Vascular Smooth Muscle Cells Orchestrate the Assembly of Type I Collagen via α2β1 Integrin, RhoA, and Fibronectin Polymerization

Li, Shaohua; Diepstraten, Caroline Van Den; D’Souza, Sudhir J.A.; Chan, Bosco M.C.; Pickering, J. Geoffrey

doi:10.1016/s0002-9440(10)63464-5

Cited by 151 publications

(152 citation statements)

References 42 publications

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“…The absence of certain ECM proteins can lead to impaired collagen fibril formation even when collagen synthesis and secretion are normal (51,88). In addition, collagen-binding integrins can regulate type I and III collagen fibril assembly (45,88). This requirement for cells may reflect differences in the concentration of collagen molecules that are available for assembly in cell-based versus purified systems, differences in the presence of accessory proteins that can regulate collagen binding interactions, and differences in the formation of higher order fibrillar structures.…”

Section: Discussionmentioning

confidence: 99%

Fibronectin-dependent collagen I deposition modulates the cell response to fibronectin

Sottile

Shi²,

Rublyevska³

et al. 2007

American Journal of Physiology-Cell Physiology

150

178

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munication between cells and the extracellular matrix (ECM) is critical for regulation of cell growth, survival, migration, and differentiation. Remodeling of the ECM can occur under normal physiological conditions, as a result of tissue injury, and in certain pathological conditions. ECM remodeling leads to alterations in ECM composition and organization that can alter many aspects of cell behavior, including cell migration. The cell migratory response varies depending on the type, amount, and organization of ECM molecules present, as well as the integrin and proteoglycan repertoire of the cells. We and others have shown that the deposition of several ECM molecules, including collagen types I and III, depends on the presence and stability of ECM fibronectin. Hence, the effect of fibronectin and fibronectin matrix on cell function may partially depend on its ability to direct the deposition of collagen in the ECM. In this study, we used collagen-binding fibronectin mutants and recombinant peptides that interfere with fibronectin-collagen binding to show that fibronectindependent collagen I deposition regulates the cell migratory response to fibronectin. These data show that the ability of fibronectin to organize other proteins in the ECM is an important aspect of fibronectin function and highlight the importance of understanding how interactions between ECM proteins influence cell behavior. extracellular matrix; contractility CELL FATE DECISIONS involving cell growth, differentiation, and survival rely on the ability of cells to coordinate diverse input from cytokines, growth factors, and extracellular matrix (ECM) molecules (3,89,94). The effects of ECM molecules on cell behavior are particularly complicated, since they depend on the mixture of ECM molecules that are present, the way the ECM proteins are organized and presented to cells, and the presence of proteases, protease inhibitors, and endocytic mechanisms that can alter the levels of ECM proteins and ECM degradation products. Understanding how ECM proteins act in concert to elicit biological effects is key to understanding how cell-ECM interactions maintain normal tissue function and influence the cell response to tissue injury.There is much data showing that mixtures of different ECM molecules can have effects distinct from that of a single ECM molecule. For example, coating dishes with a combination of tenascin C and fibronectin results in altered expression of matrix metalloproteinases (MMPs) (86), whereas addition of tenascin C to dishes coated with fibrin and fibronectin results in altered cytoskeletal organization (90) compared with cells seeded in the absence of tenascin C. The ability of fibronectin null cells to produce a fibronectin matrix is also dependent on the combination of matrix proteins present on the substrate (4). Furthermore, mixed collagen and fibronectin substrates have been shown to alter the response of endothelial cells to shear stress compared with their response to fibronectin alone (59). Similarly, addition of soluble matric...

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Section: Discussionmentioning

confidence: 99%

Fibronectin-dependent collagen I deposition modulates the cell response to fibronectin

Sottile

Shi²,

Rublyevska³

et al. 2007

American Journal of Physiology-Cell Physiology

150

178

View full text Add to dashboard Cite

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“…These functions are indeed controlled by specific adhesion receptors that serve as a transmembrane link between the ECM and the cytoskeleton [18]. As a consequence of this link, the ECM can control cell activity, while the cell can affect the remodelling of the ECM [18][19][20][21][22][23][24]. The most important adhesion receptors in this process are the integrins [18].…”

Section: Discussionmentioning

confidence: 99%

Substrate-induced phenotypic switches of human smooth muscle cells: anin vitrostudy of in-stent restenosis activation pathways

Guildford

Stewart

Morris

et al. 2010

J. R. Soc. Interface.

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In-stent restenosis is a clinical complication following coronary angioplasty caused by the implantation of the metal device in the atherosclerotic vessel. Histological examination has shown a clear contribution of both inflammatory and smooth muscle cells (SMCs) to the deposition of an excess of neointimal tissue. However, the sequence of events leading to clinically relevant restenosis is unknown. This paper aims to study the phenotype of SMCs when adhering on substrates and exposed to biochemical stimuli typical of the early phases of stent implantation. In particular, human SMC phenotype was studied when adhering on extracellular matrix-like material (collagen-rich gel), thrombus-like material (fibrin gel) and stent material (stainless steel) in the presence or absence of a platelet-derived growth factor (PDGF) stimulus. Cells on the collagen and fibrin-rich substrates maintained their contractile phenotype. By contrast, cells on stainless steel acquired a secretory phenotype with a proliferation rate 50 per cent higher than cells on the natural substrates. Cells on stainless steel also showed an increase in PDGF-BB receptor expression, thus explaining the increase in proliferation observed when cells were subject to PDGF-BB stimuli. The stainless steel substrate also promoted a different pattern of b1-integrin localization and an altered expression of hyaluronan (HA) synthase isoforms where the synthesis of highmolecular-weight HA seemed to be favoured. These findings highlighted the induction of a phenotypic pattern in SMC by the stainless steel substrate whereby the formation of a HA-rich neointimal tissue is enhanced.

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“…Type I collagen fibrils do not form in the absence of an FN matrix (20,31,32), and FN is believed to serve as a scaffold for collagen fibril formation (33). As shown in Fig.…”

Section: Gј Ementioning

confidence: 99%

Regulation of Matrix Assembly through Rigidity-dependent Fibronectin Conformational Changes

Carraher

Schwarzbauer

2013

Journal of Biological Chemistry

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Background: Cell behavior is affected by changes in extracellular matrix stiffness during disease progression. Results: Fibronectin matrix assembly is inhibited on soft substrates but can be restored by manipulating cell-fibronectin binding or by partially unfolding substrate fibronectin. Conclusion: On soft substrates, cells are deficient in integrin-fibronectin bond strength and therefore cannot induce fibronectin conformational changes required for assembly. Significance: Rigidity-dependent changes in fibronectin conformation provide a novel mechanism for mechanotransduction.

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Vascular Smooth Muscle Cells Orchestrate the Assembly of Type I Collagen via α2β1 Integrin, RhoA, and Fibronectin Polymerization

Cited by 151 publications

References 42 publications

Fibronectin-dependent collagen I deposition modulates the cell response to fibronectin

Fibronectin-dependent collagen I deposition modulates the cell response to fibronectin

Substrate-induced phenotypic switches of human smooth muscle cells: anin vitrostudy of in-stent restenosis activation pathways

Regulation of Matrix Assembly through Rigidity-dependent Fibronectin Conformational Changes

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