Basic fibroblast growth factor regulates expression of heparan sulfate in human periodontal ligament cells

Shimabukuro, Yoshio; Ichikawa, Tsuneki; Terashima, Yoshimitsu; Iwayama, Tomoaki; Oohara, Hiroyuki; Kajikawa, Tetsuhiro; Kobayashi, Ryohei; Terashima, Hiroyuki; Takedachi, Masahide; Terakura, Mami; Hashikawa, Tomoko; Yamada, Satoru; Murakami, Shinya

doi:10.1016/j.matbio.2007.10.005

Cited by 19 publications

(17 citation statements)

References 46 publications

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“…FGF2 has been shown to modulate expression of GAGs and proteoglycans. In vitro treatment of human periodontal ligament cells with FGF2 resulted in increased heparin sulfate in the supernatant, and may also stimulate HAS1 and HAS2 (37). Has2 is one of three genes encoding HA synthesis and is present during palatogenesis (38).…”

Section: Discussionmentioning

confidence: 99%

Analysis of a gain-of-function FGFR2 Crouzon mutation provides evidence of loss of function activity in the etiology of cleft palate

Snyder‐Warwick¹,

Perlyn

Pan

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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Cleft palate is a common birth defect in humans and is a common phenotype associated with syndromic mutations in fibroblast growth factor receptor 2 (Fgfr2). Cleft palate occurred in nearly all mice homozygous for the Crouzon syndrome mutation C342Y in the mesenchymal splice form of Fgfr2. Mutant embryos showed delayed palate elevation, stage-specific biphasic changes in palate mesenchymal proliferation, and reduced levels of mesenchymal glycosaminoglycans (GAGs). Reduced levels of feedback regulators of FGF signaling suggest that this gain-of-function mutation in FGFR2 ultimately resembles loss of FGF function in palate mesenchyme. Knowledge of how mesenchymal FGF signaling regulates palatal shelf development may ultimately lead to pharmacological approaches to reduce cleft palate incidence in genetically predisposed humans.Crouzon syndrome | fibroblast growth factor receptor 2 | cell proliferation | cell surface receptor | glycosaminoglycan C raniosynostosis syndromes, as well as syndromic and nonsyndromic cleft palate, have been associated with fibroblast growth factor receptor (FGFR) mutations. Of the four highly conserved FGFRs, FGFR2 is the most commonly mutated FGF receptor (1-4). The FGF-FGFR family is involved in multiple intracellular signaling mechanisms in embryonic development, cell growth, wound healing, and tumorigenesis. The FGFRs are receptor tyrosine kinases that signal via a ternary complex of FGFR, FGF, and glycosaminoglycans (GAGs) (5). The ternary complex formation leads to receptor dimerization, autophosphorylation, and activation of downstream signaling cascades (6).FGF-FGFR signaling is active during palatogenesis, and genetic FGF mutations may contribute to 5% of cases of nonsyndromic cleft lip and palate (7). In children with isolated cleft palate, mutations in Fgfr1, Fgfr2, Fgfr3, and Fgf8 have been identified. Additionally, single nucleotide polymorphisms in children with nonsyndromic cleft lip and palate are associated with Fgf3, Fgf7, Fgf10, Fgf18, and Fgfr1, providing confirmation of the importance of the FGF-FGFR system in palate development (7). Knockout mouse models for Fgf10 and Fgfr2b develop cleft palate (8, 9), establishing the necessity of epithelial FGF signaling in normal palatogenesis. Cleft palate in Fgf18 −/− mice (10) suggests that mesenchymal FGF signaling may also be important for palate development.Cleft palate has been associated with both gain-of-function and loss-of-function FGFR mutations (7,(11)(12)(13)(14)(15). Why gain-of-function or loss-of-function mutations result in the same palatal phenotype remains unclear, and understanding this phenomenon may provide additional insight into the pathogenesis of cleft palate. To address this question, we have focused on Crouzon syndrome (CS), a disorder resulting from a missense Fgfr2 mutation that displays an increased incidence of cleft palate in humans (14).CS occurs with an incidence of 12.5 per million births and results from genetic gain-of-function mutations in Fgfr2 (1). Craniofacial anomalies are its hallmark...

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Section: Discussionmentioning

confidence: 99%

Analysis of a gain-of-function FGFR2 Crouzon mutation provides evidence of loss of function activity in the etiology of cleft palate

Snyder‐Warwick¹,

Perlyn

Pan

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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“…In addition, syndecan-1 (CD138; NCBI reference sequence: NP_001006947) is expressed by many cell types including plasma cells. Syndecan-2 (fibroglycan; NCBI reference sequence: NP_002989) shows somewhat restricted expression, limited mainly to fibroblasts and neurons (Ethell et al, 2001;Shimabukuro et al, 2008;Su et al, 2007). The latter is an important site for HSV-1 latency and reactivation (Shukla & Spear, 2001).…”

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confidence: 99%

Syndecan-1 and syndecan-2 play key roles in herpes simplex virus type-1 infection

Bacsa

Karasneh

Dósa

et al. 2010

Journal of General Virology

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Herpes simplex virus type 1 (HSV-1) is an important human pathogen and a leading cause of infectious blindness in the developed world. HSV-1 exploits heparan sulfate proteoglycans (HSPG) for attachment to cells. While the significance of heparan sulphate (HS) moieties in HSV-1 infection is well established, the role of specific proteoglycan core proteins in the infection process remains poorly understood. The objective of this study was to assess the roles of syndecan-1 and syndecan-2 core proteins in HSV-1 infection, both of which are expressed by many HSV-1 target cell types. Our results demonstrate that syndecan-1 and syndecan-2 gene silencing by RNA interference reduces HSV-1 entry, plaque formation and facilitates cell survival. Furthermore, HSV-1 infection increases syndecan-1 and syndecan-2 protein synthesis and a resultant increase in cell surface expression of HS. Our observations suggest that changes in syndecan-1 and syndecan-2 expression levels may be related to active viral infection. Taken together, our findings provide new insights into HSPG functions during HSV-1 entry and spread. INTRODUCTIONHerpes simplex virus type 1 (HSV-1) is a clinically important pathogen and a leading cause of infectious blindness in the developed world. HSV-1 productively infects epithelial cells and establishes latent infection in sensory ganglia for the life of the host (Kumaraguru & Rouse, 2002;Terasaka et al., 2010). Currently, no cure exists against HSV-1, which can be transmitted via asymptomatic shedding by latently infected individuals (Hill & Clement, 2009). Prevention of virus transmission to uninfected people is a real challenge compounded by our limited understanding of HSV-1-host cell interactions including virus entry, which is the first essential step for the establishment of an acute and/or latent infection.Enveloped viruses including HSV-1 penetrate host cells by inducing fusion between the virus envelope and the host cell membrane. HSV-1 entry is a stepwise process, which starts when HSV-1 envelope glycoproteins gB and gC attach to cell surface heparan sulfate proteoglycans (HSPGs) (Herold et al., 1991;Nicola et al., 2003;Trybala et al., 2000). This initial interaction enables HSV-1 glycoprotein D (gD) to bind to one of the known gD entry co-receptors. There are three classes of gD co-receptors that have been characterized: nectin-1 (HveC) and nectin-2 (HveB), which are both members of the immunoglobulin superfamily (Geraghty et al., 1998), herpesvirus entry mediator (HVEM) that belongs to the tumour necrosis factor receptor family (Montgomery et al., 1996), and 3-O-sulfated heparan sulfate (3-OS HS) which is a specifically modified form of heparan sulfate (HS) (Shukla et al., 1999b; O'Donnell et al., 2010). The binding of gD to one of its receptors leads to conformational changes in gD that allows it to activate a multiglycoprotein complex involving gB, gD, gH and gL that triggers the viral fusion with the host cell membrane (Atanasiu et al., 2007;Spear et al., 2000). This fusion mechanism is utilized...

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“…The effects of basic fibroblast growth factor-2 (FGF-2), which is known to modulate extracellular matrix (ECM) production of various cell types [19]. FGF-2 also plays role in inducing osteopontine expression, bone protein that important for bone remodeling so can prevent orthodontic relapsing [20].…”

Section: Discussionmentioning

confidence: 99%

FGF-2, MMP-8 and Integrin α2β1 Expression in Periodontal ligament Remodelling Tension Area with Nanopowder <i>Stichopus hermanii</i> Application to Prevent Orthodontic Relapsing

Prameswari¹

2017

IJMSA

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Basic fibroblast growth factor regulates expression of heparan sulfate in human periodontal ligament cells

Cited by 19 publications

References 46 publications

Analysis of a gain-of-function FGFR2 Crouzon mutation provides evidence of loss of function activity in the etiology of cleft palate

Analysis of a gain-of-function FGFR2 Crouzon mutation provides evidence of loss of function activity in the etiology of cleft palate

Syndecan-1 and syndecan-2 play key roles in herpes simplex virus type-1 infection

FGF-2, MMP-8 and Integrin α2β1 Expression in Periodontal ligament Remodelling Tension Area with Nanopowder <i>Stichopus hermanii</i> Application to Prevent Orthodontic Relapsing

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Basic fibroblast growth factor regulates expression of heparan sulfate in human periodontal ligament cells

Cited by 19 publications

References 46 publications

Analysis of a gain-of-function FGFR2 Crouzon mutation provides evidence of loss of function activity in the etiology of cleft palate

Analysis of a gain-of-function FGFR2 Crouzon mutation provides evidence of loss of function activity in the etiology of cleft palate

Syndecan-1 and syndecan-2 play key roles in herpes simplex virus type-1 infection

FGF-2, MMP-8 and Integrin α2β1 Expression in Periodontal ligament Remodelling Tension Area with Nanopowder &lt;i&gt;Stichopus hermanii&lt;/i&gt; Application to Prevent Orthodontic Relapsing

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FGF-2, MMP-8 and Integrin α2β1 Expression in Periodontal ligament Remodelling Tension Area with Nanopowder <i>Stichopus hermanii</i> Application to Prevent Orthodontic Relapsing