Multiple intracellular pathways induce expression of a zinc‐finger encoding gene (EGR1): Relationship to activation of the Na/H exchanger

Jamieson, Gordon A.; Mayforth, Ruth D.; Villereal, Mitchel L.; Sukhatme, Vikas P.

doi:10.1002/jcp.1041390207

Cited by 32 publications

(14 citation statements)

References 35 publications

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“…PKC-dependent models of Egr-1 upregulation in fibroblasts have included induction by TPA (36), IGF-I (37), and inflammatory cytokines (38), but not by serum (36,37), EGF (36), v-src (39), activated v-Fps (40), or heavy metals (41). Additional examples of PKCdependence include induction of Egr-1 by lipopolysaccharide (but not by granulocyte-macrophage colony stimulating factor) in peritoneal macrophages (42, 43); induction by plateletderived growth factor or 5HT (but not by AVP) in glomerular mesangial cells (44); induction by X-irradiation in epithelial tumors (45); and induction by anti-receptor antibody in B lymphocytes (46).…”

Section: Discussionmentioning

confidence: 99%

Urea signaling in cultured murine inner medullary collecting duct (mIMCD3) cells involves protein kinase C, inositol 1,4,5-trisphosphate (IP3), and a putative receptor tyrosine kinase.

1996

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Urea, in concentrations unique to the renal medulla, increases transcription and protein expression of several immediate-early genes (IEGs) including the zinc finger-containing transcription factor, Egr-1 . In the present study, the proximal 1.2 kb of the murine Egr-1 5 Ј -flanking sequence conferred urea-responsiveness to a heterologous luciferase reporter gene when transiently transfected into renal medullary mIMCD3 cells, and this effect was comparable with that of the extremely potent immediate-early gene inducer, O -tetradecanoylphorbol 13-acetate (TPA). Urea inducibility of Egr-1 expression was protein kinase C (PKC)-dependent because staurosporine and calphostin C abrogated the urea effect, and down-regulation of PKC through chronic TPA treatment inhibited both urea-inducible Egr-1 protein expression and gene transcription. In addition, hyperosmotic urea increased inositol 1,4,5-trisphosphate (IP 3 ) release from mIMCD3 cells and induced tyrosine phosphorylation of the receptor tyrosine kinase-specific phospholipase C (PLC) isoform, PLC-␥ . Importantly, urea-inducible Egr-1 expression was strongly genistein-sensitive, to a much greater extent than the comparable TPA-inducible Egr-1 expression. These data suggest that urea-inducible Egr-1 expression is a consequence of sequential PLC-␥ activation, IP 3 release, and PKC activation. Urea-inducible PLC-␥ activation, in conjunction with the genistein-sensitivity of ureainducible Egr-1 expression suggest the possibility of a cell surface or cytoplasmic urea-sensing receptor tyrosine kinase. (

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Section: Discussionmentioning

confidence: 99%

Urea signaling in cultured murine inner medullary collecting duct (mIMCD3) cells involves protein kinase C, inositol 1,4,5-trisphosphate (IP3), and a putative receptor tyrosine kinase.

1996

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“…In vivo stimulation, such as chemically and electrically induced seizures, triggers both the generation of PAF (20) and the accumulation of c-fos mRNA (21)(22)(23)(24) and zif-268 mRNA (25,26) in the brain. Intracerebroventricular injection of BN-50730 prior to stimulation partially inhibits the c-fos message accumulation and markedly inhibits zif-268 expression (19), suggesting that PAF is an intracellular messenger that activates gene expression through a BN-50730 sensitive intracellular PAF receptor.…”

mentioning

confidence: 99%

“…The TISJO/PGS-2 primary response gene was identified as one of several phorbol ester (28) and serum (29) inducible genes in NIH 3T3 cells, and as a v-src-inducible gene in chicken embryo fibroblasts (30 [20][21][22][23][24][25][26][27][28][29][30] pl of the supernatant after normalization of -3-galactosidase, was used in each assay and was mixed with 70-80 /4 of 2x ALL buffer. The reaction was initiated by the injection of 100 gl of 1 mM luciferin and the relative light units were determined by using an ALL luminometer recording over a 20-sec interval.…”

mentioning

confidence: 99%

Platelet-activating factor and retinoic acid synergistically activate the inducible prostaglandin synthase gene.

Bazán

Fletcher

Herschman

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

139

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Platelet-activating factor (PAF), a potent lipid mediator generated in cell injury and in the inflammatory and immune responses, promotes transcriptional activation of several primary response genes. TIS10/PGS-2 is a primary response gene encoding the inducible form of prostaglandin synthase. The inductive effects of PAF and retinoic acid (RA), alone and in combination, were studied with the regulatory region of TIS10/PGS-2 transfected into an exponentially growing glioblastoma-neuroblastoma NG108-15 hybrid in the human SH-SY5Y neuroblastoma or in the NIH 3T3 cell. RA alone exhibited only a small inductive effect. However, in the presence of RA (100 nM), a PAF-dependent (1-50 nM) synergistic activation of luciferase reporter constructs driven by regulatory regions of the TIS10/PGS-2 gene was found. The hetrazepine BN-50730, an antagonist selective for intracellular PAF binding sites, inhibited PAF and RA induction of luciferase from the TIS10/PGS-2 promoter. Thus, the intracellular PAF binding site is involved in TIS10/PGS-2 expression. Induction is rapid, suggesting that the combination of PAF and RA activates a preexisting latent transcription factor(s). Deletion studies restrict the major PAF and RA cis-acting response element of the TIS10/PGS-2 gene to a 70-nucleotide sequence as an intracellular inducer of TIS10/PGS-2 expression. The synergistic effect of RA and PAF represents an unusual convergence of nuclear signaling pathways by which, through the modulation of preexisting transcription factors, specific gene expression can be upregulated. PAF-dependent induction of TIS10/PGS-2 expression may play a role in cell injury, differentiation, inflammation, and immune responses.

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“…The biochemical processes that precede immediate early gene induction after mitogenic stimulation include signal transduction via kinase activation (31,32). Protein kinase C (PKC)-dependent and -independent pathways participate in EGRI gene induction by serum and growth factors (33). Prolonged exposure to phorbol 12-myristate 13-acetate ("12-O-tetradecanoylphorbol 13-acetate," TPA) results in downregulation of PKC activity (31,32).…”

mentioning

confidence: 99%

Protein kinase C mediates x-ray inducibility of nuclear signal transducers EGR1 and JUN.

Hallahan

Sukhatme

Sherman

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

233

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The cellular response to ionizing radiation includes growth arrest and DNA repair followed by proliferation. Induction of immediate early response genes may participate in signal transduction preceding these phenotypic responses. We analyzed mRNA expression for different classes of immediate early genes (JUN, EGRI, and FOS) after cellular x-irradiation. Increased expression ofthe EGRI andJUN genes was observed within 0.5-3 hr following x-ray exposure. Preincubation with cycloheximide was associated with superinduction of JUN and EGRI in x-irradiated cells. Inhibition of protein kinase C activity by prolonged stimulation with phorbol 12-myristate 13-acetate or the protein kinase inhibitor H7 prior to irradiation attenuated the increase in EGRI and JUN transcripts. FOS expression was not coregulated with that of EGRI following x-irradiation, suggesting a distinct regulatory pathway of this gene as compared with its regulation following serum and phorbol ester. These data implicate the EGR1 and JUN proteins as signal transducers during the cellular response to radiation injury and suggest that this effect is mediated in part by a protein kinase C-dependent pathway.Exposure to ionizing radiation results in pleiotropic biological responses such as cell cycle-specific growth arrest and repair of damaged DNA. Proliferation subsequent to irradiation results in repopulation of injured tissues and tumors (1, 2). In addition, certain cells produce growth factors or cytokines in response to x-rays (3, 4). To effect these delayed responses to injury, x-rays may induce nuclear signaltransducer genes whose products couple early biochemical second-messenger signals to long-term phenotypic changes. Several of these genes encode transcription factors that initiate a cascade of molecular events. Immediate early response genes that encode transcription factors include the JUN family (JUN, JUNB, and JUND; refs. 5-9), the EGR family (EGRI,and 4;, and the FOS family (FOS, FRAI, and FOSB) (13-16). JUN tTo whom reprint requests should be addressed. 2156The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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Multiple intracellular pathways induce expression of a zinc‐finger encoding gene (EGR1): Relationship to activation of the Na/H exchanger

Cited by 32 publications

References 35 publications

Urea signaling in cultured murine inner medullary collecting duct (mIMCD3) cells involves protein kinase C, inositol 1,4,5-trisphosphate (IP3), and a putative receptor tyrosine kinase.

Urea signaling in cultured murine inner medullary collecting duct (mIMCD3) cells involves protein kinase C, inositol 1,4,5-trisphosphate (IP3), and a putative receptor tyrosine kinase.

Platelet-activating factor and retinoic acid synergistically activate the inducible prostaglandin synthase gene.

Protein kinase C mediates x-ray inducibility of nuclear signal transducers EGR1 and JUN.

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