Integrin‐mediated signaling regulates AP‐1 transcription factors and proliferation in osteoblasts

Cowles, Elizabeth A.; Brailey, Lisa L.; Gronowicz, Gloria

doi:10.1002/1097-4636(20001215)52:4<725::aid-jbm18>3.3.co;2-f

Cited by 37 publications

(51 citation statements)

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“…c-Fos expression negatively correlates with increased neuronal cell death in the hippocampus during kainic acid-induced seizure, indicating an anti-apoptotic role for the protein in this scenario (60). Osteoblast binding to extracellular matrix proteins such as FN through integrins induces c-Fos and c-Jun expression via protein kinase C and phosphotyrosine kinase signaling pathways (61). FN is required for vascular endothelial growth factor-induced c-Fos induction, mitogenic response, and cell migration in T47D breast cancer cells (62).…”

Section: Discussionmentioning

confidence: 99%

Fibronectin Increases Matrix Metalloproteinase 9 Expression through Activation of c-Fos via Extracellular-regulated Kinase and Phosphatidylinositol 3-Kinase Pathways in Human Lung Carcinoma Cells

Han

Ritzenthaler

Sitaraman

et al. 2006

Journal of Biological Chemistry

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Matrix metalloproteinases (MMPs) 2 are a family of zinc enzymes responsible for degradation of extracellular matrix components including basement membrane collagen, interstitial collagens, fibronectin (FN), and various proteoglycans during normal remodeling and repair processes (1, 2). The potent proteolytic activities of MMPs are mainly regulated by the concomitant expression of specific tissue inhibitors of matrix metalloproteinases (3). Excessive or inappropriate expression of MMPs may contribute to the pathogenesis of tissue destructive processes in a wide variety of diseases including lung disorders like bronchial asthma, chronic obstructive pulmonary disease, acute lung injury, pulmonary hypertension, and interstitial lung diseases (2, 4). In addition, MMPs have been implicated in the progression and metastases of different tumors including lung cancer (see later in text).One member of the MMP family is the 92-kDa type IV collagenase MMP-9. The MMP-9 gene is encoded on chromosome 20 and its expression is under the control of a 2.2-kb upstream regulatory sequence harboring binding sites for AP-1, NF-B, Sp1, and others (5). MMP-9 expression is increased in malignant cancers when compared with benign tumors and non-invasive ones, and there is compelling in vitro and in vivo evidence for a role of MMP-9 in tumor invasion and angiogenesis (6, 7). Its dramatic overexpression in cancer and various inflammatory conditions suggest that this protease is a potential target for the development of novel therapeutic interventions (8).Because of its perceived importance, our research focuses on the factors that increase MMP-9 expression in the lung. Our search led us to FN, a matrix glycoprotein highly expressed in tobacco-related lung disease that has been shown to stimulate lung carcinoma cell growth through several mechanisms (9 -11). Cell adhesion to FN results in MMP secretion in normal and tumor cell systems (12)(13)(14). These studies suggest that tumor cell interactions with FN might lead to MMP-9 expression thereby promoting cancer cell migration, invasion, and related processes. However, the mechanisms by which FN stim-* This work was supported by American Lung Association Bioresearch Grant RG-10215N (to S. W. H.) and by a Merit Review Grant from the Department of Veterans Affairs (to J. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C.

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Section: Discussionmentioning

confidence: 99%

Fibronectin Increases Matrix Metalloproteinase 9 Expression through Activation of c-Fos via Extracellular-regulated Kinase and Phosphatidylinositol 3-Kinase Pathways in Human Lung Carcinoma Cells

Han

Ritzenthaler

Sitaraman

et al. 2006

Journal of Biological Chemistry

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“…Integrin-mediated binding of extracellular matrix components regulates AP-1 activity in many cell types, including osteoblasts (47,48). A key role for AP-1 family members in osteoblast function (49,50) and osteoblast-specific gene expression (51-53) has been described.…”

Section: ␣-Nac Interacts With Ilk In Mammalian Cells-mentioning

confidence: 99%

Integrin-linked Kinase Regulates the Nuclear Entry of the c-Jun Coactivator α-NAC and Its Coactivation Potency

Quélo

Gauthier

Hannigan

et al. 2004

Journal of Biological Chemistry

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“…As a result, the crosslinking induced a significant structure development from nanoscale range to microscale range. The GA and ChS play important roles in controlling the function of osteoblast [29,30]. Some authors described on the possibility to obtain collagen/HA and collagen/ wollastonite scaffolds via a freeze-drying technique.…”

Section: Introductionmentioning

confidence: 99%

Organic/Inorganic bioactive materials Part II: in vitro bioactivity of Collagen-Calcium Phosphate Silicate/Wollastonite hybrids

et al. 2009

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Abstract:In the present study, novel hybrid materials of Collagen (C) and Calcium Phosphate Silicate/Wollastonite (CPS/W) were synthesized.The CPS/W ceramic was prepared via polystep sol-gel method. The dissolution test of CPS/W ceramic was filled with TRIS-HCl buffer. FTIR depicts that hydroxyl carbonate apatite (OHCO 3 HA) was observed after 3 days of immersion in TRIS-HCl buffer. Biohybrids of C-CPS/W were produced from diluted hydrochloric acid collagen type I and ceramic powder with different ratios of C and CPS/W equal to 25:75 and 75:25 wt.%. The synthesized hybrids were characterized by FTIR, XRD and SEM. FTIR depicts a "red shift" if amide I could be attributed to the fact that the collagen prefers to chelate Ca 2+ from partial dissolution of CPS/W ceramic. The growth of B-type carbonate containing hydroxyapatite (B-CO 3 HA) on the C-CPS/W hybrids soaked in 1.5SBF was observed. The negatively charged carboxylate groups from the collagen may be responsible for hydroxyapatite (HA) deposition. This fact was confirmed by the "red shift" of carboxylate groups of collagen in FTIR spectra. The formation of HA was observed by FTIR, XRD and SEM.© Versita Warsaw and Springer-Verlag Berlin Heidelberg.

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Integrin‐mediated signaling regulates AP‐1 transcription factors and proliferation in osteoblasts

Cited by 37 publications

References 0 publications

Fibronectin Increases Matrix Metalloproteinase 9 Expression through Activation of c-Fos via Extracellular-regulated Kinase and Phosphatidylinositol 3-Kinase Pathways in Human Lung Carcinoma Cells

Fibronectin Increases Matrix Metalloproteinase 9 Expression through Activation of c-Fos via Extracellular-regulated Kinase and Phosphatidylinositol 3-Kinase Pathways in Human Lung Carcinoma Cells

Integrin-linked Kinase Regulates the Nuclear Entry of the c-Jun Coactivator α-NAC and Its Coactivation Potency

Organic/Inorganic bioactive materials Part II: in vitro bioactivity of Collagen-Calcium Phosphate Silicate/Wollastonite hybrids

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