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• _5 value "Interestingly, when lysates from co-transfection experiments were blotted with anti-receptor antibodies, a loss of EGFR, ErbB2, ErbB3, and ErbB4 was observed in the presence of LRIG1, but no loss of insulin receptor was observed despite very efficient transfection of these cells (Fig. 1C, compare lanes 1 and 3 in all panels). These observations suggest that a functional consequence of LRIG1 interaction with receptor tyrosine kinases may be suppression of receptor levels to lower the efficiency of signaling." provenance.
• _6 value "To determine whether LRIG1 expression influences the ubiquitination and degradation rate of ErbB receptors in the inducible expression system, we focused on the effect of LRIG1 expression on the properties of EGFR in the PC3-LRIG1 cells. Similar to the results with transfected 293T cells (Fig. 3), we observed that the induction of LRIG1 expression markedly augmented the ubiquitination of EGFR in response to EGF treatment (Fig. 5A). This potentiation of ligand-stimulated EGFR ubiquitination correlated with a suppression of EGFR tyrosine phosphorylation and receptor levels after growth factor treatment." provenance.
• _5 value "In the experiment illustrated in Fig. 5B, PC3-LRIG1 cells were treated with and without tetracycline to induce LRIG1 expression, and a time course of EGF stimulation of the cells was carried out. Lysates were immunoblotted with anti-phosphotyrosine and anti-EGFR antibodies. In the presence of LRIG1, EGFR responded less efficiently to EGF as determined by blotting autophosphorylated receptors with anti-phosphotyrosine. Interestingly, LRIG1 expression also resulted in an accelerated loss of EGFR." 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 "Our results show that 14 days of coinfusion of MAPK/ERK kinase inhibitor PD-098059 (PD) limited the phosphorylation of ERK and prevented IGF-I induced increases in protein (18%, P < 0.05 vs. 7%, not significant) or myofibrillar protein (23%, P < 0.01 vs. 5%, not significant)." provenance.
• _5 value "The most notable impact on IGF-I signaling was a significant blunting of IGF-I induced increase in S6K1 phosphorylation by PD-98059 coinfusion (~ 5-fold, P < 0.001 vs. 3-fold, P < 0.01)." provenance.
• _4 value "Muscle hypertrophy. Local infusion of IGF-I for 14 days resulted in a 19% increase in muscle wet weight and an 18% increase in the total protein content of the IGF but not the IGF+PD plantaris muscles (Fig. 1A, Table 1). Total protein concentration was unchanged in both treatment groups (Table 1). IGF-I infusion resulted in a 23% increase in myofibrillar protein content (IGF group) that was completely blunted by coinfusion of MEK inhibitor PD-098059 (Fig. 1B)." provenance.
• _5 value "Mitogenic indicators. The DNA content of the IGF and IGF+PD infused muscles increased ~50% compared with the contralateral muscles (Fig. 2A). The concentration of DNA was also increased by both treatments (Table 1). Similarly, there was a significant increase in the expression and/or accumulation of cyclin D1 mRNA in the IGF and IGF+PD muscles (Fig. 2B)." provenance.
• _5 value "IGF-I-related mRNA. IGF-I infusion resulted in a 48 and 63% increase in IGFBP-5 mRNA in the IGF and IGFPD muscles, respectively (Fig. 7A). The mRNA for IGFBP-4 increased significantly (4-fold) in the IGFPD but not IGF muscles (Fig. 7B)." provenance.
• _6 value "IGF-I-related mRNA. IGF-I infusion resulted in a 48 and 63% increase in IGFBP-5 mRNA in the IGF and IGFPD muscles, respectively (Fig. 7A). The mRNA for IGFBP-4 increased significantly (4-fold) in the IGFPD but not IGF muscles (Fig. 7B)." provenance.
• _6 value "PDGF stimulation of quiescent NIH 3T3 cells leads to activation of both the PI3'-kinase3→PDK1→AKT and the RAF→MEK→ERK signaling pathways and repression of p27Kip1 expression (Fig. 3A)." provenance.
• _5 value "PDGF stimulation of quiescent NIH 3T3 cells leads to activation of both the PI3'-kinase3→PDK1→AKT and the RAF→MEK→ERK signaling pathways and repression of p27Kip1 expression (Fig. 3A)." provenance.
• _7 value "Hs766T cells express activated KRAS and display elevated levels of pERK1/2 and pAKT (Fig. 4C)." provenance.
• _5 value "Treatment of Hs766T cells with the PI3'-kinase inhibitor LY294002 led to a selective decrease in pAKT with little or no effect on pERK1/2." provenance.
• _4 value "both the PI3'-kinase and the MEK inhibitors led to accumulation of p27Kip1 expression." provenance.
• _5 value "both the PI3'-kinase and the MEK inhibitors led to accumulation of p27Kip1 expression." provenance.
• _5 value "both the PI3'-kinase and the MEK inhibitors led to accumulation of p27Kip1 expression." provenance.
• _9 value "Phosphorylation of p27Kip1 on threonine 187 (T187) by active cdk2 leads to its recognition by the F-box protein SCFSkp2, thereby promoting p27Kip1 ubiquitination and destruction by the 26S proteasome (45)." provenance.
• _7 value "AKT promoted nuclear export of RAF-induced p21Cip1 into a cytoplasmic compartment as reported previously (Fig. 7C) (65)." provenance.
• _6 value "COS-7 cells were transiently transfected with expression vectors for SUMO-1 together with HDAC4 or HDAC4-K559R followed by immunoprecipitation using the anti-HDAC4 antibodies and an assay for histone deacetylase activity (Figure 4B). Although the two proteins were expressed at a similar level (inset), the HDAC activity associated with HDAC4-K559R was significantly reduced, to a level barely above that of endogenous HDAC4 (compare lane 3 with lanes 1 and 2)." provenance.
• _5 value "As seen in Figure 4C, both the modified and unmodified HDAC4 species were retained efficiently by GST–N-CoR, GST–MEF2C and GST–14-3-3ε but not by the GST–PML control." provenance.
• _5 value "As seen in Figure 4C, both the modified and unmodified HDAC4 species were retained efficiently by GST–N-CoR, GST–MEF2C and GST–14-3-3ε but not by the GST–PML control." provenance.
• _6 value "Moreover RanBP2 functions catalytically as 5 ng of BP2ΔFG were sufficient to promote modification of a 100-fold molar excess of HDAC4. Thus, RanBP2 plays an E3-like role in SUMO modification of HDAC4." provenance.
• _5 value "A POSH mutant that is unable to bind Akt2" provenance.
• _7 value "In addition, we show that the association of MLK3 with POSH is increased upon inhibition of the endogenous phosphatidylinositol 3-kinase/Akt signaling pathway." provenance.
• _6 value "This increase in the MLK-POSH complex is accompanied by an increase in phospho-c-Jun, a measure of JNK pathway activation (Fig. 5B)." provenance.
• _6 value "In this report, we show that the PGC-1α promoter is regulated by both CaMKIV and CnA activity. CaMKIV activates PGC-1α largely through the binding of cAMP response element-binding protein to the PGC-1α promoter." 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.
• _6 value "Promoter fragments that contain either 2 or 6 kb of 5' flanking region of mouse PGC-1α both are activated at least 3-fold by the expression of constitutively active CaMKIV (Fig. 1A). In contrast, expression of a constitutively active CnA has very little effect on reporter gene activity, consistent with the results obtained previously for PGC-1α mRNA expression in CaMKIV and CnA transgenic mice (11). However, the combination of CaMKIV and CnA has a powerful effect on the PGC-1α promoter, increasing transcription by ~7-fold (Fig. 1A)." provenance.
• _5 value "Promoter fragments that contain either 2 or 6 kb of 5' flanking region of mouse PGC-1α both are activated at least 3-fold by the expression of constitutively active CaMKIV (Fig. 1A). In contrast, expression of a constitutively active CnA has very little effect on reporter gene activity, consistent with the results obtained previously for PGC-1α mRNA expression in CaMKIV and CnA transgenic mice (11). However, the combination of CaMKIV and CnA has a powerful effect on the PGC-1α promoter, increasing transcription by ~7-fold (Fig. 1A)." 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.
• _7 value "Expression of myoglobin in C2C12 myotubes also required infection of both PGC-1α and MEF2C (Fig. 5C)." provenance.
• _5 value "Troponin I slow is induced after infection with virally encoded MEF2C, and the addition of PGC-1α has no further effect (Fig. 5D). In contrast, GLUT4 transcript levels can be elevated by PGC-1α alone, independent of MEF2C infection, consistent with previous reports (7) (Fig. 5E)." provenance.
• _4 value "The anaphase-promoting complex (APC) or cyclosome is a ubiquitin ligase that initiates anaphase and mitotic exit." provenance.
• _7 value "APC phosphorylation by Cdk1, but not by Plk1, is sufficient for increased Cdc20 binding and APC activation." provenance.
• _5 value "Cdc20 peptides were only found in mitotic APC samples, confirming that Cdc20 associates with APC in a mitosis-specific manner." 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 "These observations indicate that normal Plk1 levels are not essential for APC-mediated degradation of cyclin A." 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.
• _7 value "The interaction of the cell survival kinase, Akt1 (5), with the prostate apoptosis response-4 protein, Par-4 (6), results in phosphorylation and silencing of Par-4 (7) and thus offers an intervention target for the selective induction of apoptosis in cancer cells." 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.
• _4 value "Par-4 knockout mice spontaneously develop tumors of the liver, lung, and endometrium, exhibit prostatic intraepithelial neoplasia (PIN), and show an increased frequency of estrogen-inducible tumors in the endometrium and BBN-inducible tumors in the bladder (18)." provenance.
• _5 value "Indeed, our recent studies reveal that binding of Akt1 to Par-4 results in both Par-4 phosphorylation and inactivation of its proapoptotic potential (7)." provenance.
• _7 value "Indeed, our recent studies reveal that binding of Akt1 to Par-4 results in both Par-4 phosphorylation and inactivation of its proapoptotic potential (7)." provenance.
• _6 value "Nuclear translocation of Par-4 is essential for the inhibition of NF-κB-dependent transcriptional activity" provenance.
• _5 value "Par-4 partner proteins WT1, ZIPK/DAXX, and THAP" provenance.
• _7 value "We recently showed that the cancer-selective proapoptotic protein Par-4 is a key target for inactivation by PI3K/Akt signaling" provenance.
• _4 value "lungs from HckF/F mice showed areas of mild emphysema, as histologically evident from alveolar enlargement with the loss of the orderly appearance of the acinus, and signs of fibrosis characterized by deposition of extracellular matrix in the alveolar septa (Fig. 2, e and f)." provenance.
• _5 value "BAL-F recovered from the lungs of mutant mice revealed elevated levels of IL-5 (70 ± 27 pg/ml in HckY/Y versus 17 ± 5 pg/ml in HckY/Y) and eotaxin (37 ± 8 pg/ml in HckY/Y versus 23 ± 4 pg/ml in HckY/Y), features associated with eosinophilia (28, 29)." provenance.
• _3 value "Such a pulmonary challenge with LPS elicits a rapid and transient neutrophilic inflammatory response, followed by macrophage invasion into the alveolar spaces (31)." provenance.
• _4 value "BMDMs derived from HckF/F mice exhibited an enhanced capacity to migrate when tested in in vitro \"wound-healing\" assays (unpublished data)." provenance.
• _5 value "PMNs from HckF/F mice released approximately twofold more superoxide in response to TNFα or fMLP stimulation than did their wild-type counterparts when plated on fibrinogen-coated microtiter plates" provenance.
• _4 value "In transiently transfected MCF-7 human breast cancer cells, overexpression of COUP-TFI inhibited TCDD-activated reporter gene activity from the CYP1A1 promoter. TCDD inhibited estradiol (E2)-activated reporter gene activity from a consensus ERE and from the EREs in the pS2 and Fos genes, and COUP-TFI did not block the antiestrogenic activity of TCDD." provenance.
• _7 value "Estradiol reportedly blocked TCDD-induced accumulation of CYP1A1 mRNA and AHR-mediated activation of the CYP1A1 gene promoter in MCF-7 cells (32)." provenance.
• _5 value "TCDD inhibits E2-induction of pS2, a human breast cancer prognostic marker (47), and stimulates c-fos expression (48)." provenance.
• _5 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.
• _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.
• _7 value "GSK-3 activity is inhibited through phosphorylation of serine 21 in GSK-3α and serine 9 in GSK-3β. These serine residues of GSK-3 have been previously identified as targets of protein kinase B (PKByAkt), a serineythreonine kinase located downstream of phosphatidylinositol 3-kinase." provenance.
• _7 value "Here, we show that serine 21 in GSK-3α and serine 9 in GSK-3β are also physiological substrates of cAMP dependent protein kinase A. Protein kinase A physically associates with, phosphorylates, and inactivates both isoforms of GSK-3." provenance.
• _4 value "In Rat1, NIH 3T3, and HEK293 cells, increases in the intracellular levels of cAMP stimulate phosphorylation of GSK-3α and -β, as demonstrated by immunoblotting with GSK-3 phosphorylation-specific antibodies. As shown in Fig. 1, the cell-permeable cAMP analogue 8-Br-cAMP induced a marked increase in phosphorylation of GSK-3α and - β at serine 21 and 9, respectively, whereas the structurally related cGMP analogue 8-Br-cGMP had little effect. Forskolin, which activates adenyl cyclase thus raising intracellular cAMP levels (15), triggered a similar elevation in GSK-3 phosphorylation at serine 21 and 9. In Rat1 cells, isoproterenol, which activates the b-adrenergic receptor stimulating adenylate cyclase and increasing endogenous cAMP levels (16, 17), also efficiently stimulated GSK-3 phosphorylation at these serine sites. In NIH 3T3 cells that contain few of the β-adrenergic receptors, stimulation with other G-protein-coupled receptor agonists, such as lysophosphatidic acid. also led to GSK-3 phosphorylation (data not shown)" provenance.
• _4 value "In Rat1, NIH 3T3, and HEK293 cells, increases in the intracellular levels of cAMP stimulate phosphorylation of GSK-3α and -β, as demonstrated by immunoblotting with GSK-3 phosphorylation-specific antibodies. As shown in Fig. 1, the cell-permeable cAMP analogue 8-Br-cAMP induced a marked increase in phosphorylation of GSK-3α and - β at serine 21 and 9, respectively, whereas the structurally related cGMP analogue 8-Br-cGMP had little effect. Forskolin, which activates adenyl cyclase thus raising intracellular cAMP levels (15), triggered a similar elevation in GSK-3 phosphorylation at serine 21 and 9. In Rat1 cells, isoproterenol, which activates the b-adrenergic receptor stimulating adenylate cyclase and increasing endogenous cAMP levels (16, 17), also efficiently stimulated GSK-3 phosphorylation at these serine sites. In NIH 3T3 cells that contain few of the β-adrenergic receptors, stimulation with other G-protein-coupled receptor agonists, such as lysophosphatidic acid. also led to GSK-3 phosphorylation (data not shown)" provenance.
• _4 value "In Rat1, NIH 3T3, and HEK293 cells, increases in the intracellular levels of cAMP stimulate phosphorylation of GSK-3α and -β, as demonstrated by immunoblotting with GSK-3 phosphorylation-specific antibodies. As shown in Fig. 1, the cell-permeable cAMP analogue 8-Br-cAMP induced a marked increase in phosphorylation of GSK-3α and - β at serine 21 and 9, respectively, whereas the structurally related cGMP analogue 8-Br-cGMP had little effect. Forskolin, which activates adenyl cyclase thus raising intracellular cAMP levels (15), triggered a similar elevation in GSK-3 phosphorylation at serine 21 and 9. In Rat1 cells, isoproterenol, which activates the b-adrenergic receptor stimulating adenylate cyclase and increasing endogenous cAMP levels (16, 17), also efficiently stimulated GSK-3 phosphorylation at these serine sites. In NIH 3T3 cells that contain few of the β-adrenergic receptors, stimulation with other G-protein-coupled receptor agonists, such as lysophosphatidic acid. also led to GSK-3 phosphorylation (data not shown)" provenance.
• _4 value "In Rat1, NIH 3T3, and HEK293 cells, increases in the intracellular levels of cAMP stimulate phosphorylation of GSK-3α and -β, as demonstrated by immunoblotting with GSK-3 phosphorylation-specific antibodies. As shown in Fig. 1, the cell-permeable cAMP analogue 8-Br-cAMP induced a marked increase in phosphorylation of GSK-3α and - β at serine 21 and 9, respectively, whereas the structurally related cGMP analogue 8-Br-cGMP had little effect. Forskolin, which activates adenyl cyclase thus raising intracellular cAMP levels (15), triggered a similar elevation in GSK-3 phosphorylation at serine 21 and 9. In Rat1 cells, isoproterenol, which activates the b-adrenergic receptor stimulating adenylate cyclase and increasing endogenous cAMP levels (16, 17), also efficiently stimulated GSK-3 phosphorylation at these serine sites. In NIH 3T3 cells that contain few of the β-adrenergic receptors, stimulation with other G-protein-coupled receptor agonists, such as lysophosphatidic acid. also led to GSK-3 phosphorylation (data not shown)" provenance.
• _4 value "PI3K-dependent activation of PKB is an intermediary in the phosphorylation and inactivation of GSK-3 induced by insulin and other growth factors (10, 12, 14). Insulin and IGF-1 efficiently activate the PI3K pathway in NIH 3T3 and Rat1 cells, respectively. GSK-3 phosphorylation induced by insulin and IGF-1 were eliminated by pretreatment with the PI3K inhibitors wortmannin or LY294002. In contrast, the effects of 8-Br-cAMP or forskolin on GSK-3 phosphorylation in these cell lines were not altered by inhibition of PI3K activity with wortmannin or LY294002 (Fig. 2A), excluding the possibility that PKA induces GSK-3 phosphorylation through activation of PI3K." provenance.
• _5 value "PI3K-dependent activation of PKB is an intermediary in the phosphorylation and inactivation of GSK-3 induced by insulin and other growth factors (10, 12, 14). Insulin and IGF-1 efficiently activate the PI3K pathway in NIH 3T3 and Rat1 cells, respectively. GSK-3 phosphorylation induced by insulin and IGF-1 were eliminated by pretreatment with the PI3K inhibitors wortmannin or LY294002. In contrast, the effects of 8-Br-cAMP or forskolin on GSK-3 phosphorylation in these cell lines were not altered by inhibition of PI3K activity with wortmannin or LY294002 (Fig. 2A), excluding the possibility that PKA induces GSK-3 phosphorylation through activation of PI3K." provenance.
• _6 value "PI3K-dependent activation of PKB is an intermediary in the phosphorylation and inactivation of GSK-3 induced by insulin and other growth factors (10, 12, 14). Insulin and IGF-1 efficiently activate the PI3K pathway in NIH 3T3 and Rat1 cells, respectively. GSK-3 phosphorylation induced by insulin and IGF-1 were eliminated by pretreatment with the PI3K inhibitors wortmannin or LY294002. In contrast, the effects of 8-Br-cAMP or forskolin on GSK-3 phosphorylation in these cell lines were not altered by inhibition of PI3K activity with wortmannin or LY294002 (Fig. 2A), excluding the possibility that PKA induces GSK-3 phosphorylation through activation of PI3K." provenance.
• _6 value "PI3K-dependent activation of PKB is an intermediary in the phosphorylation and inactivation of GSK-3 induced by insulin and other growth factors (10, 12, 14). Insulin and IGF-1 efficiently activate the PI3K pathway in NIH 3T3 and Rat1 cells, respectively. GSK-3 phosphorylation induced by insulin and IGF-1 were eliminated by pretreatment with the PI3K inhibitors wortmannin or LY294002. In contrast, the effects of 8-Br-cAMP or forskolin on GSK-3 phosphorylation in these cell lines were not altered by inhibition of PI3K activity with wortmannin or LY294002 (Fig. 2A), excluding the possibility that PKA induces GSK-3 phosphorylation through activation of PI3K." provenance.
• _4 value "To determine whether PKA-induced PKB activation accounts for GSK-3 phosphorylation after treatment with 8-Br-cAMP, forskolin, or isoproterenol, PKB phosphorylation at serine 473 and threonine 308, which is crucial for activation of PKB (20), was assessed. As expected, insulin and IGF-1 strongly stimulated phosphorylation of PKB at serine 473 in NIH 3T3 or Rat1 cells (Fig. 2B). In contrast, 8-Br-cAMP, forskolin, and isoproterenol did not significantly alter PKB phosphorylation at serine 473 (Fig. 2B). Similar results were obtained with a threonine 308 phosphorylation-specific antibody (data not shown)." provenance.
• _5 value "Forskolin increased PKB activity weakly in Rat1 and NIH 3T3 cells. A slightly stronger stimulation of PKB activity was seen in Rat1 cells treated with isoproterenol. However, activation of PKB by forskolin or isoproterenol was much less than that induced by IGF-1 or insulin (Fig. 2C)." provenance.
• _6 value "These in vivo and in vitro observations establish that PKA can directly phosphorylate and inactivate GSK-3." provenance.
• _6 value "BAD was originally demonstrated to be phosphorylated at serine 136 by PKB (32, 33). However, BAD can also be inactivated through phosphorylation of serine 112 by Rsk, which is located downstream of mitogen-activated protein kinases (MAPKyErk) (34–36), or alternatively by mitochondriaanchored PKA (37). Additionally, Rsk can phosphorylate CREB at the same serine 133 site as PKA, leading to the expression of cAMP-responsive genes (34)." provenance.
• _6 value "BAD was originally demonstrated to be phosphorylated at serine 136 by PKB (32, 33). However, BAD can also be inactivated through phosphorylation of serine 112 by Rsk, which is located downstream of mitogen-activated protein kinases (MAPKyErk) (34–36), or alternatively by mitochondriaanchored PKA (37). Additionally, Rsk can phosphorylate CREB at the same serine 133 site as PKA, leading to the expression of cAMP-responsive genes (34)." provenance.
• _6 value "BAD was originally demonstrated to be phosphorylated at serine 136 by PKB (32, 33). However, BAD can also be inactivated through phosphorylation of serine 112 by Rsk, which is located downstream of mitogen-activated protein kinases (MAPKyErk) (34–36), or alternatively by mitochondriaanchored PKA (37). Additionally, Rsk can phosphorylate CREB at the same serine 133 site as PKA, leading to the expression of cAMP-responsive genes (34)." provenance.
• _4 value "VEGF was initially defined, characterized, and purified for its ability to induce vascular leak and permeability as well as for its ability to promote endothelial cell proliferation (Ferrara, 1999)." 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.
• _5 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.
• _7 value "The protein C/protein S pathway is initiated when thrombin interacts with the endothelial cell receptor thrombomodulin, facilitating activation of protein C (Sadler, 1997)." provenance.
• _5 value "Activated protein C inactivates two cofactors essential for blood coagulation: factors VIIIa and Va." 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.
• _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.
• _5 value "In endothelial cells, thrombin causes vWF release, the appearance of P-selectin at the plasma membrane, production of PAF and chemokines." provenance.
• _3 value "The NO generation by endothelial cells is constitutive but may be enhanced by a wide variety of compounds, including acetylcholine, angiotensin II, bradykinin, histamine, adenine nucleotides, arachidonic acid" provenance.
• _3 value "The NO generation by endothelial cells is constitutive but may be enhanced by a wide variety of compounds, including acetylcholine, angiotensin II, bradykinin, histamine, adenine nucleotides, arachidonic acid" provenance.
• _3 value "The NO generation by endothelial cells is constitutive but may be enhanced by a wide variety of compounds, including acetylcholine, angiotensin II, bradykinin, histamine, adenine nucleotides, arachidonic acid" provenance.
• _5 value "EDRF diffuses to the vascular smooth muscle cells where it stimulates soluble guanylate cyclase, resulting in an increased formation of cyclic GMP and subsequent relaxation (Fig. 2A) (Denninger and Marletta, 1999)." provenance.
• _4 value "Endothelial cells constitutively release PGI2 (Moncada et al., 1976) which appears to be involved in the regulation of resting vascular tone, in addition to EDRF. It is released in higher amount in response to ligand binding on the cell surface such as thrombin, arachidonic acid, histamine, serotonin" provenance.
• _6 value "The endothelinA (ETA) receptor is situated on the vascular smooth muscle cells and has a high affinity for ET-1 and ET-2 but not for ET-3." provenance.
• _6 value "The endothelinA (ETA) receptor is situated on the vascular smooth muscle cells and has a high affinity for ET-1 and ET-2 but not for ET-3." provenance.
• _6 value "the endothelinB (ETB) receptor is situated on the endothelial cells and has a similar affinity for the three endothelin isoforms." provenance.
• _6 value "the endothelinB (ETB) receptor is situated on the endothelial cells and has a similar affinity for the three endothelin isoforms." provenance.
• _6 value "The result of ET binding to ETB receptor on endothelial cells is the release of EDRF/ PGI2, which opposes the vasoconstricting action of ET." provenance.
• _6 value "Endothelial (eNOS) and neuronal (nNOS) isoforms are constitutively expressed and are activated by calmodulin/calcium." provenance.
• _5 value "eNOS activity is also regulated at the transcriptional level: VEGF, insulin, bFGF increase eNOS expression while hypoxia and oxidized LDL decrease it (Sase and Michel, 1997)." provenance.
• _5 value "the induced adherence in inflammatory situation requires induction of L-selectin ligand and/or of E- and P-selectins on the endothelial surface. E-selectin is transcriptionally induced by cytokines such as IL-1, TNF-α, or by LPS (Klein et al., 1995; Scholz et al., 1996)." provenance.
• _6 value "In contrast, P-selectin is stored in the membrane of storage granules, the Weibel– Palade bodies, in endothelial cells (McEver et al., 1989). Fusion of these granules with the plasma membrane is rapidly stimulated by proinflammatory mediators such as histamine and thrombin." provenance.

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