dc.creator | Cavagis A.D.M. | |
dc.creator | Takamori E.R. | |
dc.creator | Granjeiro J.M. | |
dc.creator | Oliveira R.C. | |
dc.creator | Ferreira C.V. | |
dc.creator | Peppelenbosch M.P. | |
dc.creator | Zambuzzi W.F. | |
dc.date | 2014 | |
dc.date | 2015-06-25T17:56:49Z | |
dc.date | 2015-11-26T14:47:09Z | |
dc.date | 2015-06-25T17:56:49Z | |
dc.date | 2015-11-26T14:47:09Z | |
dc.date.accessioned | 2018-03-28T21:57:21Z | |
dc.date.available | 2018-03-28T21:57:21Z | |
dc.identifier | | |
dc.identifier | Oral Diseases. Blackwell Publishing Ltd, v. 20, n. 8, p. 780 - 786, 2014. | |
dc.identifier | 1354523X | |
dc.identifier | 10.1111/odi.12202 | |
dc.identifier | http://www.scopus.com/inward/record.url?eid=2-s2.0-84911990471&partnerID=40&md5=c3c967b0ddefc3886a74d623293b612c | |
dc.identifier | http://www.repositorio.unicamp.br/handle/REPOSIP/87123 | |
dc.identifier | http://repositorio.unicamp.br/jspui/handle/REPOSIP/87123 | |
dc.identifier | 2-s2.0-84911990471 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1253150 | |
dc.description | Objective: Our poor understanding of how inflammatory mediators can affect osteoblast behavior led us to investigate the tumor necrosis factor (TNF)α-induced focal adhesion kinase (FAK) and Src phosphorylation. Material and Methods: MC3T3-E1 pre-osteoblast cells were harvested at specific time points after either TNFα treatment or RAW267 stimulated conditioned medium, and thereafter cell extracts were prepared for Immunoblotting assay. ELISA detected TNFα content at conditioned medium. Tumor necrosis factor-α-neutralizing antibodies also were used. Results: It was possible to show that TNFα provokes attenuation at Y-phosphorylation of both FAK (at Y397) and Src (at Y416) proteins (P < 0.05), suggesting a decrease in their activities. The very similar profile was observed when osteoblasts were incubated with conditioned medium from lipopolysaccharide (LPS)-stimulated macrophages, it being significantly different than control (FAK and Src, P < 0.05). Nevertheless, in order to validate these findings, we decided to pre-incubate osteoblasts with anti-TNFα neutralizing antibody (2 μg ml-1) prior exposing to conditioned medium. Importantly, our results revealed that there was a diminution on those conditioned medium effects when the same biological parameters were evaluated (P < 0.05). Moreover, we also showed that TNFα impairs osteoblast adhesion, suggesting an interesting role on osteoblast performance. Conclusions: Altogether, these results suggest that LPS-stimulated macrophage mediators attenuate both FAK and Src activations in osteoblast, suggesting a novel role for TNFα on osteoblast performance. | |
dc.description | 20 | |
dc.description | 8 | |
dc.description | 780 | |
dc.description | 786 | |
dc.description | Alikhani, M., Alikhani, Z., Graves, D.T., Apoptotic effects of LPS on fibroblasts are indirectly mediated through TNFR1 (2004) J Dent Res, 83, pp. 671-676 | |
dc.description | Amber, I.J., Hibbs, J.B., Jr., Taintor, R.R., Vavrin, Z., The L-arginine dependent effector mechanism is induced in murine adenocarcinoma cells by culture supernatant from cytotoxic activated macrophages (1988) J Leukoc Biol, 43, pp. 187-192 | |
dc.description | Amber, I.J., Hibbs, J.B., Jr., Parker, C.J., Johnson, B.B., Taintor, R.R., Vavrin, Z., Activated macrophage conditioned medium: identification of the soluble factors inducing cytotoxicity and the L-arginine dependent effector mechanism (1991) J Leukoc Biol, 49, pp. 610-620 | |
dc.description | Brown, M.C., Perrotta, J.A., Turner, C.E., Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding (1996) J Cell Biol, 135, pp. 1109-1123 | |
dc.description | Chan, P.Y., Kanner, S.B., Whitney, G., Aruffo, A., A transmembrane-anchored chimeric focal adhesion kinase is constitutively activated and phosphorylated at tyrosine residues identical to pp125FAK (1994) J Biol Chem, 269, pp. 20567-20574 | |
dc.description | Corotti, M.V., Zambuzzi, W.F., Paiva, K.B., Immunolocalization of matrix metalloproteinases-2 and -9 during apical periodontitis development (2009) Arch Oral Biol, 54, pp. 764-771 | |
dc.description | Dong, J., Cui, X., Jiang, Z., Sun, J., MicroRNA-23a modulates tumor necrosis factor-alpha-induced osteoblasts apoptosis by directly targeting Fas (2013) J Cell Biochem, 114, pp. 2738-2745 | |
dc.description | Garlet, G.P., Destructive and protective roles of cytokines in periodontitis: a re-appraisal from host defense and tissue destruction viewpoints (2010) J Dent Res, 89, pp. 1349-1363 | |
dc.description | Gilbert, L., He, X., Farmer, P., Inhibition of osteoblast differentiation by tumor necrosis factor-alpha (2000) Endocrinology, 141, pp. 3956-3964 | |
dc.description | Gilbert, L., He, X., Farmer, P., Expression of the osteoblast differentiation factor RUNX2 (Cbfa1/AML3/Pebp2alpha A) is inhibited by tumor necrosis factor-alpha (2002) J Biol Chem, 277, pp. 2695-2701 | |
dc.description | Gilbert, L.C., Chen, H., Lu, X., Nanes, M.S., Chronic low dose tumor necrosis factor-α (TNF) suppresses early bone accrual in young mice by inhibiting osteoblasts without affecting osteoclasts (2013) Bone, 56, pp. 174-183 | |
dc.description | Hartree, E.F., Determination of proteins: a modification of Lowry method that gives a linear photometric response (1972) Anal Biochem, 48, pp. 422-427 | |
dc.description | Kitajima, I., Soejima, Y., Takasaki, I., Beppu, H., Tokioka, T., Maruyama, I., Ceramide-induced nuclear translocation of NF-kappa B is a potential mediator of the apoptotic response to TNF-alpha in murine clonal osteoblasts (1996) Bone, 19, pp. 263-270 | |
dc.description | Klemke, R.L., Cai, S., Giannini, A.L., Gallagher, P.J., de Lanerolle, P., Cheresh, D.A., Regulation of cell motility by mitogen-activated protein kinase (1997) J Cell Biol, 37, pp. 481-492 | |
dc.description | Loomer, P.M., Sigusch, B., Sukhu, B., Ellen, R.P., Tenenbaum, H.C., Direct effects of metabolic products and sonicated extracts of Porphyromonas gingivalis 2561 on osteogenesis in vitro (1994) Infect Immun, 62, pp. 1289-1297 | |
dc.description | Loomer, P.M., Ellen, R.P., Tenenbaum, H.C., Characterization of inhibitory effects of suspected periodontopathogens on osteogenesis in vitro (1995) Infect Immun, 63, pp. 3287-3296 | |
dc.description | Menezes, R., Bramante, C.M., da Silva Paiva, K.B., Receptor activator NFkappaB-ligand and osteoprotegerin protein expression in human periapical cysts and granulomas (2006) Oral Surg Oral Med Oral Pathol Oral Radiol Endod, 102, pp. 404-409 | |
dc.description | Milani, R., Ferreira, C.V., Granjeiro, J.M., Phosphoproteome reveals an atlas of protein signaling networks during osteoblast adhesion (2010) J Cell Biochem, 109, pp. 957-966 | |
dc.description | Mon, N.N., Kokuryo, T., Hamaguchi, M., Inflammation and tumor progression: a lesson from TNF-alpha-dependent FAK signaling in cholangiocarcinoma (2009) Methods Mol Biol, 512, pp. 279-293 | |
dc.description | Schlaepfer, D.D., Jones, K.C., Hunter, T., Multiple Grb2-mediated integrin-stimulated signaling pathways to ERK2/mitogen-activated protein kinase: summation of both c-Src- and focal adhesion kinase initiated tyrosine phosphorylation events (1998) Mol Cell Biol, 18, pp. 2571-2585 | |
dc.description | Schwartz, M.A., Integrin signaling revisited (2011) Trends Cell Biol, 11, pp. 466-470 | |
dc.description | Sherry, B., Yarlett, N., Strupp, A., Cerami, A., Identification of cyclophilin as a proinflammatory secretory product of lipopolysaccharide-activated macrophages (1992) Proc Natl Acad Sci USA, 89, pp. 3511-3515 | |
dc.description | Smilenov, L.B., Mikhailov, A., Pelham, R.J., Marcantonio, E.E., Gundersen, G.G., Focal adhesion motility revealed in stationary fibroblasts (1999) Science, 286, pp. 1172-1174 | |
dc.description | de Souza Queiroz, K.C., Zambuzzi, W.F., Santos de Souza, A.C., A possible anti-proliferative and anti-metastatic effect of irradiated riboflavin in solid tumours (2007) Cancer Lett, 258, pp. 126-134 | |
dc.description | Thammasitboon, K., Goldring, S.R., Boch, J.A., Role of macrophages in LPS-induced osteoblast and PDL cell apoptosis (2006) Bone, 38, pp. 845-852 | |
dc.description | Zambuzzi, W.F., Bruni-Cardoso, A., Granjeiro, J.M., On the road to understanding of the osteoblast adhesion: cytoskeleton organization is rearranged by distinct signaling pathways (2009) J Cell Biochem, 108, pp. 134-144 | |
dc.description | Zambuzzi, W.F., Granjeiro, J.M., Parikh, K., Yuvaraj, S., Peppelenbosch, M.P., Ferreira, C.V., Modulation of Src activity by low molecular weight protein tyrosine phosphatase during osteoblast differentiation (2008) Cell Physiol Biochem, 22, pp. 497-506 | |
dc.description | Zambuzzi, W.F., Milani, R., Teti, A., Expanding the role of Src and protein-tyrosine phosphatases balance in modulating osteoblast metabolism: lessons from mice (2010) Biochimie, 92, pp. 327-332 | |
dc.language | en | |
dc.publisher | Blackwell Publishing Ltd | |
dc.relation | Oral Diseases | |
dc.rights | fechado | |
dc.source | Scopus | |
dc.title | Tnfα Contributes For Attenuating Both Y397fak And Y416src Phosphorylations In Osteoblasts | |
dc.type | Artículos de revistas | |