Evidence for the location of a binding sequence for the α2β1 integrin of endothelial cells, in the β1 subunit of laminin

Underwood, P.A.; Bennett, F.A.; Kirkpatrick, Alan; Bean, Penny; Moss, Bernard

doi:10.1042/bj3090765

Cited by 38 publications

(18 citation statements)

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“…α1β1 and α2β1 integrins are involved in binding to native collagen type I while αvβ3 is activated in response to denatured collagen type I [56,[59][60][61][62]. The α2β1 integrin binds to the GFOGER sequence in native collagen type I and does not bind to denatured collagen type I [60,62,[63][64][65]. The αvβ3 integrin binds to denatured collagen type I almost exclusively via matricryptic RGD sequences that are exposed upon denaturation and unwinding of the triple helix [59,61,[66][67][68].…”

Section: Discussionmentioning

confidence: 99%

Phagocytosis and remodeling of collagen matrices

Abraham

Dice

Lee

et al. 2007

Experimental Cell Research

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The biodegradation of collagen and the deposition of new collagen-based extracellular matrices are of central importance in tissue remodeling and function. Similarly, for collagen-based biomaterials used in tissue engineering, the degradation of collagen scaffolds with accompanying cellular infiltration and generation of new extracellular matrix is critical for integration of in vitro grown tissues in vivo. In earlier studies we observed significant impact of collagen structure on primary lung fibroblast behavior in vitro in terms of collagen uptake and matrix remodeling. Therefore, in the present work, the response of human fibroblasts (IMR-90) to the structural state of collagen was studied with respect to phagocytosis in the presence and absence of inhibitors. Protein content and transcript levels for Collagen I (Col-1), Matrix Metalloproteinase 1 (MMP-1), Matrix Metalloproteinase 2 (MMP-2), Tissue Inhibitor of Matrix Metalloproteinase 1 (TIMP-1), Tissue Inhibitor of Matrix Metalloproteinase 2 (TIMP-2), and Heat Shock Protein 70 (HSP-70) were characterized as a function of collagen matrix concentration, structure and cell culture time to assess effects on cellular collagen matrix remodeling processes. Phagocytosis of collagen was assessed quantitatively by uptake of collagen coated fluorescent beads incorporated into the pre-formed collagen matrices. Significantly higher levels of collagen phagocytosis were observed for the cells grown on the denatured collagen vs. native collagen matrices. Significant reduction in collagen phagocytosis was observed by blocking several phagocytosis pathways when the cells were grown on denatured collagen versus non-denatured collagen. Collagen phagocytosis inhibition effects were significantly greater for PDL57 IMR-90 cells versus PDL48 cells, reflecting a reduced number of collagen processing pathways available to the older cells. Transcript levels related to the deposition of new extracellular matrix proteins varied as a function of the structure of the collagen matrix presented to the cells. A four-fold increase in transcript level of Col-1 and a higher level of collagen matrix incorporation were observed for cells grown on denatured collagen versus cells grown on non-denatured collagen. The data suggest that biomaterial matrices incorporating denatured collagen may promote more active remodeling toward new extracellular matrices in comparison to cells grown on non-denatured collagen. A similar effect of cellular action toward denatured (wound-related) collagen in the remodeling of tissues in vivo may have significant impact on tissue regeneration as well as the progression of collagen-related diseases.

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Section: Discussionmentioning

confidence: 99%

Phagocytosis and remodeling of collagen matrices

Abraham

Dice

Lee

et al. 2007

Experimental Cell Research

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“…laminin. [72][73][74] RGD sequence has been extensively applied in modifying synthetic biomaterials to provide cell-adhesive sites.…”

Section: -70mentioning

confidence: 99%

Biochemical and Biophysical Cues in Matrix Design for Chronic and Diabetic Wound Treatment

Xiao

Ahadian

Radišić

2017

Tissue Engineering Part B: Reviews

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Progress in biomaterial science and engineering and increasing knowledge in cell biology have enabled us to develop functional biomaterials providing appropriate biochemical and biophysical cues for tissue regeneration applications. Tissue regeneration is particularly important to treat chronic wounds of people with diabetes. Understanding and controlling the cellular microenvironment of the wound tissue are important to improve the wound healing process. In this study, we review different biochemical (e.g., growth factors, peptides, DNA, and RNA) and biophysical (e.g., topographical guidance, pressure, electrical stimulation, and pulsed electromagnetic field) cues providing a functional and instructive acellular matrix to heal diabetic chronic wounds. The biochemical and biophysical signals generally regulate cell-matrix interactions and cell behavior and function inducing the tissue regeneration for chronic wounds. Some technologies and devices have already been developed and used in the clinic employing biochemical and biophysical cues for wound healing applications. These technologies can be integrated with smart biomaterials to deliver therapeutic agents to the wound tissue in a precise and controllable manner. This review provides useful guidance in understanding molecular mechanisms and signals in the healing of diabetic chronic wounds and in designing instructive biomaterials to treat them.

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“…Probably the best-known sequence binding to integrins is arginine-glycine-aspartic acid (RGD). It is found in many ECM proteins, including fibronectin, laminin, collagen type-IV, tenascin and thrombospondin (Benoit & Anseth, 2005a;Comisar et al, 2007;Underwood et al, 1995). However, the RGD motif and its derivatives are not the only integrin-binding sequence used for scaffold modification.…”

Section: Fibronectin and Small Cell Adhesion Motifsmentioning

confidence: 99%