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• _8 value "Furthermore, we noted that collagen-stimulated DDR1 interacted with the p85 subunit of PI3K (Fig. 7b), and we also observed that adherence of HB2 cells to collagen caused tyrosine phosphorylation of the p85 of PI3K (Fig. 7c), a phenomenon associated with activation of this enzyme. Neither of these events was observed in cells pretreated with pertussis toxin (Fig. 7a,b,c)." provenance.
• _5 value "Furthermore, we noted that collagen-stimulated DDR1 interacted with the p85 subunit of PI3K (Fig. 7b), and we also observed that adherence of HB2 cells to collagen caused tyrosine phosphorylation of the p85 of PI3K (Fig. 7c), a phenomenon associated with activation of this enzyme. Neither of these events was observed in cells pretreated with pertussis toxin (Fig. 7a,b,c)." provenance.
• _6 value "Tumor necrosis factor α (TNFα) strongly increased the expression of E-selectin in human umbilical vein endothelial cells (HUVEC). This effect was independent of the activation of SAPK2/p38 induced by TNFα." provenance.
• _4 value "Adhesion of HT-29 cells on a monolayer of HUVEC pretreated with TNFα was dependent on E-selectin expression but was independent of SAPK2/p38 activity of both HUVEC and tumor cells. The adhesion of HT-29 cells to E-selectin-expressing HUVEC led to the activation of SAPK2/p38 in the tumor cells as reflected by the increased phosphorylation of the actin-polymerizing factor HSP27 by mitogen-activated protein kinase 2/3, a direct target of SAPK2/p38. Moreover, a recombinant E-selectin/Fc chimera quickly increased the activation of SAPK2/p38 in HT-29 cells. Blocking the increased activity of SAPK2/p38 of HT-29 cells by SB203580 or by expressing a dominant negative form of SAPK2/p38 inhibited their transendothelial migration." provenance.
• _5 value "inhibiting the TNFα-induced increase in SAPK2/p38 activity by SB203580 did not impair the expression of E-selectin, which suggested that activation of SAPK2/p38 was not required for the expression of this adhesion molecule (Fig. 1,G and H). Accordingly, blocking the SAPK2/p38 activity of HUVEC with SB203580 did not inhibit the adhesion of HT-29 cells to HUVEC (Fig. 2A)." provenance.
• _3 value "inhibiting the TNFα-induced increase in SAPK2/p38 activity by SB203580 did not impair the expression of E-selectin, which suggested that activation of SAPK2/p38 was not required for the expression of this adhesion molecule (Fig. 1,G and H). Accordingly, blocking the SAPK2/p38 activity of HUVEC with SB203580 did not inhibit the adhesion of HT-29 cells to HUVEC (Fig. 2A)." provenance.
• _5 value "Impairing E-selectin-mediated activation of SAPK2p38 and HSP27 phosphorylation of HT-29 cells with SB203580 (Fig. 4A and data not shown) or by expressing a dominant negative form of SAPK2/p38 inhibited their migration across activated HUVEC (Fig.4B)." provenance.
• _3 value "Impairing E-selectin-mediated activation of SAPK2p38 and HSP27 phosphorylation of HT-29 cells with SB203580 (Fig. 4A and data not shown) or by expressing a dominant negative form of SAPK2/p38 inhibited their migration across activated HUVEC (Fig.4B)." provenance.
• _5 value "Incubation of medium conditioned by human smooth muscle cells that contained pro-MMP-2, with plasma membrane extracts prepared from EC treated with TNF-α, interleukin-1β, or OxLDL, increased the proteolytic conversion of 72-kDa proMMP-2 to new gelatinolytic bands of 70- and 68-kDa corresponding to the processed active MMP-2 (Fig. 7A). Proteolytic processing of pro-MMP-2 was reduced in membrane extracts incubated with anti-MT1-MMP antibody (Fig. 7A and B)." provenance.
• _5 value "Northern analyses and RNase protection assays revealed that exposure of cultured EC to TNF-α, interleukin-1β, or Ox-LDL results in the accumulation of MT1- MMP mRNA" provenance.
• _5 value "Interestingly, TSC exposure decreased H4K16Ac and increased H3K27me3 levels within the Dkk-1 promoter region in both lung cancer lines." provenance.
• _5 value "Knockdown of SirT1 also seemed to somewhat increase Dkk-1 expression in untreated Calu-6cells and partially abrogate TSC-mediated repression of Dkk-1 (Fig. 4C)." provenance.
• _4 value "Western blot analysis (Fig. 5B) revealed that TSC-mediated repression of Dkk-1 coincided with dose-dependent phosphorylation of LDL receptor related protein 6(LRP-6) and dishevelled-2 (Dvl-2) indicative of activation of Wnt receptor complex, as well as JNK, a downstream effector of noncanonical Wnt signaling." provenance.
• _5 value "Western blot analysis (Fig. 5B) revealed that TSC-mediated repression of Dkk-1 coincided with dose-dependent phosphorylation of LDL receptor related protein 6(LRP-6) and dishevelled-2 (Dvl-2) indicative of activation of Wnt receptor complex, as well as JNK, a downstream effector of noncanonical Wnt signaling." provenance.
• _6 value "shRNA-mediated knockdown of Dkk-1 enhanced phosphorylation of JNK in Calu-6cells (Fig. 5C), suggesting that activation of JNK in these cells following TSC exposure was due, at least in part, to activation of Wnt signaling, rather than nonspecific responses to genotoxic stress." provenance.
• _5 value "Wnt5a (which encodes a ligand implicated in noncanonical Wnt signaling; ref. 32) was markedly induced in TSC-treated Calu-6cells as well as Calu-6cells transfected with shRNA targeting Dkk-1." provenance.
• _2 value "Excess amounts of reactive oxygen species (ROS) such as O2.- and H2O2 have deleterious effects on cells and contribute to various cardiovascular diseases including hypertension, heart failure, atherosclerosis, and diabetes (41), while physiological concentrations of ROS are involved in signaling to mediate cell migration, growth, and differentiation (32)." provenance.
• _5 value "Nox2 is a critical component of endothelial NADPH oxidase (38), and its expression and Nox2-dependent ROS production are increased by oxidized LDL, endothelin-1, angiotensin II, VEGF, and angiopoietin-2 in ECs (99). Nox1 is involved in shear stressinduced ROS production which is required for monocyte adhesion (93) and stimulates branching morphogenesis in sinusoidal ECs (55). Nox4 is most abundantly expressed in ECs, and involved in basal- (2) and Ang II-induced (109) O2- production. Moreover, p47phox is involved in cytokine, growth factor, or shear stress-stimulated ROS production in ECs (48, 67, 107)." provenance.
• _4 value "Nox2 is a critical component of endothelial NADPH oxidase (38), and its expression and Nox2-dependent ROS production are increased by oxidized LDL, endothelin-1, angiotensin II, VEGF, and angiopoietin-2 in ECs (99). Nox1 is involved in shear stressinduced ROS production which is required for monocyte adhesion (93) and stimulates branching morphogenesis in sinusoidal ECs (55). Nox4 is most abundantly expressed in ECs, and involved in basal- (2) and Ang II-induced (109) O2- production. Moreover, p47phox is involved in cytokine, growth factor, or shear stress-stimulated ROS production in ECs (48, 67, 107)." provenance.
• _5 value "Nox2 is a critical component of endothelial NADPH oxidase (38), and its expression and Nox2-dependent ROS production are increased by oxidized LDL, endothelin-1, angiotensin II, VEGF, and angiopoietin-2 in ECs (99). Nox1 is involved in shear stressinduced ROS production which is required for monocyte adhesion (93) and stimulates branching morphogenesis in sinusoidal ECs (55). Nox4 is most abundantly expressed in ECs, and involved in basal- (2) and Ang II-induced (109) O2- production. Moreover, p47phox is involved in cytokine, growth factor, or shear stress-stimulated ROS production in ECs (48, 67, 107)." provenance.
• _4 value "After agonist stimulation or during active EC migration, p47phox translocates to the membrane ruffles through association with WAVE1 and Rac1/PAK1 (107), as well as to the focal complexes in lamellar protrusions through binding to adaptor TRAF4 and Hic-5, a focal contact scaffold (108)." provenance.
• _2 value "Exogenous H2O2 stimulates induction of HIF1α and VEGF by various cell types including ECs, and promote cell proliferation and migration, cytoskeletal reorganization, and tube formation in ECs (99)." provenance.
• _5 value "The mitogenic and chemotactic effects of VEGF in ECs are mediated mainly through VEGFR2 (76). VEGFR2 is activated through ligandstimulated receptor dimerization and transphosphorylation (autophosphorylation) of tyrosine residues in the cytoplasmic kinase domain. At present, tyrosine residues 951 and 996 in the kinase insert domain, and 1054 and 1059 in the kinase catalytic domain, have been identified as autophosphorylation sites for VEGFR2 in a bacterial expression system (30). This event is followed by activation of downstream signaling pathways such as Src, PI3 kinase, MAP kinases, and Akt, which is essential for VEGF-induced actin reorganization, cell migration, and proliferation of ECs." provenance.
• _5 value "The mitogenic and chemotactic effects of VEGF in ECs are mediated mainly through VEGFR2 (76). VEGFR2 is activated through ligandstimulated receptor dimerization and transphosphorylation (autophosphorylation) of tyrosine residues in the cytoplasmic kinase domain. At present, tyrosine residues 951 and 996 in the kinase insert domain, and 1054 and 1059 in the kinase catalytic domain, have been identified as autophosphorylation sites for VEGFR2 in a bacterial expression system (30). This event is followed by activation of downstream signaling pathways such as Src, PI3 kinase, MAP kinases, and Akt, which is essential for VEGF-induced actin reorganization, cell migration, and proliferation of ECs." provenance.
• _5 value "The mitogenic and chemotactic effects of VEGF in ECs are mediated mainly through VEGFR2 (76). VEGFR2 is activated through ligandstimulated receptor dimerization and transphosphorylation (autophosphorylation) of tyrosine residues in the cytoplasmic kinase domain. At present, tyrosine residues 951 and 996 in the kinase insert domain, and 1054 and 1059 in the kinase catalytic domain, have been identified as autophosphorylation sites for VEGFR2 in a bacterial expression system (30). This event is followed by activation of downstream signaling pathways such as Src, PI3 kinase, MAP kinases, and Akt, which is essential for VEGF-induced actin reorganization, cell migration, and proliferation of ECs." provenance.
• _8 value "TNF-α inhibits VEGF signaling by recruiting SHP-2 to the VEGFR2 in ECs (42)." provenance.
• _4 value "Cav1 is tyrosine phosphorylated by ROS (14, 17)and by various growth factors(54, 70), including VEGF(61). We have demonstrated that VEGF promotes the release of VEGFR2 from caveolae/lipid rafts, which is contemporaneous with the tyrosine phosphorylation of Cav1(Tyr14) and VEGFR2 and their colocalization at focal complexes, appearing as small-dot like structures at the edge of lamellipodia (Figs. 1 and 2)(52)." provenance.
• _6 value "Phospho-caveolin interacts with Grb7 (63), low molecular weight protein tyrosine phosphatase (16), and Csk, a negative regulator for Src (13)." provenance.
• _6 value "In ECs, VEGF stimulates ARF6 association with Rac1, which is cotemporaneous with Rac1 activation. The dominant negative ARF6 (T27N),inhibits VEGF-stimulated GTP-loading of Rac1, ROS production, and VEGFR2 autophosphorylation. These results suggest that ARF6 is an upstream mediator for Rac1, which may contribute to ROS production that mediates VEGFR2 autophosphorylation in ECs (Fig. 1)." provenance.
• _3 value "Tyrosine phosphorylation of VE-cadherin is required for reducing cell–cell adhesions and is mediated through cSrc which is dependent on ROS (69,103)." provenance.
• _7 value "At the leading edge of cells, Rac1 also links the adenomatous polyposis coli (APC) protein to actin filaments through binding to IQGAP1, thereby regulating polarization and directional migration by forming a complex with APC and CLIP-170. Of note, Nox2 also binds to and colocalizes with IQGAP1 at the leading edge in actively migrating ECs (Fig. 2)(50)." provenance.
• _3 value "The model was appropriate for testing the effects of desaturase inhibition because, after subplantar injection of carrageenan, an acute and localized inflammatory response occurs in the footpad, characterized by increased edema and neutrophil infiltration. Inhibition of edema was obtained with aspirin and indomethacin and was comparable to that obtained in the rat model." provenance.
• _3 value "D. Dietary AA restored edema and MPO activity." provenance.
• _6 value "Phosphorylation of cytoplasmic FOXO at specific sites by JNK initiates translocation into the nucleus" provenance.
• _6 value "Akt-dependent phosphorylation reduces the DNA-binding activity of FOXO, interferes with binding to the co-activators p300/CBP, and inactivates the FOXO nuclear translocation signal" provenance.
• _6 value "Akt-dependent phosphorylation reduces the DNA-binding activity of FOXO, interferes with binding to the co-activators p300/CBP, and inactivates the FOXO nuclear translocation signal" provenance.
• _7 value "The Akt-phosphorylated FOXO is exported from the nucleus in a CRM1- and 14-3-3-dependent process" provenance.
• _10 value "The Akt-phosphorylated FOXO is exported from the nucleus in a CRM1- and 14-3-3-dependent process" provenance.
• _10 value "Akt-phosphorylated FOXO interacts with the ubiquitin ligase Skp2 and is targeted for proteasomal degradation." provenance.
• _6 value "FOXO proteins intervene in the cell cycle by activating the cyclin-dependent kinase (CDK) inhibitors p27kip1 and p21cip1." provenance.
• _6 value "They also repress transcription of cyclin D1 and D2, which results in an attenuation of CDK4 activity and reduced phosphorylation of Rb protein, and hence increased binding activity of E2F family members to Rb." provenance.
• _8 value "Phosphorylation of the N-terminal Akt motif disrupts the interaction of this domain with the transcriptional co-activators p300/CBP and facilitates binding of FOXO to a 14-3-3 protein instead" provenance.
• _5 value "Oxidative stress, for instance a low concentration of hydrogen peroxide (H2O2),leads to an activation of the small GTPase Ral, which in turn is instrumental in the phosphorylation and activation of the Jun N-terminal kinase JNK." provenance.
• _7 value "JNK-induced phosphorylation initiates nuclear import of FOXO proteins and activation of their transcriptional regulatory potential." provenance.
• _6 value "Nuclear import triggered by oxidative stress results in association of FOXO proteins with proteins that have histone acetylase activity, such as p300/CBP and p300/CBP-associated factor (PCAF)." provenance.
• _6 value "Acetylated and JNK-phosphorylated nuclear FOXO then recruits SIRT1, a constitutively nuclear, nicotinamide adenine dinucleotide-dependent protein deacetylase. This recruitment, like the nuclear import, is dependent on oxidative stress signals." provenance.
• _6 value "Down-regulation of ErbB-3 by means of short hairpin RNA leads to decreased phospho-Akt levels in the gefitinib-sensitive NSCLC cell lines, Calu-3 (WT EGFR) and H3255 (L858R EGFR), but has no effect on Akt activation in the gefitinib-resistant cell lines, A549 and H522." provenance.
• _4 value "Vascular endothelial growth factor (VEGF) stimulates angiogenesis by activating VEGF receptor-2 (VEGFR-2)." provenance.
• _5 value "VEGF-B is another ligand of VEGFR-1 (ref. 18), but loss of VEGF-B (Vegfb–/–) does not affect vascular development19." provenance.
• _5 value "In pathological conditions, PlGF is upregulated and stimulates angiogenesis via displacement of VEGF from VEGF-R1 to VEGFR2 and via activation of VEGFR-1, of which a larger fraction is membraneassociated." provenance.
• _6 value "Finally, we observed that co-expression of LRIG1 suppresses EGF-stimulated transformation of NIH3T3 fibroblasts and that the inducible expression of LRIG1 in PC3 prostate tumor cells suppresses EGF- and neuregulin-1-stimulated cell cycle progression." provenance.
• _6 value "Stimulation with EGF or NRG1β resulted in a dramatic shift of cells into S-phase in the absence of LRIG1 expression. However, the presence of LRIG1 markedly suppressed these effects." provenance.
• _6 value "Interestingly, other LRR domain-containing proteins have also been demonstrated to interact with receptor tyrosine kinases. Decorin, a secreted proteoglycan containing nine LRRs, has been shown to interact with the EGF receptor and ErbB2 to initially enhance their activities (27, 28). Decorin interaction with receptors has been suggested to mediate prolonged receptor down-regulation and the inhibition of cellular growth through enhanced expression of p21waf1 (29)." provenance.
• _4 value "Insulin-like growth factor-I (IGF-I) has been shown to stimulate a hypertrophy response in skeletal muscles in vivo. In vitro studies have delineated two primary intracellular pathways that appear to mediate the effects of IGF-I in skeletal muscle: the Ras-ERK pathway and the phosphoinositide-3 kinase pathway." provenance.
• _5 value "Insulin-like growth factor-I (IGF-I) has been shown to stimulate a hypertrophy response in skeletal muscles in vivo. In vitro studies have delineated two primary intracellular pathways that appear to mediate the effects of IGF-I in skeletal muscle: the Ras-ERK pathway and the phosphoinositide-3 kinase pathway." provenance.
• _6 value "Introduction of MLK3 into cells alone activates the JNK signaling pathway, as assessed by Western blot analysis of phospho-c-Jun levels (Fig. 6A)." provenance.
• _6 value "Moreover, we show that a positive feedback loop exists between PGC-1α and members of the myocyte enhancer factor 2 (MEF2) family of transcription factors. MEF2s bind to the PGC-1α promoter and activate it, predominantly when coactivated by PGC-1α. MEF2 activity is stimulated further by CnA signaling." provenance.
• _7 value "Moreover, we show that a positive feedback loop exists between PGC-1α and members of the myocyte enhancer factor 2 (MEF2) family of transcription factors. MEF2s bind to the PGC-1α promoter and activate it, predominantly when coactivated by PGC-1α. MEF2 activity is stimulated further by CnA signaling." provenance.
• _6 value "Moreover, we show that a positive feedback loop exists between PGC-1α and members of the myocyte enhancer factor 2 (MEF2) family of transcription factors. MEF2s bind to the PGC-1α promoter and activate it, predominantly when coactivated by PGC-1α. MEF2 activity is stimulated further by CnA signaling." provenance.
• _4 value "As shown in Fig. 1C, mutagenesis of the CRE site abolished induction of the mouse PGC-1α promoter by forskolin, as expected." provenance.
• _6 value "As shown in Fig. 2A, a coactivation by PGC-1α of both MEF2C and MEF2D, but not NFAT, was observed on the PGC-1α promoter. These data suggest that PGC-1α might participate in the activation of its own promoter and that the MEF2 proteins may function both in the regulation of PGC-1α expression and as downstream targets of PGC-1α coactivation of other muscle-selective genes." provenance.
• _8 value "As shown in Fig. 2B, CnA is able to substantially increase the activity of MEF2C and MEF2D on the PGC-1α promoter. The strongest effect was observed when MEF2C or MEF2D was expressed with both CnA and PGC-1α (Fig. 2B)." provenance.
• _6 value "We next examined whether mutations of this MEF2 site affects MEF2 activity on the PGC-1α promoter. The mutated 2-kb promoter (called ΔMEF2; see Fig. 3A) is no longer able to mediate MEF2C or MEF2D induction alone, when activated by CnA or coactivated by PGC-1α, suggesting that this site is responsible for the MEF2 action (Fig. 3B). Moreover, electrophoretic mobility-shift assays revealed binding of MEF2C to this MEF-binding site but not the mutated ΔMEF site in the PGC-1α promoter (Fig. 3C). The identity of the MEF2C–DNA complex was confirmed by using an anti-MEF2 antibody that leads to a supershift of the DNA–protein complex." provenance.
• _6 value "To confirm that the coactivation of MEF2C by PGC-1α observed in reporter gene assays (Fig. 3B) was linked to direct binding of these two proteins, we tested whether PGC-1α directly interacts with MEF2C on this MEF-binding site. Increasing amounts of PGC-1α protein (amino acids 31–797) decreased the mobility of the complex containing MEF2C bound to the MEF-binding site, as visualized by a supershift in electrophoretic mobility-shift assays (Fig. 3D). As a control, PGC-1α protein that lacks the MEF2C-interaction domain (amino acids 1–180; see ref. 7) was not able to bind to MEF2C. Inclusion of an MEF2- specific antibody was able to supershift further the protein–DNA complex containing MEF2C, PGC-1α, and the MEF2-binding site (Fig. 3E). Neither a shift nor a supershift could be obtained when using the mutated ΔMEF site. These results indicate that MEF2s bind to the PGC-1α promoter and that PGC-1α coactivates MEF2 proteins on the PGC-1α promoter by a direct protein–protein interaction." provenance.
• _8 value "To confirm that the coactivation of MEF2C by PGC-1α observed in reporter gene assays (Fig. 3B) was linked to direct binding of these two proteins, we tested whether PGC-1α directly interacts with MEF2C on this MEF-binding site. Increasing amounts of PGC-1α protein (amino acids 31–797) decreased the mobility of the complex containing MEF2C bound to the MEF-binding site, as visualized by a supershift in electrophoretic mobility-shift assays (Fig. 3D). As a control, PGC-1α protein that lacks the MEF2C-interaction domain (amino acids 1–180; see ref. 7) was not able to bind to MEF2C. Inclusion of an MEF2- specific antibody was able to supershift further the protein–DNA complex containing MEF2C, PGC-1α, and the MEF2-binding site (Fig. 3E). Neither a shift nor a supershift could be obtained when using the mutated ΔMEF site. These results indicate that MEF2s bind to the PGC-1α promoter and that PGC-1α coactivates MEF2 proteins on the PGC-1α promoter by a direct protein–protein interaction." provenance.
• _6 value "Real-time PCR primers were designed for the PGC-1α 3' untranslated region that allows for determination of the levels of ectopically expressed and endogenous PGC-1α. As shown in Fig. 4B and as expected, ectopic PGC-1α is detected only in the muscle of transgenic mice. Strikingly, a 7-fold elevation of endogenous PGC-1α mRNA was seen in the transgenic animals as compared with wild-type mice (Fig. 4B). A robust increase in the transcript levels of cytochrome c and myoglobin also was observed in the RNA isolated from skeletal muscle of the transgenic mice, whereas GAPDH transcript levels remained unchanged (Fig. 4B). These results indicate a regulation of PGC-1α transcription by PGC-1α protein in an apparent autoregulatory loop." provenance.
• _7 value "Expression of myoglobin in C2C12 myotubes also required infection of both PGC-1α and MEF2C (Fig. 5C)." provenance.
• _7 value "APC phosphorylation by Cdk1, but not by Plk1, is sufficient for increased Cdc20 binding and APC activation." provenance.
• _7 value "APC phosphorylation by Cdk1, but not by Plk1, is sufficient for increased Cdc20 binding and APC activation." provenance.
• _4 value "We raised antibodies against two mitosis-specific sites on Cdc27 (phospho-S427 and phospho-T447) and one each on Apc1 (phospho-S355), Cdc16 (phospho-S558) and Cdc23 (phospho-T556." provenance.
• _4 value "We raised antibodies against two mitosis-specific sites on Cdc27 (phospho-S427 and phospho-T447) and one each on Apc1 (phospho-S355), Cdc16 (phospho-S558) and Cdc23 (phospho-T556." provenance.
• _4 value "We raised antibodies against two mitosis-specific sites on Cdc27 (phospho-S427 and phospho-T447) and one each on Apc1 (phospho-S355), Cdc16 (phospho-S558) and Cdc23 (phospho-T556." provenance.
• _6 value "Immunopurified S-phase APC was phosphorylated in vitro using Cdk1, Plk1, or both in the presence of either non-radioactive ATP or [γ-32P]ATP. The latter reactions were analysed by SDS–PAGE followed by silver staining and phosphorimaging (Figure 3A). Both kinases were able to phosphorylate Apc1, Cdc27, Apc5, Cdc16 and Cdc23." provenance.
• _6 value "Immunopurified S-phase APC was phosphorylated in vitro using Cdk1, Plk1, or both in the presence of either non-radioactive ATP or [γ-32P]ATP. The latter reactions were analysed by SDS–PAGE followed by silver staining and phosphorimaging (Figure 3A). Both kinases were able to phosphorylate Apc1, Cdc27, Apc5, Cdc16 and Cdc23." provenance.
• _6 value "Immunopurified S-phase APC was phosphorylated in vitro using Cdk1, Plk1, or both in the presence of either non-radioactive ATP or [γ-32P]ATP. The latter reactions were analysed by SDS–PAGE followed by silver staining and phosphorimaging (Figure 3A). Both kinases were able to phosphorylate Apc1, Cdc27, Apc5, Cdc16 and Cdc23." provenance.
• _6 value "Immunopurified S-phase APC was phosphorylated in vitro using Cdk1, Plk1, or both in the presence of either non-radioactive ATP or [γ-32P]ATP. The latter reactions were analysed by SDS–PAGE followed by silver staining and phosphorimaging (Figure 3A). Both kinases were able to phosphorylate Apc1, Cdc27, Apc5, Cdc16 and Cdc23." provenance.
• _6 value "Immunopurified S-phase APC was phosphorylated in vitro using Cdk1, Plk1, or both in the presence of either non-radioactive ATP or [γ-32P]ATP. The latter reactions were analysed by SDS–PAGE followed by silver staining and phosphorimaging (Figure 3A). Both kinases were able to phosphorylate Apc1, Cdc27, Apc5, Cdc16 and Cdc23." provenance.
• _4 value "Mutations and deletions of tumor suppressor genes, such as p53 or PTEN (phosphatase and tensin homologue deleted on chromosome 10), are two of the several events underlying the loss of apoptotic pathways (4)." provenance.
• _4 value "Mutations and deletions of tumor suppressor genes, such as p53 or PTEN (phosphatase and tensin homologue deleted on chromosome 10), are two of the several events underlying the loss of apoptotic pathways (4)." provenance.
• _4 value "Akt1 is a key cell survival protein functionally involved in antiapoptosis in various cancers (8, 9)." provenance.
• _7 value "A, Akt1, which is activated by PI3K, plays a central role in cell survival by inactivating key agonists of apoptosis." provenance.
• _3 value "Par-4 localizes both to the cytoplasm and the nucleus in many but not all cancer cells and clinical specimens (6, 13–17)." provenance.
• _6 value "PTEN induced apoptosis in prostate cancer cells via a mechanism that was inhibited by blocking endogenous Par-4 expression with RNA interference." provenance.
• _4 value "the lungs of all adult HckF/F mice (3–4 mo and older) showed areas of atelectasis, inflammatory infiltration into the interstitium and alveoli, and some areas of enlarged airspaces" provenance.
• _4 value "We examined how TCDD, alone or in combination with E2, affected luciferase reporter gene expression from the CYP1A1 promoter in MCF-7 cells. As anticipated, TCDD induced a 3.5-fold induction of luciferase activity (Fig. 7A). E2 stimulated a 2-fold induction of luciferase activity from the CYP1A1 promoter." provenance.
• _6 value "Here we tested how expression of COUP–TFI affected TCDD activity from the natural ERE sequences from the pS2 and c-fos promoters in transiently transfected MCF-7 cells. E2 alone stimulated a 1.6- to 2.1-fold induction in luciferase activity from the pS2 ERE (Fig. 8A). 4-OHT blocked the E2 activity, indicating the specificity of the induction by ER. TCDD alone gave a 1.4-fold induction in luciferase activity. Cotreatment with TCDD suppressed E2-stimulated luciferase activity. COUP–TFI inhibited both E2- and TCDD-stimulated luciferase activity from pS2." provenance.
• _5 value "Although both ERα and AHR/ARNT specifically interact with the regulatory region of the c-fos gene, only E2 induced reporter activity from the FOS-1211 construct (Fig. 8B). The FOS-1211 oligomer binds ERa and AHR/ARNT in EMSA (data not shown). TCDD suppressed the E2-stimulated luciferase activity. COUP–TFI significantly inhibited E2-stimulated luciferase activity from FOS–1211, but had no effect in TCDD-treated cells." provenance.
• _4 value "Ang1 and ephrinB2 are subsequently required for further remodeling and maturation of this initially immature vasculature notably as endothelial cells integrate with supporting cells such as smooth muscle cells and pericytes." provenance.
• _4 value "VEGFR2 is the main receptor able to induce endothelial cell proliferation as well as migratory and sprouting activity and to help promote endothelial cells to form tubule-like structures" provenance.
• _4 value "Ang1 would rather have a permissive role by optimizing the manner by which endothelial cells interact with each other and integrate with supporting cells and matrix." provenance.
• _4 value "PGI2 and NO are constitutively released by endothelial cells but their synthesis is increased in response to a similar range of agonists, notably molecules involved in the coagulation process (e.g., bradykinine and thrombin)" provenance.
• _6 value "To be effective, protein C must form a complex with protein S, which is synthesized by endothelial cells (Stern et al., 1991; Esmon, 2000)." provenance.
• _5 value "Complex formation between thrombin and thrombomodulin also prevents thrombin from being able to clot fibrinogen or to activate platelets (Esmon, 1995)." provenance.
• _8 value "Complex formation between thrombin and thrombomodulin also prevents thrombin from being able to clot fibrinogen or to activate platelets (Esmon, 1995)." provenance.
• _7 value "It must be noted that the natural inhibitor of t-PA, plasminogen activator inhibitor type 1 (PAI-1) is also constitutively secreted by endothelial cells." provenance.
• _6 value "The second is the von Willebrand factor (vWF) of which endothelial cells are the major source (Denis, 2002). vWF is constitutively secreted into the plasma and the subendothelial matrix. It is also stored in high amount in Weibel–Palade bodies, which can be mobilized rapidly in response to agonists like thrombin (van Mourik et al., 2002)." provenance.
• _6 value "vWF binds and stabilizes coagulation factor VIII and is a specific factor required for the binding of platelets to exposed extracellular matrix components when the vessel wall is damaged (Ruggeri and Preissner, 1999)." provenance.
• _4 value "vWF binds and stabilizes coagulation factor VIII and is a specific factor required for the binding of platelets to exposed extracellular matrix components when the vessel wall is damaged (Ruggeri and Preissner, 1999)." provenance.
• _6 value "However, when exposed to thrombin, cytokines, or LPS, endothelial cells synthesize and express tissue factor at their surface (Nawroth et al., 1986; Mackman, 1997)." provenance.
• _5 value "Thrombin is the main effector protease of the coagulation cascade. Factor Xa, activated by factor VIIa and tissue factor, converts prothrombin to active thrombin." provenance.

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