Matricellular proteins: extracellular modulators of cell function

Börnstein, Paul; Sage, E. Helene

doi:10.1016/s0955-0674(02)00361-7

Cited by 860 publications

(718 citation statements)

References 67 publications

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“…These proteins, usually referred as matricellular proteins, though not being structurally related, regulate similar biological functions during embryonic development, tissue injury and cancer development mainly by promoting adhesion, migration and survival of cells (Bornstein and Sage, 2002). While absent in almost all normal healthy adult tissues, expression of SPARC for example is restored in many cancer types (Framson and Sage, 2004) and it has been demonstrated that SPARC overexpression is correlated with an increase in invasiveness and survival of cancer cells (Rich et al, 2003;Shi et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

Periostin promotes invasiveness and resistance of pancreatic cancer cells to hypoxia-induced cell death: role of the β4 integrin and the PI3k pathway

Baril¹,

Gangeswaran²,

Mahon³

et al. 2006

Oncogene

256

244

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Pancreatic ductal adenocarcinoma is a devastating disease, characterized by a rapid progression and poor treatment response. Using gene expression profiling of pancreatic cancer tissues, we previously identified periostin as a potential diagnostic and therapeutic target. In this study, we report the overexpression of periostin in a larger set of pancreatic cancer tissues and show that although the periostin transcript is exclusively expressed in tumour cells, the protein product is only detected in the extracellular matrix adjacent to cancer cells. Using an enzyme-linked immunosorbent assay (ELISA) assay, we show significantly increased levels of periostin in the sera of pancreatic cancer patients compared to non-cancer controls. We demonstrate that periostin promotes the invasiveness of tumour cells by increasing the motility of cells without inducing expression of proteases, and enhances the survival of tumour cells exposed to hypoxic conditions. At the molecular level, we provide evidence that the a 6 b 4 integrin complex acts as the cell receptor of periostin in pancreatic cancer cells and that interaction promotes phosphorylation of focal adhesion kinase (FAK) and protein kinase B (AKT) though activation of the PI3 kinase pathway, but not the RAS/MEK/ERK pathway. These findings suggest an important role of periostin in pancreatic cancer and provide a rationale to study periostin for diagnostic and therapeutic applications.

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Section: Discussionmentioning

confidence: 99%

Periostin promotes invasiveness and resistance of pancreatic cancer cells to hypoxia-induced cell death: role of the β4 integrin and the PI3k pathway

Baril¹,

Gangeswaran²,

Mahon³

et al. 2006

Oncogene

256

244

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show abstract

“…Reports of POSTN mRNA upregulation [11][12][13] and our data shown here demonstrating abundant periostin in a contractile fibrosis like DD, therefore, are not altogether unexpected. 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.…”

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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“…(Bornstein and Sage 2002) Typically, they interact with both other ECM components and cell-surface receptors, often intervening in their interactions. They are often highly expressed during differentiation, wound healing, tissue remodeling and similar processes.…”

Section: Matricellular Proteinsmentioning

confidence: 99%

“…Thrombospondins 1 and 2 form homotrimeric structures and are considered to be matricellular proteins, while thrombospondins 3 and 4 are structurally somewhat different and are not considered to be matricellular proteins. (Bornstein and Sage 2002) Thrombospondin 1 is thought to be a major activator of TGFβ, most isoforms of which are present in latent forms that need activation for function. (Crawford et al 1998) Since TGFβ is thought to be of significance in affecting the normal and glaucomatous ECMs of the outflow pathway and has been shown to modify outflow facility, this may be of considerable importance.…”

Section: Matricellular Proteinsmentioning

confidence: 99%

“…(Ghert et al 2001) It has both adhesive and anti-adhesive effects and is involved in cell migration, ECM remodeling, development, tumorogenesis and wound healing. (Chiquet-Ehrismann et al 1988;Vainio et al 1989;Ghert et al 2001;Bornstein and Sage 2002;Chiquet-Ehrismann and Chiquet 2003;ChiquetEhrismann 2004) Some of these processes occur via tenascin C's association with fibronectin fibrils and effects on fibronectin-cell interactions. (Chung et al 1995;Ghert et al 2001) In addition to exhibiting changes in levels with various treatments that modify outflow facility (see later), tenascin C also undergoes a number of changes in mRNA splicing (Keller et al, manuscript in preparation).…”

Section: Matricellular Proteinsmentioning

confidence: 99%

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Extracellular matrix in the trabecular meshwork

Acott

Kelley

2008

Experimental Eye Research

417

443

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The extracellular matrix (ECM) of the trabecular meshwork (TM) is thought to be important in regulating intraocular pressure (IOP) in both normal and glaucomatous eyes. IOP is regulated primarily by a fluid resistance to aqueous humor outflow. However, neither the exact site nor the identity of the normal resistance to aqueous humor outflow has been established. Whether the site and nature of the increased outflow resistance, which is associated with open-angle glaucoma, is the same or different from the normal resistance is also unclear.The ECMs of the TM beams, juxtacanalicular region (JCT) and Schlemm's canal (SC) inner wall are comprised of fibrillar and non-fibrillar collagens, elastin-containing microfibrils, matricellular and structural organizing proteins, glycosaminoglycans (GAGs) and proteoglycans. Both basement membranes and stromal ECM are present in the TM beams and JCT region. Cell adhesion proteins, cell surface ECM receptors and associated binding proteins are also present in the beams, JCT and SC inner wall region.The outflow pathway ECM is relatively dynamic, undergoing constant turnover and remodeling. Regulated changes in enzymes responsible for ECM degradation and biosynthetic replacement are observed. IOP homeostasis, triggered by pressure changes or mechanical stretching of the TM, appears to involve ECM turnover. Several cytokines, growth factors and drugs, which affect the outflow resistance, change ECM component expression, mRNA alternative splicing, cellular cytoskeletal organization or all of these. Changes in ECM associated with open-angle glaucoma have been identified.

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Matricellular proteins: extracellular modulators of cell function

Cited by 860 publications

References 67 publications

Periostin promotes invasiveness and resistance of pancreatic cancer cells to hypoxia-induced cell death: role of the β4 integrin and the PI3k pathway

Periostin promotes invasiveness and resistance of pancreatic cancer cells to hypoxia-induced cell death: role of the β4 integrin and the PI3k pathway

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

Extracellular matrix in the trabecular meshwork

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