Syndecans-1 and -4 Are Induced During Wound Repair of Neonatal but Not Fetal Skin

Gallo, Richard L.; Kim, Choll; Kokenyesi, Robert; Adzick, N. Scott; Bernfield, Merton

doi:10.1111/1523-1747.ep12365571

Cited by 157 publications

(143 citation statements)

References 41 publications

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“…Syndecan-1 and syndecan-4 expression is induced in the skin after incisional wounding [48,49]. Syndecan-4 expression is induced in carotid artery tissue after balloon-catheter injury of the vessel [50].…”

Section: Expression Of Syndecansmentioning

confidence: 99%

Syndecans: multifunctional cell-surface co-receptors

Carey

1997

Biochemical Journal

621

497

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This review will summarize our current state of knowledge of the structure, biochemical properties and functions of syndecans, a family of transmembrane heparan sulphate proteoglycans. Syndecans bind a variety of extracellular ligands via their covalently attached heparan sulphate chains. Syndecans have been proposed to play a role in a variety of cellular functions, including cell proliferation and cell–matrix and cell–cell adhesion. Syndecan expression is highly regulated and is cell-type- and developmental-stage-specific. The main function of syndecans appears to be to modulate the ligand-dependent activation of primary signalling receptors at the cell surface. Principal functions of the syndecan core proteins are to target the heparan sulphate chains to the appropriate plasma-membrane compartment and to interact with components of the actin-based cytoskeleton. Several functions of the syndecans, including syndecan oligomerization and actin cytoskeleton association, have been localized to specific structural domains of syndecan core proteins.

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Section: Expression Of Syndecansmentioning

confidence: 99%

Syndecans: multifunctional cell-surface co-receptors

Carey

1997

Biochemical Journal

621

497

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“…Its expression by fibroblasts, among other cell types, is transiently up-regulated during tissue repair (Gallo et al, 1996). In addition, syndecan-4-null mice develop normally but show abnormal wound healing (Echtermeyer et al, 2001).…”

Section: Cell Contractility Requires Syndecan-4 Signalingmentioning

confidence: 99%

“…Transmembrane heparan sulfate proteoglycans (HSPGs) of the syndecan family bind to ECM proteins and cooperate with heterodimeric integrin receptors to regulate cell adhesive activities (Bloom et al, 1999;Kusano et al, 2000;. One member of this family, syndecan-4, is up-regulated during tissue repair (Gallo et al, 1996) and syndecan-4 -null mice show defects in wound healing (Echtermeyer et al, 2001). Syndecan-4 binds to FN and probably to tenascin-C via its GAG side chains (Salmivirta et al, 1991;.…”

Section: Introductionmentioning

confidence: 99%

Coregulation of Fibronectin Signaling and Matrix Contraction by Tenascin-C and Syndecan-4

Midwood

Valenick

Hsia

et al. 2004

MBoC

133

139

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Syndecan-4 is a ubiquitously expressed heparan sulfate proteoglycan that modulates cell interactions with the extracellular matrix. It is transiently up-regulated during tissue repair by cells that mediate wound healing. Here, we report that syndecan-4 is essential for optimal fibroblast response to the three-dimensional fibrin-fibronectin provisional matrix that is deposited upon tissue injury. Interference with syndecan-4 function inhibits matrix contraction by preventing cell spreading, actin stress fiber formation, and activation of focal adhesion kinase and RhoA mediated-intracellular signaling pathways. Tenascin-C is an extracellular matrix protein that regulates cell response to fibronectin within the provisional matrix. Syndecan-4 is also required for tenascin-C action. Inhibition of syndecan-4 function suppresses tenascin-C activity and overexpression of syndecan-4 circumvents the effects of tenascin-C. In this way, tenascin-C and syndecan-4 work together to control fibroblast morphology and signaling and regulate events such as matrix contraction that are essential for efficient tissue repair. INTRODUCTIONTissue architecture is defined by the three-dimensional (3D) organization of the proteins and proteoglycans that comprise the extracellular matrix (ECM). Individual ECM components influence cell arrangements and activities through binding to transmembrane receptors, thus initiating intracellular signaling and altering gene expression and other downstream events. Tissues undergo continual maintenance and remodeling through controlled deposition and removal of specific ECM components. These changes in ECM composition and organization modulate cell behaviors and serve important roles throughout development and in the adult during both physiological and pathological processes (Lukashev and Werb, 1998).The provisional matrix that forms at sites of tissue injury undergoes extensive remodeling and turnover during wound repair. Composed predominantly of covalently cross-linked fibrin and plasma fibronectin (FN), this fibrin-FN provisional matrix coordinates the activities of cells involved in wound repair. It is remodeled over time to recapitulate normal tissue and this remodeling involves cellmediated contraction and deposition of new FN-rich matrix (Clark, 1996;Midwood et al., 2004). FN, a major component of the matrix, is a ubiquitously expressed, multifunctional extracellular glycoprotein that promotes cell adhesion. It controls many intracellular pathways and influences a wide range of cell functions (Hynes, 1990). For example, FN within a 3D fibrin-FN provisional matrix initiates signaling via focal adhesion kinase (FAK) and RhoA in order to promote fibroblast spreading, stress fiber formation, and focal adhesion assembly (Wenk et al., 2000;.The provisional matrix contacts many other ECM proteins that are induced at different stages of tissue repair, including thrombospondins, SPARC, and tenascin-C. These proteins are specifically up-regulated at wound sites where they modulate cell-ECM interactions (re...

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“…The level of syndecan-1 expression in skin keratinocytes is upregulated during wound healing. Both mRNA and protein levels of syndecan-1 are induced up to 20-fold in migrating keratinocytes (Elenius et al, 1991;Gallo et al, 1996). Furthermore, during development, e.g.…”

Section: Introductionmentioning

confidence: 99%

The activation and composition of FiRE (an FGF-inducible response element) differ in a cell type- and growth factor-specific manner

1998

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The expression of the heparan sulfate proteoglycan, syndecan-1, is induced both in keratinocytes and in ®broblasts during development and tissue regeneration. Here we report that in keratinocytes the syndecan-1 gene was stimulated by EGF but not by FGF-2. In ®broblasts it was stimulated by FGF-2 but not by EGF. Likewise, the recently discovered FGF-inducible response element (FiRE) on the gene of syndecan-1 was stimulated by FGF-2 in ®broblasts and by EGF in keratinocytes, but not vice versa. The FiRE has two binding sites for an activator protein-1 (AP-1), one for an FGF-inducible nuclear factor (FIN-1) and one for an upstream stimulatory factor-1 (USF-1). The growth factorstimulated binding of these transcription factors, as well as their requirement for FiRE activation, varied between the two cell types. First, although AP-1s were required for activation of FiRE in both cell types, the binding of AP-1 to FiRE was increased by growth factor-stimulation only in ®broblasts and not in keratinocytes. Secondly, FiRE did not bind FIN-1 nor needed the FIN-1 binding site for EGF-stimulated activation in keratinocytes, in contrast to the FGF-stimulated activation of FiRE in ®broblasts. Thirdly, EGF, which did not activate FiRE in ®broblasts, failed to activate FIN-1 in these cells. Finally, an USF-1 binding site that was necessary for activation of FiRE in keratinocytes was not needed in ®broblasts. These data suggest mechanisms by which members of the EGF-and FGF-families can di erentially stimulate transcription through AP-1 regulated elements in a cell type-speci®c manner.

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Syndecans-1 and -4 Are Induced During Wound Repair of Neonatal but Not Fetal Skin

Cited by 157 publications

References 41 publications

Syndecans: multifunctional cell-surface co-receptors

Syndecans: multifunctional cell-surface co-receptors

Coregulation of Fibronectin Signaling and Matrix Contraction by Tenascin-C and Syndecan-4

The activation and composition of FiRE (an FGF-inducible response element) differ in a cell type- and growth factor-specific manner

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