macromolecules rather than the collagens in cartilage fibrils

The binding capacity of α1β1-, α2β1- and α10β1-integrins depends on non-collagenous surface macromolecules rather than the collagens in cartilage fibrils

Collagen Scaffolds in Cartilage Tissue Engineering and Relevant Approaches for Future Development

Integrin-Ligand Interactions in Inflammation, Cancer, and Metabolic Disease: Insights Into the Multifaceted Roles of an Emerging Ligand Irisin

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