Matches in Nanopublications for { ?s <http://www.w3.org/ns/prov#value> ?o ?g. }
- _3 value "Simultaneous overexpression of selenophosphate synthetase and phospholipid-hydroperoxide GSH peroxidase (PHGPx) [250] blocks activation of NF-kB by IL-1. Overexpression of SOD [84] or GSH peroxidase [81, 211] abolished NF-kB activation by preventing degradation of IkB after stimulation with TNF-a. The precise mechanism(s) through which oxidants and reductants influence activation of NF-kB is presently unknown; however, there is evidence that antioxidant enzyme (AOE372), a redox-sensitive thioredoxin peroxidase, regulates IkB phosphorylation [246]. Phosphatases The phosphatases are an important component of most signal transduction pathways, because failure to reverse kinase actions can disrupt normal cellular functions. For example, transfection of human fibroblasts with constitutively active ras (hRasV12) inhibits cell growth and ultimately results in a senescentlike phenotype [441]. Similarly, constitutive ERK activation has an inhibitory effect on cell cycle progression [442,443]. Both the serine/threonine phosphatases and the PTPs are known to be redox-sensitive [82,144,153,156,271,281, 444-449]. The mechanism of redox effects on activity is probably best understood for the PTPs. Without exception, the PTPs contain a highly conserved region of 11 amino acid residues in their catalytic domain; specifi- cally, (Ile/Val)-His-Cys-X-Ala-Gly-X-X-Arg-(Ser/Thr)- Gly, where X is a nonconserved amino acid [17]. Either oxidation or mutation of the cysteine renders these molecules inactive [17,281]. H2O2 is a potent inhibitor of PTPs. As in the case of other oxidants, H2O2 probably oxidizes the thiolate anion at the catalytic site [280]. Because formation of a phosphorylcysteine intermediate seems to be critical to PTP activity [450-452], blocking it through oxidation of the cysteine inactivates the molecules. In many cases, treatment of cells with H2O2 stimulates increases in protein phosphorylation by inhibiting phosphatase-catalyzed removal of phosphate groups. Furthermore, mitogens that increase cellular ox- idant production may stimulate phosphorylation indirectly by decreasing phosphatase activity. Additional mechanisms are involved in stimulation of pathways activated by growth factors that increase oxidant production, however, because there are known instances in which the oxidants they produce have no effect on protein phosphorylation. For example, TGF-b1 stimulates phosphorylation of numerous proteins and has been shown to cause a large increase in H2O2 production; however, its effects on protein phosphorylation are not blocked by catalase [453]. Furthermore, H2O2 is effective in promoting phosphorylation of phospholipase D, the PDGF receptor, and PKC-a even after pretreatment of Swiss 3T3 fibroblasts with orthovanadate to inhibit phosphatases [454]. Thus, although diminished phosphatase activity may partially account for increased phosphorylation in some cases, it cannot totally account for oxidation effects on phosphorylation in every case. SPECIFICITY In general, there is good agreement between studies on redox effects on any given gene; albeit, not all oxidizing or reducing treatments exert equivalent effects. This is clearly demonstrated in studies of pag , which encodes a protein associated with cellular proliferation. Pag protein inhibits the tyrosine kinase activity of the Abelson (abl ) protein by binding to its SH3-binding domain [455]. BSO, menadione, sodium arsenate, and diethyl maleate all stimulate pag expression, but H2O2 does not [269]. Conversely, H2O2 stimulates c-fos expression (Table 1), although 4-hydroynonenal (a product of v-6-polyunsaturated fatty acid peroxidation) not only fails to induce c-fos expression but is actually inhibitory to c-fos induction by EGF and PDGF [185]. Similarly, some oxidants such as diamide decrease hypoxia-induced signals [201], although others such as H2O2 increase them [124]. As might be expected, the effects of any stimu..." provenance.
- _3 value "Simultaneous overexpression of selenophosphate synthetase and phospholipid-hydroperoxide GSH peroxidase (PHGPx) [250] blocks activation of NF-kB by IL-1. Overexpression of SOD [84] or GSH peroxidase [81, 211] abolished NF-kB activation by preventing degradation of IkB after stimulation with TNF-a. The precise mechanism(s) through which oxidants and reductants influence activation of NF-kB is presently unknown; however, there is evidence that antioxidant enzyme (AOE372), a redox-sensitive thioredoxin peroxidase, regulates IkB phosphorylation [246]. Phosphatases The phosphatases are an important component of most signal transduction pathways, because failure to reverse kinase actions can disrupt normal cellular functions. For example, transfection of human fibroblasts with constitutively active ras (hRasV12) inhibits cell growth and ultimately results in a senescentlike phenotype [441]. Similarly, constitutive ERK activation has an inhibitory effect on cell cycle progression [442,443]. Both the serine/threonine phosphatases and the PTPs are known to be redox-sensitive [82,144,153,156,271,281, 444-449]. The mechanism of redox effects on activity is probably best understood for the PTPs. Without exception, the PTPs contain a highly conserved region of 11 amino acid residues in their catalytic domain; specifi- cally, (Ile/Val)-His-Cys-X-Ala-Gly-X-X-Arg-(Ser/Thr)- Gly, where X is a nonconserved amino acid [17]. Either oxidation or mutation of the cysteine renders these molecules inactive [17,281]. H2O2 is a potent inhibitor of PTPs. As in the case of other oxidants, H2O2 probably oxidizes the thiolate anion at the catalytic site [280]. Because formation of a phosphorylcysteine intermediate seems to be critical to PTP activity [450-452], blocking it through oxidation of the cysteine inactivates the molecules. In many cases, treatment of cells with H2O2 stimulates increases in protein phosphorylation by inhibiting phosphatase-catalyzed removal of phosphate groups. Furthermore, mitogens that increase cellular ox- idant production may stimulate phosphorylation indirectly by decreasing phosphatase activity. Additional mechanisms are involved in stimulation of pathways activated by growth factors that increase oxidant production, however, because there are known instances in which the oxidants they produce have no effect on protein phosphorylation. For example, TGF-b1 stimulates phosphorylation of numerous proteins and has been shown to cause a large increase in H2O2 production; however, its effects on protein phosphorylation are not blocked by catalase [453]. Furthermore, H2O2 is effective in promoting phosphorylation of phospholipase D, the PDGF receptor, and PKC-a even after pretreatment of Swiss 3T3 fibroblasts with orthovanadate to inhibit phosphatases [454]. Thus, although diminished phosphatase activity may partially account for increased phosphorylation in some cases, it cannot totally account for oxidation effects on phosphorylation in every case. SPECIFICITY In general, there is good agreement between studies on redox effects on any given gene; albeit, not all oxidizing or reducing treatments exert equivalent effects. This is clearly demonstrated in studies of pag , which encodes a protein associated with cellular proliferation. Pag protein inhibits the tyrosine kinase activity of the Abelson (abl ) protein by binding to its SH3-binding domain [455]. BSO, menadione, sodium arsenate, and diethyl maleate all stimulate pag expression, but H2O2 does not [269]. Conversely, H2O2 stimulates c-fos expression (Table 1), although 4-hydroynonenal (a product of v-6-polyunsaturated fatty acid peroxidation) not only fails to induce c-fos expression but is actually inhibitory to c-fos induction by EGF and PDGF [185]. Similarly, some oxidants such as diamide decrease hypoxia-induced signals [201], although others such as H2O2 increase them [124]. As might be expected, the effects of any stimu..." provenance.
- _3 value "Simultaneous overexpression of selenophosphate synthetase and phospholipid-hydroperoxide GSH peroxidase (PHGPx) [250] blocks activation of NF-kB by IL-1. Overexpression of SOD [84] or GSH peroxidase [81, 211] abolished NF-kB activation by preventing degradation of IkB after stimulation with TNF-a. The precise mechanism(s) through which oxidants and reductants influence activation of NF-kB is presently unknown; however, there is evidence that antioxidant enzyme (AOE372), a redox-sensitive thioredoxin peroxidase, regulates IkB phosphorylation [246]. Phosphatases The phosphatases are an important component of most signal transduction pathways, because failure to reverse kinase actions can disrupt normal cellular functions. For example, transfection of human fibroblasts with constitutively active ras (hRasV12) inhibits cell growth and ultimately results in a senescentlike phenotype [441]. Similarly, constitutive ERK activation has an inhibitory effect on cell cycle progression [442,443]. Both the serine/threonine phosphatases and the PTPs are known to be redox-sensitive [82,144,153,156,271,281, 444-449]. The mechanism of redox effects on activity is probably best understood for the PTPs. Without exception, the PTPs contain a highly conserved region of 11 amino acid residues in their catalytic domain; specifi- cally, (Ile/Val)-His-Cys-X-Ala-Gly-X-X-Arg-(Ser/Thr)- Gly, where X is a nonconserved amino acid [17]. Either oxidation or mutation of the cysteine renders these molecules inactive [17,281]. H2O2 is a potent inhibitor of PTPs. As in the case of other oxidants, H2O2 probably oxidizes the thiolate anion at the catalytic site [280]. Because formation of a phosphorylcysteine intermediate seems to be critical to PTP activity [450-452], blocking it through oxidation of the cysteine inactivates the molecules. In many cases, treatment of cells with H2O2 stimulates increases in protein phosphorylation by inhibiting phosphatase-catalyzed removal of phosphate groups. Furthermore, mitogens that increase cellular ox- idant production may stimulate phosphorylation indirectly by decreasing phosphatase activity. Additional mechanisms are involved in stimulation of pathways activated by growth factors that increase oxidant production, however, because there are known instances in which the oxidants they produce have no effect on protein phosphorylation. For example, TGF-b1 stimulates phosphorylation of numerous proteins and has been shown to cause a large increase in H2O2 production; however, its effects on protein phosphorylation are not blocked by catalase [453]. Furthermore, H2O2 is effective in promoting phosphorylation of phospholipase D, the PDGF receptor, and PKC-a even after pretreatment of Swiss 3T3 fibroblasts with orthovanadate to inhibit phosphatases [454]. Thus, although diminished phosphatase activity may partially account for increased phosphorylation in some cases, it cannot totally account for oxidation effects on phosphorylation in every case. SPECIFICITY In general, there is good agreement between studies on redox effects on any given gene; albeit, not all oxidizing or reducing treatments exert equivalent effects. This is clearly demonstrated in studies of pag , which encodes a protein associated with cellular proliferation. Pag protein inhibits the tyrosine kinase activity of the Abelson (abl ) protein by binding to its SH3-binding domain [455]. BSO, menadione, sodium arsenate, and diethyl maleate all stimulate pag expression, but H2O2 does not [269]. Conversely, H2O2 stimulates c-fos expression (Table 1), although 4-hydroynonenal (a product of v-6-polyunsaturated fatty acid peroxidation) not only fails to induce c-fos expression but is actually inhibitory to c-fos induction by EGF and PDGF [185]. Similarly, some oxidants such as diamide decrease hypoxia-induced signals [201], although others such as H2O2 increase them [124]. As might be expected, the effects of any stimu..." provenance.
- _5 value "Simultaneous overexpression of selenophosphate synthetase and phospholipid-hydroperoxide GSH peroxidase (PHGPx) [250] blocks activation of NF-kB by IL-1. Overexpression of SOD [84] or GSH peroxidase [81, 211] abolished NF-kB activation by preventing degradation of IkB after stimulation with TNF-a. The precise mechanism(s) through which oxidants and reductants influence activation of NF-kB is presently unknown; however, there is evidence that antioxidant enzyme (AOE372), a redox-sensitive thioredoxin peroxidase, regulates IkB phosphorylation [246]. Phosphatases The phosphatases are an important component of most signal transduction pathways, because failure to reverse kinase actions can disrupt normal cellular functions. For example, transfection of human fibroblasts with constitutively active ras (hRasV12) inhibits cell growth and ultimately results in a senescentlike phenotype [441]. Similarly, constitutive ERK activation has an inhibitory effect on cell cycle progression [442,443]. Both the serine/threonine phosphatases and the PTPs are known to be redox-sensitive [82,144,153,156,271,281, 444-449]. The mechanism of redox effects on activity is probably best understood for the PTPs. Without exception, the PTPs contain a highly conserved region of 11 amino acid residues in their catalytic domain; specifi- cally, (Ile/Val)-His-Cys-X-Ala-Gly-X-X-Arg-(Ser/Thr)- Gly, where X is a nonconserved amino acid [17]. Either oxidation or mutation of the cysteine renders these molecules inactive [17,281]. H2O2 is a potent inhibitor of PTPs. As in the case of other oxidants, H2O2 probably oxidizes the thiolate anion at the catalytic site [280]. Because formation of a phosphorylcysteine intermediate seems to be critical to PTP activity [450-452], blocking it through oxidation of the cysteine inactivates the molecules. In many cases, treatment of cells with H2O2 stimulates increases in protein phosphorylation by inhibiting phosphatase-catalyzed removal of phosphate groups. Furthermore, mitogens that increase cellular ox- idant production may stimulate phosphorylation indirectly by decreasing phosphatase activity. Additional mechanisms are involved in stimulation of pathways activated by growth factors that increase oxidant production, however, because there are known instances in which the oxidants they produce have no effect on protein phosphorylation. For example, TGF-b1 stimulates phosphorylation of numerous proteins and has been shown to cause a large increase in H2O2 production; however, its effects on protein phosphorylation are not blocked by catalase [453]. Furthermore, H2O2 is effective in promoting phosphorylation of phospholipase D, the PDGF receptor, and PKC-a even after pretreatment of Swiss 3T3 fibroblasts with orthovanadate to inhibit phosphatases [454]. Thus, although diminished phosphatase activity may partially account for increased phosphorylation in some cases, it cannot totally account for oxidation effects on phosphorylation in every case. SPECIFICITY In general, there is good agreement between studies on redox effects on any given gene; albeit, not all oxidizing or reducing treatments exert equivalent effects. This is clearly demonstrated in studies of pag , which encodes a protein associated with cellular proliferation. Pag protein inhibits the tyrosine kinase activity of the Abelson (abl ) protein by binding to its SH3-binding domain [455]. BSO, menadione, sodium arsenate, and diethyl maleate all stimulate pag expression, but H2O2 does not [269]. Conversely, H2O2 stimulates c-fos expression (Table 1), although 4-hydroynonenal (a product of v-6-polyunsaturated fatty acid peroxidation) not only fails to induce c-fos expression but is actually inhibitory to c-fos induction by EGF and PDGF [185]. Similarly, some oxidants such as diamide decrease hypoxia-induced signals [201], although others such as H2O2 increase them [124]. As might be expected, the effects of any stimu..." provenance.
- _3 value "others clearly are not [19, 43]. In fact, the ROS-induced modulation of gene expression associated with DNA repair can occur in the absence of DNA damage [44]. Some of the effects of UV radiation exposure on various pathways are probably stimulated by DNA damage; however, UVA radiation (320-380 nm), which produces little DNA damage, is effective at inducing expression of collagenase [45], heme oxygenase [46,47], ICAM-1 [48], IL-10 [49], cjun, c-fos, and activation of the JNK MAP kinase pathway [50] and at stimulating increases in ferritin protein [51]. Furthermore, exposure of cells to singlet oxygen generation without light exposure stimulates collagenase production [52]. Redox changes that alter gene expression are not limited to increases in oxidation. Antioxidant treatments can also stimulate increases in the expression of certain genes [53-57]. Although it is possible that autoxidation of antioxidant compounds produces enough ROS to stimulate changes in gene expression through oxidizing rather than reducing mechanisms, this seems improbable. Keogh et al. [55] examined several parameters of oxidation in fibroblasts stimulated to increase c-fos abundance with different antioxidant compounds and found no evidence of increased oxidation; albeit, the antioxidant effects observed were small and were manifested primarily as an increase in GSH concentration. It is also possible that secondary effects of chemical treatments rather than their oxidant/antioxidant properties are responsible for the effects on signal transduction and gene expression. This too seems improbable, because oxidants have been used to block the effects of antioxidant compounds [25,33,58,59] and vice versa [11,26,36,60-77] in a number of independent studies. Choi and Moore [78] examined a series of structural isomers of butylated hydroxytoluene and observed that only those compounds with relatively high antioxidant potential are capable of inducing c-fos." provenance.
- _5 value "activated V12-H-Ras can induce the p21 promoter through the same region of the p21 promoter by a p53-independent mechanism in NIH3T3 cells E2F1 is required for induction of the p21 promoter by activated Ras" provenance.
- _4 value "In 10.5 days old phox2b heterozygous mouse embryos' ventral r4, Efb1 (a general marker of early postmitotic neurons) was expressed in postmitotic neurons, which accumulate in the mantle layer. Whereas in phox2b mutants, Ebf1 expression was abolished in ventral r4." provenance.
- _4 value "Lack of early postmitotic markers in the ventral region of rhombomere 4 in phox2b deficit mice. In ventral r4 of the heterozygous, Math3 was transiently expressed on the cells in the process of emigration from the neuroepithelium and accumulation at the internal margin of the mantle layer. Whereas in the homozygous mutants, the expression of gene was abrogated in the ventral region of r4." provenance.
- _2 value "Progesterone inhibits the proliferation of normal breast epithelial cells in vivo, as well as breast cancer cells in vitro." provenance.
- _3 value "tBH treatment of hRPE cells resulted in increased expression of FasL and Fas. Glutathione and NAC completely abrogated tBH-induced increase in FasL and Fas expression" provenance.
- _4 value "PD 98059 (5 to 50 microM) partially inhibited PAF-induced RANTES production. PD 98059 at that concentration caused a 40% decrease in RANTES production." provenance.
- _4 value "PD 98059 (5 to 50 microM) partially inhibited PAF-induced RANTES production. PD 98059 at that concentration caused a 40% decrease in RANTES production." provenance.
- _5 value "Highly purified ATM phosphorylated PHAS-I, the 32-kDa subunit of RPA, serine 15 of p53, and Chk2 in vitro." provenance.
- _6 value "This study aimed to determine the relative contribution of CDK inhibitors to these events. Following progestin treatment, the majority of cyclin E- and D-CDK complexes were bound to p27(Kip1) and few were bound to p21(Cip1)." provenance.
- _5 value "Modified assertion" provenance.
- _2 value "Butyrate blocked cells mainly in the G(1) phase of the cell cycle, whereas trichostatin A was inhibitory in both G(1) and G(2) phases." provenance.
- _3 value "Our results demonstrate that salicyclic acid, cGMP analog, okadaic acid, IBMX, dipyridamole and glutamate significantly enhance BDNF production in DA neuronal cells." provenance.
- _5 value "synthesis of HSP-72 and -90 was inhibited when cells were treated with the protein kinase A inhibitor, H89" provenance.
- _6 value "FGD1 encodes a guanine nucleotide exchange factor (GEF) that specifically activates the Rho GTPase Cdc42" provenance.
- _4 value "inhibition of PDE4 results in uniquely potent induction of apoptosis" provenance.
- _6 value "ATF1 and CREB can be phosphorylated by Rsk2 which is a protein kinase directly activated by Erk MAP kinase. These results suggest a signaling pathway in which Erk MAP kinase activates the c-fos enhancer by direct phosphorylation of p62TCF and by activation of Rsk related kinases that phosphorylate ATF1 and CREB." provenance.
- _6 value "ATF1 and CREB can be phosphorylated by Rsk2 which is a protein kinase directly activated by Erk MAP kinase. These results suggest a signaling pathway in which Erk MAP kinase activates the c-fos enhancer by direct phosphorylation of p62TCF and by activation of Rsk related kinases that phosphorylate ATF1 and CREB." provenance.
- _6 value "ATF1 and CREB can be phosphorylated by Rsk2 which is a protein kinase directly activated by Erk MAP kinase. These results suggest a signaling pathway in which Erk MAP kinase activates the c-fos enhancer by direct phosphorylation of p62TCF and by activation of Rsk related kinases that phosphorylate ATF1 and CREB." provenance.
- _5 value "We further find that the FAP1 site binds ATF1 and CREB from HeLa nuclear extracts and that the phosphorylation of these factors is induced by TPA. ATF1 and CREB can be phosphorylated by Rsk2(RPS6KA3) which is a protein kinase directly activated by Erk (MAPK1) MAP kinases. These results suggest a signaling pathway in which Erk MAP kinase activates the c-fos enhancer by direct phosphorylation of p62TCF and by activation of Rsk related kinases that phosphorylate ATF1 and CREB." provenance.
- _7 value "When applied locally to a passive cell edge, HA promoted the formation of lamellipodial protrusions in the direction of the stimulus. This process was inhibited by the prior injection of cells with dominant-negative N17Rac recombinant protein or by pretreatment of cells with monoclonal anti-CD44 antibodies, interfering with HA binding, implying the direct involvement of CD44 in signaling to Rac1." provenance.
- _3 value "Spontaneous NO donors, S-nitroso-N-acetylpenicillamine (SNAP) and 3-(2-hydroxy-1-methyl-2-nitrosohydrazino)-N-methyl-1-propanamin e, elicited a dose-dependent increase in AR mRNA to a maximum of 7-fold in 12 h." provenance.
- _3 value "Cells and organs producing PAF in response to exogenous stimulations Neutrophils Human IL-6 Human GM-CSF and zymosan Eosinophils Human IgG, IL-5, PMA Monocytes Human LPS [361] Human HIV infection Peritoneal macrophages Mouse HGF, TNF-a Lung mast cells Human Anti-IgE [363] Bone marrow mast cells Mouse Monoclonal IgE and antigen" provenance.
- _4 value "Mesenteric artery Rat Vasodilation [348]" provenance.
- _6 value "PAFR promoter 2 contained AP-2 and Sp-1 binding sites we demonstrated that PAF activates p44ERK1/p42ERK2 in CHO cells stably expressing PAF receptor" provenance.
- _6 value "PAFR promoter 2 contained AP-2 and Sp-1 binding sites we demonstrated that PAF activates p44ERK1/p42ERK2 in CHO cells stably expressing PAF receptor" provenance.
- _6 value "These results are consistent with our previous data showing that PAF is able to translocate PKCa and PKCe from cytosol to plasma membrane" provenance.
- _4 value "increased vasopermeability observed when PAF is injected intradermally or intravenously" provenance.
- _3 value "# Jubilant: PERP is a direct target of 53, involved in p53-dependent apoptosis. High level PERP expression correlated with the induction of cell death, with 21 percent of cells undergoing apoptosis by 16 hours. Accumulation of high levels of PERP gene expression is dependent on p53, E1A and DNA damage which are all essential for E1A-induced apoptosis in mouse endothelial fibroblasts." provenance.
- _5 value "PKC-theta activation of NF-kappaB is mediated through the selective induction of IKKbeta, while the Cot- and NIK-dependent pathway involves induction of both IKKalpha and IKKbeta." provenance.
- _5 value "PKC-theta activation of NF-kappaB is mediated through the selective induction of IKKbeta, while the Cot- and NIK-dependent pathway involves induction of both IKKalpha and IKKbeta." provenance.
- _5 value "PKC-theta acts directly or indirectly to stimulate phosphorylation of IKKbeta, leading to activation of this enzyme" provenance.
- _5 value "To investigate the regulation of the CCR1 chemokine receptor, a rat basophilic leukemia (RBL-2H3) cell line was modified to stably express epitope-tagged receptor. These cells responded to RANTES (regulated upon activation normal T expressed and secreted), macrophage inflammatory protein-1alpha, and monocyte chemotactic protein-2 to mediate phospholipase C activation, intracellular Ca(2+) mobilization and exocytosis." provenance.
- _3 value "EGR2 knockout mice exhibit defects in hindbrain patterning, peripheral nerve myelination and bone formation" provenance.
- _3 value "loss of EGR4 results in male infertility due to increased germ cell apoptosis and defective spermiogenesis" provenance.
- _5 value "UCP3 gene expression increases in skeletal muscle in response to thyroid hormone administration" provenance.
- _4 value "A deficiency in PPT1 results in a genetic disease, infantile neuronal ceroid lipofuscinosis, associated with massive death of cortical neurons. Overexpressed PPT1 showed the same acidic pH optimum (pH 4.0) as the endogenous enzyme, when assayed with a P0-derived octapeptide substrate, and reduced the growth rate by 30%." provenance.
- _4 value "C2-ceramide-induced membrane association of p21Ras was reduced by 30-50% in PPT1-overexpressing cells compared with control." provenance.
- _5 value "Overexpression of PPT1 inhibited this C2-ceramide- or LY294002-mediated activation of caspase-3 by 50%." provenance.
- _5 value "Stra13 expression is transcriptionally repressed and maintained at a low level in cells through a negative autoregulatory mechanism that is brought about by its interaction with the corepressor histone deacetylase (HDAC1)." provenance.
- _5 value "Expression of BHLHB1 dramatically inhibited E2A-mediated transcription activation in NIH 3T3 fibroblasts and Jurkat T cells." provenance.
- _4 value "We found that overexpression of WT Akt1 promoted insulin-stimulated p70S6 kinase (p70S6K) activity and increased the basal activity of GSK3 beta, but did not promote insulin-stimulated GLUT4 translocation or glucose uptake." provenance.
- _2 value "These observations suggest that overexression of the PDI gene significantly suppresses ischemia-induced apoptosis in the CA1 area of the hippocampus. In summary, we have demonstrated here that PDI is up regulated in response to hypoxia or transient forbrain ischemia in astrocytes" provenance.
- _3 value "We isolated and identified a stress protein that is up-regulated in response to hypoxia in primary-cultured glial cells. Protein-disulfide isomerase (PDI) was up-regulated not only by hypoxia in glia in vitro, but also by transient forebrain ischemia in rats in vivo." provenance.
- _3 value "We isolated and identified a stress protein that is up-regulated in response to hypoxia in primary-cultured glial cells. Protein-disulfide isomerase (PDI) was up-regulated not only by hypoxia in glia in vitro, but also by transient forebrain ischemia in rats in vivo." provenance.
- _3 value "We isolated and identified a stress protein that is up-regulated in response to hypoxia in primary-cultured glial cells. Protein-disulfide isomerase (PDI) was up-regulated not only by hypoxia in glia in vitro, but also by transient forebrain ischemia in rats in vivo." provenance.
- _3 value "trichostatin A (TSA), an inhibitor of histone deacetylases Complex hybridization of cDNA arrays revealed repression of Bcl-xL, CRAB2 and TFIID/TAFII31 as well as induction of p21waf1/cip1, GATA-2, hsp86, ID1, ID2 and ID3 mRNA expression, which could be verified by Northern blotting." provenance.
- _3 value "trichostatin A (TSA), an inhibitor of histone deacetylases Complex hybridization of cDNA arrays revealed repression of Bcl-xL, CRAB2 and TFIID/TAFII31 as well as induction of p21waf1/cip1, GATA-2, hsp86, ID1, ID2 and ID3 mRNA expression, which could be verified by Northern blotting." provenance.
- _3 value "trichostatin A (TSA), an inhibitor of histone deacetylases Complex hybridization of cDNA arrays revealed repression of Bcl-xL, CRAB2 and TFIID/TAFII31 as well as induction of p21waf1/cip1, GATA-2, hsp86, ID1, ID2 and ID3 mRNA expression, which could be verified by Northern blotting." provenance.
- _3 value "trichostatin A (TSA), an inhibitor of histone deacetylases Complex hybridization of cDNA arrays revealed repression of Bcl-xL, CRAB2 and TFIID/TAFII31 as well as induction of p21waf1/cip1, GATA-2, hsp86, ID1, ID2 and ID3 mRNA expression, which could be verified by Northern blotting." provenance.
- _3 value "trichostatin A (TSA), an inhibitor of histone deacetylases Complex hybridization of cDNA arrays revealed repression of Bcl-xL, CRAB2 and TFIID/TAFII31 as well as induction of p21waf1/cip1, GATA-2, hsp86, ID1, ID2 and ID3 mRNA expression, which could be verified by Northern blotting." provenance.
- _3 value "trichostatin A (TSA), an inhibitor of histone deacetylases Complex hybridization of cDNA arrays revealed repression of Bcl-xL, CRAB2 and TFIID/TAFII31 as well as induction of p21waf1/cip1, GATA-2, hsp86, ID1, ID2 and ID3 mRNA expression, which could be verified by Northern blotting." provenance.
- _6 value "demonstrate that the inhibition of the aPKCs or the down-regulation of p62 severely abrogates NF-kappaB activation by IL-1 and TRAF6, suggesting that both proteins are critical intermediaries in this pathway" provenance.
- _6 value "K8 and K18 both bind the cytoplasmic domain of TNFR2 and moderate TNF-induced, Jun NH(2)-terminal kinase (JNK) intracellular signaling and NFkappaB activation." provenance.
- _5 value "K8 and K18 both bind the cytoplasmic domain of TNFR2 and moderate TNF-induced, Jun NH(2)-terminal kinase (JNK) intracellular signaling and NFkappaB activation." provenance.
- _4 value "Inhibition of STAT3 activation by SOCS could be overcome by overexpression of native JAK1 and JAK2." provenance.
- _4 value "Inhibition of STAT3 activation by SOCS could be overcome by overexpression of native JAK1 and JAK2." provenance.
- _6 value "We found that STAT3, but not STAT5, was activated in response to IGF-I in 293T cells cotransfected with IGF-IR and STAT expression vectors. Moreover, tyrosine phosphorylation of STAT3, JAK1, and JAK2 was increased upon IGF-I stimulation of endogenous IGF-IR in 293T cells transfected with the respective STAT or JAK expression vector." provenance.
- _4 value "Here we demonstrate that the stress signaling agents anisomycin, arsenite, and tumor necrosis factor-alpha stimulate the specific enzyme activity of CK2 in the human cervical carcinoma HeLa cells by up to 8-fold, and this could be blocked by the p38 MAP kinase inhibitor SB203580." provenance.
- _5 value "We show that p38alpha MAP kinase, in a phosphorylation-dependent manner, can directly interact with the alpha and beta subunits of CK2 to activate the holoenzyme through what appears to be an allosteric mechanism." provenance.
- _6 value "NADPH stimulated production of H2O2 in a time- and concentration-dependent manner (Fig. 2A)....H2O2 production was significantly inhibited by pretreatment with either catalase or with the NADPH oxidase inhibitor DPI at each concentration of NADPH examined (Fig. 2B). " provenance.
- _2 value "We recently showed that H2O2 stimulates [Ca21]i oscillations in human aortic endothelial cells (HAEC)1 (11)." provenance.
- _4 value "These results demonstrate that C/EBPbeta deletion decreases plasma FFA levels and increases insulin signal transduction specifically in skeletal muscle, and both contribute to increased whole-body insulin sensitivity." provenance.
- _4 value "In addition, we demonstrated that the PAF receptor participates in the signaling pathway, which results in the induction of PAF acetylhydrolase expression in response to endotoxin." provenance.
- _5 value "Additional fragments derived from the promoters of phospholipid transfer protein and hepatic nuclear factor-4 (HNF4) and the apoCIII enhancer that had been shown to bind GST.ZF3-8 in vitro were also used in reporter assays. Transcriptional repression in the presence of ZNF202 was similar to the one observed for the apoE and apoAIV promoters (Table I)" provenance.
- _5 value "Additional fragments derived from the promoters of phospholipid transfer protein and hepatic nuclear factor-4 (HNF4) and the apoCIII enhancer that had been shown to bind GST.ZF3-8 in vitro were also used in reporter assays. Transcriptional repression in the presence of ZNF202 was similar to the one observed for the apoE and apoAIV promoters (Table I)" provenance.
- _5 value "IL-17 activates the transcription factor nuclear factor (NF)-kappaB and c-Jun NH(2)-terminal kinase (JNK)" provenance.
- _5 value "In embryonic fibroblasts (EFs) derived from TRAF6 knockout mice, IL-17 failed to activate the IkappaB kinases (IKKs) and JNK. Consequently, IL-17-induced IL-6 and intercellular adhesion molecule 1 expression in the TRAF6-deficient cells was abolished." provenance.
- _7 value "In embryonic fibroblasts (EFs) derived from TRAF6 knockout mice, IL-17 failed to activate the IkappaB kinases (IKKs) and JNK. Consequently, IL-17-induced IL-6 and intercellular adhesion molecule 1 expression in the TRAF6-deficient cells was abolished." provenance.
- _6 value "phosphorylation of extracellular signal-regulated kinase (ERK), but not of c-Jun NH2-terminal kinase or p38, was induced by cross-linking of Fas" provenance.
- _5 value "Insulin receptor substrates (IRS-1 and -2) are essential for intracellular signaling by insulin and IGF-I, anabolic regulators of bone metabolism." provenance.
- _3 value "osteoblasts from homozygous deficient mice treated with insulin or IGF1 failed to induce tyrosine phosphorylation of cellular proteins and showed reduced proliferation and differentiation" provenance.
- _3 value "p53 induce cell cycle arrest through activation of the cyclin-dependent kinase inhibitor p21(WAF1/Cip1) gene" provenance.
- _9 value "Calreticulin appears to also associate with cytoplasmic domain of integrin alpha7 in a manner highly dependent on the cytosolic Ca(2+) concentration. It appeared that intracellular Ca(2+) release was a prerequisite for Ca(2+) influx and that calreticulin associated with the integrin cytoplasmic domain mediated the coupling of between the Ca(2+) release and Ca(2+) influx." provenance.
- _3 value "Western and Northern blot analysis of macrophage-type inducible NO synthase (iNOS) demonstrated that thapsigargin treatment induces the expression of the iNOS protein and iNOS mRNA." provenance.
- _3 value "# Ariadne: In vitro , bacterially expressed glutathione S -transferase-PASS1 fusion protein bound to hsp27, and hsp27 was co-immunoprecipitated with c-Myc-tagged PASS1 overexpressed in several cell lines. [Binding]" provenance.
- _4 value "The sequences of the other cDNA fragments were identical to those of contrapsin, transketolase, and vanin-3. The latter two were up-regulated, whereas contrapsin was down-regulated in neonatal MT-null mice." provenance.
- _8 value "Using a series of specific small molecule inhibitors, both protein kinase C (PKC) and phosphoinositide-3 kinase (PI-3K) appeared to be required for SDF-1alpha-mediated phosphorylation of focal adhesion proteins and the migration of both CTS and primary marrow CD34(+) cells, whereas the mitogen-activated protein kinases ERK-1 and -2 were not." provenance.
- _8 value "Using a series of specific small molecule inhibitors, both protein kinase C (PKC) and phosphoinositide-3 kinase (PI-3K) appeared to be required for SDF-1alpha-mediated phosphorylation of focal adhesion proteins and the migration of both CTS and primary marrow CD34(+) cells, whereas the mitogen-activated protein kinases ERK-1 and -2 were not." provenance.
- _5 value "Using a series of specific small molecule inhibitors, both protein kinase C (PKC) and phosphoinositide-3 kinase (PI-3K) appeared to be required for SDF-1alpha-mediated phosphorylation of focal adhesion proteins and the migration of both CTS and primary marrow CD34(+) cells, whereas the mitogen-activated protein kinases ERK-1 and -2 were not." provenance.
- _7 value "We observed that several other focal adhesion components, including focal adhesion kinase (FAK) and the adaptor molecules Crk and Crk-L, are phosphorylated on SDF-1alpha stimulation." provenance.
- _7 value "We observed that several other focal adhesion components, including focal adhesion kinase (FAK) and the adaptor molecules Crk and Crk-L, are phosphorylated on SDF-1alpha stimulation." provenance.
- _5 value "We observed that several other focal adhesion components, including focal adhesion kinase (FAK) and the adaptor molecules Crk and Crk-L, are phosphorylated on SDF-1alpha stimulation." provenance.
- _5 value "We observed that several other focal adhesion components, including focal adhesion kinase (FAK) and the adaptor molecules Crk and Crk-L, are phosphorylated on SDF-1alpha stimulation." provenance.
- _5 value "We found that GATA-1 is capable of suppressing the myeloid phenotype without interfering with PU.1 gene expression, but instead was capable of inhibiting the activity of the PU.1 protein in a dose-dependent manner." provenance.
- _6 value "The results presented here delineate a novel signaling pathway from HGF to the GTPase Rap1 which depends on the interaction of the adapter protein CRKL with the exchange factor C3G and could be linked to cell migration." provenance.
- _4 value "Overexpression experiments in REF52 rat fibroblasts showed that BFL-1 conferred increased resistance to apoptosis induced by serum deprivation" provenance.
- _2 value "Overexpression experiments in REF52 rat fibroblasts showed that BFL-1 conferred increased resistance to apoptosis induced by serum deprivation" provenance.
- _4 value "This pathway involves stimulation of phosphatidylinositol 3-kinase (PI3K) binding to insulin receptor substrate-1 and insulin receptor substrate-2, activation of PI3K and protein kinase B (AKT), and PI3K-dependent activation of cyclic nucleotide phosphodiesterase 3B, a cAMP-degrading enzyme." provenance.
- _4 value "IL-4-producing CD30+ clones also produced high levels of IL-10. The production of IL-10 by CD30+ clones was much higher in early than in late Rheumatoid Arthritis." provenance.
- _3 value "For instance, cranial and spinal nerve transection, ischemia, corpus callosum transection, and colchicine treatment increased DINE mRNA expression" provenance.
- _3 value "Similar responses are observed for the serum and glucocorticoid-regulated kinase and channel-inducing factor genes. All four genes show clear and rapid up-regulation of their mRNA levels by aldosterone, which is paralleled by GR-mediated up-regulation of expression." provenance.
- _3 value "evaluated Mat1a and Mat2a methylation in liver and in other tissues, such as kidney Mat1a is hypomethylated in liver and hypermethylated in non-expressing tissues the opposite situation is found in Mat2a histones associated to Mat1a and Mat2a genes showed enhanced levels of acetylation in expressing tissues" provenance.
- _6 value "# Jubilant: It was proved that Reactive oxygen species generation was dependent on P22-PHOX subunit of NADPHoxidase. Transfection with antisense P22-PHOX oligonucleotides reduced the Angiotensin induced Reactive oxygen species induction" provenance.
- _9 value "Ang II also induced the rapid formation of ROS, which could be inhibited by a specific antibody as well as by antisense against the p22phox subunit of the NAD(P)H oxidase. JNK and p38 MAPK, but not ERK, activation was inhibited by an inhibitor of NAD(P)H oxidase. Antisense against p22phox also solely inhibited p38 MAPK but did not affect ERK." provenance.
- _6 value "Ang II also induced the rapid formation of ROS, which could be inhibited by a specific antibody as well as by antisense against the p22phox subunit of the NAD(P)H oxidase. JNK and p38 MAPK, but not ERK, activation was inhibited by an inhibitor of NAD(P)H oxidase. Antisense against p22phox also solely inhibited p38 MAPK but did not affect ERK." provenance.