The integrin–collagen connection – a glue for tissue repair?

Zeltz, Cédric; Gullberg, Donald

doi:10.1242/jcs.180992

Cited by 174 publications

(127 citation statements)

References 184 publications

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“…Alternatively, a material lacking in cell adhesion sites, like alginate, prevents cells from binding, encouraging a chondrogenic morphology. [95,96] Cell morphology, such as a fibroblastic or chondrogenic morphology, has been shown to be an indicator for cell behavior and matrix production. [97] Scaffold mechanical properties are known to direct stem cell fate, where materials with stiffer structures promote osteogenic differentiation.…”

Section: Cellular Contributionsmentioning

confidence: 99%

Next generation tissue engineering of orthopedic soft tissue-to-bone interfaces

et al. 2017

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Soft tissue-to-bone interfaces are complex structures that consist of gradients of extracellular matrix materials, cell phenotypes, and biochemical signals. These interfaces, called entheses for ligaments, tendons, and the meniscus, are crucial to joint function, transferring mechanical loads and stabilizing orthopedic joints. When injuries occur to connected soft tissue, the enthesis must be re-established to restore function, but due to structural complexity, repair has proven challenging. Tissue engineering offers a promising solution for regenerating these tissues. This prospective review discusses methodologies for tissue engineering the enthesis, outlined in three key design inputs: materials processing methods, cellular contributions, and biochemical factors.

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Section: Cellular Contributionsmentioning

confidence: 99%

Next generation tissue engineering of orthopedic soft tissue-to-bone interfaces

et al. 2017

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“…Recent results have shown that α 1 β 1 , α 2 β 1 , and α 11 β 1 integrins recognize a triple-helical GFOGER (GlyPhe-Hyp-Gly-Glu-Arg amino acid) sequence present on several collagens (including COL1). 25 To determine whether the GFOGER sequence is the binding site for MVs, we chemically synthesized a soluble GFOGER peptide and evaluated its role in the interaction between COL1 and MVs.…”

Section: The Gfoger Sequence Is Involved In the Mvs' Interaction Withmentioning

confidence: 99%

Oligogalacturonic Acid Inhibits Vascular Calcification by Two Mechanisms

Hodroge

Trecherel

Cornu

et al. 2017

ATVB

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Objective— Cardiovascular diseases constitute the leading cause of mortality worldwide. Calcification of the vessel wall is associated with cardiovascular morbidity and mortality in patients having many diseases, including diabetes mellitus, atherosclerosis, and chronic kidney disease. Vascular calcification is actively regulated by inductive and inhibitory mechanisms (including vascular smooth muscle cell adaptation) and results from an active osteogenic process. During the calcification process, extracellular vesicles (also known as matrix vesicles) released by vascular smooth muscle cells interact with type I collagen and then act as nucleating foci for calcium crystallization. Our primary objective was to identify new, natural molecules that inhibit the vascular calcification process. Approach and Results— We have found that oligogalacturonic acids (obtained by the acid hydrolysis of polygalacturonic acid) reduce in vitro inorganic phosphate–induced calcification of vascular smooth muscle cells by 80% and inorganic phosphate–induced calcification of isolated rat aortic rings by 50%. A specific oligogalacturonic acid with a degree of polymerization of 8 (DP8) was found to inhibit the expression of osteogenic markers and, thus, prevent the conversion of vascular smooth muscle cells into osteoblast-like cells. We also evidenced in biochemical and immunofluorescence assays a direct interaction between matrix vesicles and type I collagen via the GFOGER sequence (where single letter amino acid nomenclature is used, O=hydroxyproline) thought to be involved in interactions with several pairs of integrins. Conclusions— DP8 inhibits vascular calcification development mainly by inhibition of osteogenic marker expression but also partly by masking the GFOGER sequence—thereby, preventing matrix vesicles from binding to type I collagen.

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“…The relatively mild phenotypes exhibited by mice lacking collagen-binding integrins suggest that, apart from the redundancy expected from the expression of other types of nonintegrin collagen receptors, there is also redundancy between different collagen-binding integrins (Zeltz and Gullberg 2016;Zeltz et al 2014). Early work on integrins as therapeutic targets focused on the development of integrin-blocking monoclonal antibodies.…”

Section: Targeting Collagen Adhesion Receptors In Anti-fibrotic Theramentioning

confidence: 99%

Contribution of collagen adhesion receptors to tissue fibrosis

Coelho

McCulloch

2016

Cell Tissue Res

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Fibrosis is the result of a wound-healing response that fails to restore normal tissue structure function. One of the critical hallmarks of fibrosis is disrupted collagen remodeling. In tissue homeostasis, the production, deposition and organization of collagen is balanced by the degradation and remodeling of collagen within the existing matrix. After injury or chronic infection, tissues initiate a wound-healing response that is intended to create a new ECM for restoring tissue structure and function. If the wound-healing response is dysregulated or if the tissue injury or infection is severe or long-lasting, collagen deposition exceeds collagen degradation and the tissue repair process leads to fibrosis. The fibrotic repair response is extraordinarily complex and involves a wide spectrum of cells, signaling pathways and regulatory systems, some of which can be readily disrupted and thereby contribute to fibrotic lesions. The dysregulated collagen remodeling is a common end-point of all fibrotic disorders, and one of the rate-limiting steps of collagen remodeling is the binding of cells to collagen fibrils by specific cell adhesion receptors. In this review, we describe how the expression and function of collagen adhesion receptors contribute to collagen processing events that contribute to tissue fibrosis. Graphical abstract Balance between collagen remodeling in health and disease.

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The integrin–collagen connection – a glue for tissue repair?

Cited by 174 publications

References 184 publications

Next generation tissue engineering of orthopedic soft tissue-to-bone interfaces

Next generation tissue engineering of orthopedic soft tissue-to-bone interfaces

Oligogalacturonic Acid Inhibits Vascular Calcification by Two Mechanisms

Contribution of collagen adhesion receptors to tissue fibrosis

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