Extracellular matrix dynamics in development and regenerative medicine

Daley, William P.; Peters, Sarah; Larsen, Melinda

doi:10.1242/jcs.006064

Cited by 868 publications

(751 citation statements)

References 134 publications

(104 reference statements)

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“…Periostin is a member of a subset of secreted ECM-associated molecules termed "matri-cellular" proteins [48][49][50] that modulate interactions with structural components of the ECM, such as collagens, and a variety of cell surface receptors, such as integrins, to regulate cellular differentiation in development [51] and connective tissue disease [52]. Based on these data and numerous studies demonstrating that the ECM can potently regulate cellular differentiation [53][54][55][56][57], where possible we incorporated our periostin treatments into the collagen substrate, rather than simply amending the tissue culture media, to more closely replicate in vivo conditions. Periostin has been shown to promote collagen fibrillogenesis and alter the deposition of ECM proteins in other systems [58] and larger scale microarray studies have identified COL1A1 mRNA, encoding the collagen α1 component of heterotrimeric and homotrimeric type-1 collagen [59], as up-regulated in DD cord [11,12].…”

Section: Discussionmentioning

confidence: 99%

Periostin differentially induces proliferation, contraction and apoptosis of primary Dupuytren's disease and adjacent palmar fascia cells

Vi¹,

Feng²,

Zhu³

et al. 2009

Experimental Cell Research

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Dupuytren's disease, (DD), is a fibroproliferative condition of the palmar fascia in the hand, typically resulting in permanent contracture of one or more fingers. This fibromatosis is similar to scarring and other fibroses in displaying excess collagen secretion and contractile myofibroblast differentiation. In this report we expand on previous data demonstrating that POSTN mRNA, which encodes the extra-cellular matrix protein periostin, is up-regulated in Dupuytren's disease cord tissue relative to phenotypically normal palmar fascia. We demonstrate that the protein product of POSTN, periostin, is abundant in Dupuytren's disease cord tissue while little or no periostin immunoreactivity is evident in patient-matched control tissues. The relevance of periostin up-regulation in DD was assessed in primary cultures of cells derived from diseased and phenotypically unaffected palmar fascia from the same patients. These cells were grown in type-1 collagen-enriched culture conditions with or without periostin addition to more closely replicate the in vivo environment. Periostinwas found to differentially regulate the apoptosis, proliferation, α smooth muscle actin expression and stressed Fibroblast Populated Collagen Lattice contraction of these cell types. We hypothesize that periostin, secreted by disease cord myofibroblasts into the extra-cellular matrix, promotes the transition of resident fibroblasts in the palmar fascia toward a myofibroblast phenotype, thereby promoting disease progression.

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Section: Discussionmentioning

confidence: 99%

Periostin differentially induces proliferation, contraction and apoptosis of primary Dupuytren's disease and adjacent palmar fascia cells

Vi¹,

Feng²,

Zhu³

et al. 2009

Experimental Cell Research

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“…Changes in these interactions as a consequence of ECM remodeling give rise to specific cell‐signaling and intracellular cascades. These processes are central to physiology and pathological processes, such as tissue self‐repair and tumorigenesis 1b,1c. As mimics of such dynamic interactions, artificial matrices with the reversible display of bioactive ligands have attracted much attention.…”

mentioning

confidence: 99%

An Epitope‐Imprinted Biointerface with Dynamic Bioactivity for Modulating Cell–Biomaterial Interactions

et al. 2017

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In this study, an epitope‐imprinting strategy was employed for the dynamic display of bioactive ligands on a material interface. An imprinted surface was initially designed to exhibit specific affinity towards a short peptide (i.e., the epitope). This surface was subsequently used to anchor an epitope‐tagged cell‐adhesive peptide ligand (RGD: Arg‐Gly‐Asp). Owing to reversible epitope‐binding affinity, ligand presentation and thereby cell adhesion could be controlled. As compared to current strategies for the fabrication of dynamic biointerfaces, for example, through reversible covalent or host–guest interactions, such a molecularly tunable dynamic system based on a surface‐imprinting process may unlock new applications in in situ cell biology, diagnostics, and regenerative medicine.

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“…The ECM determines cell behavior by manipulating cell shape, proliferation, migration, differentiation, and death. 71 Scarless regenerative healing is an intrinsic property of the fetal skin. 72 Major differences in the ECM of the fetal and the adult skin account for the sharp contrast in healing phenotype between the fetus and adult skin.…”

Section: Mirna and Regenerative Medicinementioning

confidence: 99%