Role of MAP Kinases p42erk-2/p44erk-1 in Cementum-derived Attachment-protein-mediated Cell Attachment

Komaki, Motohiro; Kang, Ming-Hsi; Narayanan, A. Sampath

doi:10.1177/00220345000790101001

Cited by 8 publications

(7 citation statements)

References 33 publications

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“…Consistent with a previous report (Komaki et al, 2000), the spreading of gingival fibroblasts activated the MAPK cascade, resulting in increases in levels of phosphorylated p42 (Erk-2). Such changes in MAPK phosphorylation are likely to signal cell-cycle progression (Lavoie et al, 1996).…”

Section: Hip/l29 Modulation Of Bfgf Bioactivitysupporting

confidence: 92%

Heparan Sulfate Interacting Protein (HIP/L29) Negatively Regulates Growth Responses to Basic Fibroblast Growth Factor in Gingival Fibroblasts

Baraniak²,

Julian³

et al. 2002

J Dent Res

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Basic fibroblast growth factor (bFGF) modulates gingival growth, and its release from heparan sulfate (HS) in the extracellular matrix (ECM) governs local tissue bioavailability. We identified a heparin/HS interacting protein (HIP/L29) that recognizes specific HS sequences. We hypothesize that HIP/L29, by modulating the interactions of bFGF with HS chains on proteoglycans, could regulate bFGF bioavailability. To investigate interactions between bFGF and HIP/L29, we isolated and cultured fibroblasts from normal gingiva and overgrown gingiva from patients on cyclosporine (CSA). bFGF significantly stimulated gingival fibroblast proliferation with or without heparin. Recombinant human HIP/L29 dramatically decreased bFGF-induced proliferation, but did not alter responses to insulin-like growth factor-1 (IGF-1). Analysis of mitogen-activated protein kinase (MAPK) phosphorylation patterns showed that bFGF stimulation of p44 (Erk-1), but not p42 (Erk-2), also was inhibited by HIP/L29 in a dose-dependent manner. Together, these results support our hypothesis that HIP/L29 modulates the bioavailability and action of bFGF.

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Section: Hip/l29 Modulation Of Bfgf Bioactivitysupporting

confidence: 92%

Heparan Sulfate Interacting Protein (HIP/L29) Negatively Regulates Growth Responses to Basic Fibroblast Growth Factor in Gingival Fibroblasts

Baraniak²,

Julian³

et al. 2002

J Dent Res

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“…We have previously shown that attachment to CAP induces sustained activation of ERK‐2, which lasts for up to 12 h (10, 36) . ERK‐2 activation has been shown to be necessary for expression of AP‐1 proteins and cyclin D 1 expression (11, 12, 37–39) .…”

Section: Discussionmentioning

confidence: 99%

Role of D1 and E Cyclins in Cell Cycle Progression of Human Fibroblasts Adhering to Cementum Attachment Protein

Yokokoji

Narayanan

2001

Journal of Bone and Mineral Research

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Cementum attachment protein (CAP) is a collagenous protein present in the matrix of tooth cementum that mediates preferential attachment of some mesenchymal cell types, and CAP binding capacity is related to mineralizing tissue-forming capacity in culture. We have examined if adhesion to surfaces containing CAP as the only attachment protein permits human fibroblasts to escape G 1 arrest and synthesize DNA, and if adhesion to CAP modulates the levels of cyclins D 1 and E. Human gingival fibroblasts (HGFs) were serum-starved, trypsinized, and added to plates coated with CAP or bovine serum albumin (BSA). Cells were then exposed to either 10% fetal bovine serum (FBS) or to cementum-derived growth factor (CGF), an insulin-like growth factor I (IGF-I)-like molecule sequestered in tooth cementum, plus epidermal growth factor (EGF). DNA synthesis was measured as [ 3 H]thymidine uptake, and cyclin D 1 and E levels were determined by Western analysis. Cyclin E-dependent kinase (Cdk) activity was assessed in terms of H1 kinase activity in immunoprecipitates of cyclin E. Cells adhering to CAP synthesized DNA, whereas on BSA they remained unattached and did not synthesize DNA. Protein levels of cyclin D 1 were higher in cells adhering to CAP in the absence and presence of growth factors. Cyclin E levels were not affected by adhesion alone, but they increased in the presence of growth factors. Cyclin E-associated kinase activity was higher in cells adherent on CAP, and it increased further in the presence of growth factors. Our results indicate that adhesion to CAP increases cyclin D 1 levels and cyclin E-associated Cdk activity, and that these increases contribute to cell cycle progression. We previously observed that the signaling reactions induced during adhesion are characteristic of the CAP; together these observations indicate that specific matrix components present in the local environment can contribute to recruitment and differentiation of specific cell types for normal homeostasis and wound healing.

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“…Both the Erk and Akt pathways have been found to enhance cell survival, growth and proliferation (Khwaja & Downward 1997; Yujiri et al 1998; Erhardt et al 1999; Jasleen et al 2000; Wilkinson & Millar 2000). However, in human gingival fibroblasts adherent to cementum‐derived attachment protein, cell proliferation is not affected by PD98059, the Erk inhibitor (Komaki et al 2000). Gu et al (2002) showed that in adenocarcinoma, survival signals from LN‐10 are PI 3‐kinase/Akt mediated, but Erk signalling was operative in carcinoma cells adherent to fibronectin.…”

Section: Discussionmentioning

confidence: 99%

Laminin‐2 stimulates the proliferation of epithelial cells in a conjunctival epithelial cell line

2004

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Laminin-2 (LN-2, alpha2beta1gamma1) is a basement membrane-associated laminin isoform usually considered in the context of muscle and nerve tissues. To test the hypothesis that LN-2 can additionally modulate epithelial cell biology, an analysis of the role of LN-2 in cell adhesion, activation of signalling intermediates and proliferation was undertaken. A virally transformed human conjunctival epithelial cell line (HC0597) was utilized in this study. Adhesion assays using function-inhibiting antibodies demonstrated that alpha3beta1 integrin is essential for the rapid attachment of conjunctival epithelial cells to LN-2. Bromodeoxyuridine (BrdU) incorporation analyses revealed that, compared with LN-1 or LN-10, LN-2 significantly promotes epithelial proliferation. Phosphorylation of the signalling intermediates Erk1/2 and Akt-1 was observed within 15 min of cell adhesion to LN-2. Inhibiting alpha3beta1 integrin function decreased total cellular phosphotyrosine levels, specifically inhibited phosphorylation of Erk1/2 and Akt-1, and dampened the proliferation response of epithelial cells adherent to LN-2. Inhibition of Erk or Akt activation inhibited cell proliferation in a dose-dependent manner. However, the inhibition of Erk resulted in a stronger suppression of proliferation compared with Akt inhibition. From these results, it is concluded that human conjunctival epithelial cells adhere to immobilized LN-2 using alpha3beta1 integrin. alpha3beta1 integrin/LN-2 signalling, transduced primarily through an Erk pathway, enhances epithelial cell proliferation. These results demonstrate that LN-2 can impact on epithelial cell biology in addition to nerve and muscle, and provide information regarding the role of this isoform in ocular surface epithelial cells.

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Role of MAP Kinases p42erk-2/p44erk-1 in Cementum-derived Attachment-protein-mediated Cell Attachment

Cited by 8 publications

References 33 publications

Heparan Sulfate Interacting Protein (HIP/L29) Negatively Regulates Growth Responses to Basic Fibroblast Growth Factor in Gingival Fibroblasts

Heparan Sulfate Interacting Protein (HIP/L29) Negatively Regulates Growth Responses to Basic Fibroblast Growth Factor in Gingival Fibroblasts

Role of D1 and E Cyclins in Cell Cycle Progression of Human Fibroblasts Adhering to Cementum Attachment Protein

Laminin‐2 stimulates the proliferation of epithelial cells in a conjunctival epithelial cell line

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