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J. Biol. Chem. 275, 9805-9813. Apoptosis signal-regulating kinase 1 (ASK1) induces neuronal differentiation and survival of PC12 cells. 2000

Takeda, K., Hatai, T., Hamazaki, T.S., Nishitoh, H., Saitoh, M., Ichijo, H.

Notes: The MEK Inhibitor U0126 was shown to inhibit MAPK phosphorylation completely and to a greater extent than PD98059. The inactivation had very little effect on neurite outgrowth. MAPK phosphorylation was determined with the Anti-ACTIVE® MAPK pAb by Western blotting. (0297)

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J. Biol. Chem. 275, 37078-85. Circadian activation of bullfrog retinal mitogen-activated protein kinase associates with oscillator function. 2000

Harada, Y., Sanada, K., and Fukada, Y.

Notes: The vertebrate retina retains a circadian oscillator that seems to correspond to an in vivo circadian rhythm in MAPK phosphorylation. Activation of MAPK in bullfrog retinas was monitored by Western blot analysis using the Anti-ACTIVE® MAPK pAb (1:1000 dilution). Proteins were separated by SDS-PAGE, transferred to PVDF  membranes and incubated at 4°C overnight with the Anti-ACTIVE® MAPK pAb. (2400)

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J. Biol. Chem. 275, 2087-2097. Constitutively active mutants of the alpha1a- and the alpha1b-adrenergic receptor subtypes reveal coupling to different signaling pathways and physiological responses in rat cardiac myocytes. 2000

McWhinney, C., Wenham, D., Kanwal, S., Kalman, V., Hansen, C., Robishaw, J.D.

Notes: Rat cardiomyocytes were treated for 5 minutes with phenylephrine and lysates produced. Activated MAPK was detected by western blotting with the Anti-ACTIVE® MAPK pAb. The blots were stripped and reprobed with the Anti-Erk1/2 pAb to determine the total amount of Erk 1 and Erk 2 present in the samples. (0716)

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J. Biol. Chem. 275, 10968-10975. ERK1 and ERK2 activation by chemotactic factors in human eosinophils is interleukin 5-dependent and contributes to leukotriene C(4) biosynthesis. 2000

Bates, M.E., Green, V.L. and Bertics, P.J.

Notes: The MEK Inhibitor U0126 was shown to inhibit MAPK activation in human eosinophils. IL-5-induced leukotriene C4 release was inhibited. The inhibitor was preincubated with the cells for 1 hour prior to addition of IL-5. Activation of MAPK was followed with the Anti-ACTIVE® MAPK pAb via western blotting. (1467)

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J. Cell Biol. 150, 165-175. Glutamate slows axonal transport of neurofilaments in transfected neurons. 2000

Ackerley, S., Grierson, A.J., Brownlees, J., Thornhill, P., Anderton, B.H., Leigh, P.N., Shaw, C.E., and Miller C.C.

Notes: The authors seek to determine the role of glutamate in excitotoxicity and neurofilament accumulation seen in some neurodegenerative diseases. Neurofilament light, middle, and heavy chains were expressed from rat cDNAs cloned into the pCI-neo Mammalian Expression vector in SW-13 cells. Primary rat cortical neurons were transfected with a neurofilament middle chain and green fluorescent fusion protein. SW13 cells and primary rat cortical neurons were transfected with the ProFection® Mammalian Transfection System–Calcium Phosphate. The CytoTox 96® Non-Radioactive Cytotoxicity Assay was used to monitor glutamate toxicity in these cell. To determine the role of the MAPK and JNK signaling pathways,  SW13- cells and primary neuronal cells were immunostained for dually phosphorylated MAPK and JNK using Promega's Anti-ACTIVE® MAPK pAb and Anti-ACTIVE® JNK pAb, respectively. Cells were fixed in 4% paraformaldehyde, permeabilized in 0.1% Triton® X-100 in PBS, blocked with  0.2% Tween® 20 in TBS, and incubated with primary antibodies diluted in blocking solution. Western blot analyses were performed on the primary cortical neurons to quantitate the level of dually phosphorylated MAPK protein  The blots were also probed with a pan MAPK antibody that detects total (active and inactive) MAPK. (2382)

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Brain Res. Dev. Brain Res. 122, 97-109. Inhibition of mitogen-activated protein kinase kinase blocks proliferation of neural progenitor cells. 2000

Learish, R.D., Bruss, M.D., and Haak-Frendscho, M.

Notes: A primary cell line from rat subventricular zone which remains undifferentiated over time was developed as a model for MAPK activation. Cell were stimulated with 20 ng/ml bFGF and 20 ng/ml EGF (Promega) to activate MAPK. The MAPK pathway was inhibited with either U0126 (Promega) or  PD98059. Immunocytochemistry was performed with the Anti-ERK 1/2 pAb (1:100 dilution) to detect both active and inactive forms of MAPK proteins and with the Anti-ACTIVE™ MAPK pAb (1:100 dilution) to specifically detect the dually phosphorylated, active forms of MAPK. Cells were also immunostained with the neuron specific marker Anti-III-tubulin mAb (0.5 µg/ml). Cell proliferation was monitored with the CellTiter 96® AQueous One Solution Cell Proliferation Assay System. Apoptosis within the cell population was monitored using the DeadEnd™ Fluorometric TUNEL System. (2391)

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J. Biol. Chem. 275, 35857-62. Mitogen-activated protein kinase plays an essential role in the erythropoietin-dependent proliferation of CTLL-2 cells. 2000

Sakamoto, H., Kitamura, T., and Yoshimura, A.

Notes: The mechanism of erythropoietin receptor signaling via MAP kinase activation was examined. Mouse IL2-dependent cytotoxic T cell lines were stimulated with 10 units/ml erythropoietin, MAPK was immunoprecipitated, subjected to SDS-PAGE, and transferred onto PVDF membranes. The dually phosphorylated forms of MAPK were detected by Western blot using the Anti-ACTIVE® MAPK pAb antibody. (2396)

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Proc. Natl. Acad. Sci. USA 97(20), 10832-10837. Modulation of Akt kinase activity by binding to Hsp90 2000

Sato, S., Fujita, N., and Tsuruo, T.

Notes: Expression of a truncated Akt (1-309) caused dephosphorylation of normal Akt and activation of caspases as well as cleavage of PARP. The cleavage of PARP was followed by western blotting with the Anti-PARP p85 Fragment pAb from human 293T cell extracts. Etoposide was used for maximal induction of caspase activity in cell expressing the mutant Akt. A caspase inhibitor blocked the cleavage of PARP. The truncated Akt function by preventing the interaction of Akt with Hsp90. The truncation mutant did not affect the ability of heat shock to induce MAPK phosphorylation as determined in western blots of the human 293T cell extracts with the Anti-ACTIVE® MAPK pAb. (0047)

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J. Biol. Chem. 275, 8600-8609.. Oxidative stress disrupts glucocorticoid hormone-dependent transcription of the amiloride-sensitive epithelial sodium channel alpha-subunit in lung epithelial cells through ERK-dependnent and thioredoxin-sensitive pathways. 2000

Wang, H.-C. , Zentner, M.D., Deng, H.-T., Kim, K.-J., Wu, R., Yang, P.-C., Ann, D.K.

Notes: Addition of exogenous H2O2 to cultured A549 cells causes a rapid increase in activated Erk as judged by the Anti-ACTIVE® MAPK pAb via Western blotting. There is an inhibition of transcriptional activation of the amiloride-sensitive epithelial sodium channel α-subunit. The inhibition is reversed by 50µM U0126 MEK Inhibitor treatment 20 minutes prior to addition of H2O2 . Reporters were used for measurement of transcriptional activity and were produced in the pGL2-Promoter Vector. The reporter vectors were cotransfected into the A549 cells with the pRL-TK Vector at a 12:1 ratio. The luciferase activities were measured with the Dual-Luciferase® Reporter Assay System. Transfections were accomplished with the ProFection® Mammalian Transfection System-DEAE-Dextran. (0200)

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J. Biol. Chem. 275, 11333-11340. Phosphorylation of paxillin via the ERK mitogen-activated protein kinase cascade in EL4 thymoma cells. 2000

Ku, H., Meier, K.E.

Notes: The MEK Inhibitor U0126 blocked both PMA-stimulated MAPK phosphorylation and paxillin phosphorylation in primary mouse splenocytes and thymocytes. MAPK phosphorylation was judged by immunoblotting extracts with the Anti-ACTIVE® MAPK pAb, Rabbit, (pTEpY). The MEK Inhibitor U0126 was more effective than PD98059. (0853)

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Mol. Biol. Cell 11, 3751-3763. Sequential activation of ERK and repression of JNK by scatter factor/hepatocyte growth factor in madin-darby canine kidney epithelial cells. 2000

Paumelle, R., Tulasne, D., Leroy, C., Coll, J., Vandenbunder, B., and Fafeur, V.

Notes: The authors characterize the cell signaling pathways triggered by the multifunctional growth factor scatter factor/hepatocyte growth factor. In Madin-Darby Canine Kidney epithelial cells SF/HGF induces phosphorylation of MAPK while stimulating weakly and then repressing phosphorylation of JNK. The Anti-ACTIVE® MAPK pAb and Anti-ACTIVE® JNKpAb were used to quantitate the level of activation of the MAPK and JNK signaling pathways by Western blot analysis. (2379)

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Nat. Neurosci. 3, 323-29. Synapsins as mediators of BDNF-enhanced neurotransmitter release. 2000

Jovanovic, J.N., Czernik, A.J., Fienberg, A.A., Greengard, P., and Sihra, T.S.

Notes: Treatment of  brain-derived neurotrophic factor increased MAPK-dependent synapsin I phosphorylation in rat cerebral cortex synaptosomal preparations. MAPK activity was determined by Western blot analysis using the Anti-ACTIVE® MAPK (1:10,000 dilution) pAb to detect the dually phosphorylated forms of MAPK. CaM kinase II activity was assayed by Western blot analysis with the Anti-ACTIVE® CaM KII pAb, Rabbit, (pT286) (1:2500 dilution). The Anti-Mouse IgG (H+L), AP Conjugate (1:1000 dilution) was used as a secondary antibody in Western blot analysis to detect TrkB expression. (2393)

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J. Am. Soc. Nephrol. 11, 1607-19. The decorin high glucose response element and mechanism of its activation in human mesangial cells. 2000

Wahab, N.A., Parker, S., Sraer, J.D., and Mason, R.M.

Notes: Hyperglycemia seems to be involved in the pathogenesis of diabetic nephropathy. The authors identify regulatory promoter elements involved in gene regulation under hyperglycemic conditions and characterize some of the signaling pathways involved. Immunocytochemistry of human mesangial cells grown under normal and high glucose conditions was performed with the Anti-ACTIVE® MAPK pAb to localize dually phosphorylated, active MAPK protein. Cells were fixed in 3.7% paraformaldehyde, permeabilized with 0.1% Triton® X-100 and stained with the Anti-ACTIVE® MAPK pAb overnight at 4°C, or for 1 hour at 37°C. Gel shift assays were performed to identify a regulatory element which appears to be responsive to glucose concentration. Gel shift assays were carried out using Promega's Gel Shift Assay System. (2394)

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J. Biol. Chem. 275, 18810-18817. The inhibition of interleukin-6-dependent STAT activation by mitogen-activated protein kinases depends on tyrosine 759 in the cytoplasmic tail of glycoprotein 130. 2000

Terstegen, L., Gatsios, P., Bode, J.G., Schaper, F., Heinrich, P.C., and Graeve, L.

Notes: The effect of suppressor of cytokine signaling (SOCS) expression on the Jak/STAT, MAPK, JNK, and p38 signaling pathways was examined in HepG2, Cos-7, and NIH 3T3 cells. Both PMA and bFGF (Promega) resulted in a rapid upregulation of SOCS-3 expression.  MAPK, JNK, and p38 activation was monitored by Western blot analysis using the Anti-ACTIVE® MAPK Anti-ACTIVE® JNK pAb, and the Anti-ACTIVE® p38 pAb. Total levels of active and inactive MAPK protein was determined using the Anti-ERK 1/2 pAb, Rabbit. (2380)

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Neurosci. Lett. 282, 89-92. The mitogen-activated protein kinase cascade mediates neurotrophic effect of epidermal growth factor in cultured rat hippocampal neurons 2000

Abe, K. and Saito, H.

Notes: Rat hippocampal neurons were cultured with EGF for 5 minutes to 12 hours and monitored for activation of Erk 1 and 2 by Western blotting with the Anti-ACTIVE® MAPK pAb. Maximum stimulation occurred at about 1 hour with 5ng/ml EGF. The activation could be blocked with EGF receptor tyrosine kinase inhibitors and MEK inhibitors. Total Erk 1 and 2 present in the samples were detected with the Anti-ERK 1/2 pAb which recognized Erk 1 and 2 no matter what the phosphorylation state. (2225)

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Neurosci. Res. 36, 251-257. The p44/42 mitogen-activated protein kinase cascade is involved in the induction and maintenance of astrocyte stellation mediated by protein kinase C. 2000

Abe, K. and Saito, H.

Notes: Both PMA and dibutryl cAMP (dBcAMP) are known to cause differentiation of cultured astrocytes into process-bearing stellate cells. The U0126 MEK Inhibitor blocks the formation of stellate cells by PMA but not by dBcAMP. The cells treated with dBcAMP had the same levels of Erk 1/2 as the PMA treated cells throughout the experiment but only PMA treated cells demonstrated activation of Erk 1/2 by dual phosphorylation. Thus, it is reasonable that the U0126 MEK Inhibitor could inhibit PMA-induced stellate formation. The level of total Erk 1 and 2 was determined by Western blotting with the Anti-Erk 1/2 pAb and the level of activated Erk 1/2 was determined with the Anti-ACTIVE® MAPK pAb. Cells were treated for 20min with 10µM U0126 Inhibitor and treated with the stimulator for up to 6hr. The U0126 Inhibitor treatment blocked the stellate formation by PMA throughout the experiment. Titration of the U0126 Inhibitor was performed with 0.01 to 10µM and was compared to the PD98059 inhibitor. U0126 Inhibitor was completely inhibitory at 1 and 10µM and at 0.1µM was as inhibitory as 30µM PD98059. Protein kinase C inhibitors were also able to mimic the effect of the U0126 Inhibitor as demonstrated by the blockage of Erk 1/2 phosphorylation and stellate formation. The U0126 Inhibitor was also able to reverse the morphology of the stellate cells back to that of polygonal, undifferentiated cells. The reversal of morphology was also supported by the loss of activated Erk 1 and 2 as judged by Western blotting with the Anti-ACTIVE® MAPK pAb. (2050)

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J. Biol. Chem. 275, 5124-5130. The role of disulfide-linked dimerization in interleukin-3 receptor signaling and biological activity. 2000

Le, F., Stomski, F., Woodcock, J.M., Lopez, A.F., Gonda, T.J.

Notes: The CellTiter 96® Non-Radioactive Cell Proliferation Assay (MTT) was used to determine the effects of the expression of wildtype IL-3 receptor α and wildtype or mutant β. The proliferation of the transfected CTL-EN (an IL-2-dependent CTLL-2 cell derivative) was measured after 72 hours in the presence of IL-3. Both mutants and wildtype receptors activated Erk 1 & 2 as judged by Western blotting of cell extracts with the Anti-ACTIVE® MAPK pAb. (0849)

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J. Neurosci. 19, 664-673. A role for MAPK/ERK in sympathetic neuron survival: protection against a p53-dependent, JNK-independent induction of apoptosis by cytosine arabinoside. 1999

Anderson, C.N.G. and Tolkovsky, A.M.

Notes: The authors used Promega's Anti-ACTIVE® MAPK pAb for Western blot analysis of rat superior cervical ganglion neuronal cell extracts. The primary cultured superior cervical ganglion neuronal cells were taken from wildtype and p53 knockout rats. (1512)

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FASEB J. 13, 31-38. A Sos-derived peptidimer blocks the Ras signaling pathway by binding both Grb2 SH3 domains and displays antiproliferative activity. 1999

Cussac, D., Vidal, M., Leprince, C., Liu, W.Q., Cornille, F., Tiraboschi, G., Roques, B.P. and Garbay, C.

Notes: In this paper, Promega's Anti-ACTIVE® MAPK pAb was used to study the effect of a Sos-derived peptidimer on activation of the MAPK signalling pathway.  The antibody was used in Western blots of PC12 cell extracts to detect activated MAPK. (1290)

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Eur. J. Neurosci. 11, 2073-2082. Activation of the extracellular signal-regulated kinase 2 by metabotropic glutamate receptors. 1999

Ferrauti, F., Baldani-Guerra, B., Corsi, M., Nakanishi, S., Corti, C.

Notes: The Anti-ACTIVE® MAPK pAb was used to detect activated ERK1 and ERK2 in CHO cells transfected with the metabotropic glutamate receptor. The cells were stimulated with TPA, then the specific ERK was immunoprecipitated with a polyclonal antibody. The immunoprecipitate was probed for dual phosphorylation by Western blotting. (1198)

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Science 286, 1374-1377. Defective thymocyte maturation in p44 MAP kinase (Erk1) knockout mice. 1999

Pages, G., Guerin, S., Grall, D., Bonino, F., Smith, A., Anjuere, F., Auberger, P. and Pouyssegur, J.

Notes: Mouse embryo fibroblasts from both wildtype and Erk1 knockout mice were stimulated with serum. Erk1 and Erk2 from wildtype mouse embryo fibroblasts were shown to be phosphorylated using the Anti-ACTIVE® MAPK pAb in a Western blot analysis. In embryo fibroblasts from knockout mice, only Erk2 as phosphorylated. Total Erk1 and Erk2 proteins were detected with the Anti-ERK 1/2 pAb.  (0577)

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Mol. Cell. Biol. 19, 136-146.. Glutamate induces phosphorylation of Elk-1 and cREB, along with c-fos activation, via an extracellular signal-regulated kinase-dependent pathway in brain slices. 1999

Vanhoutte, P., Barnier, J.-V., Guibert, B., Pages, C., Besson, M.-J., Hipskind, R.A., Caboche, J.

Notes: The Anti-ACTIVE® MAPK pAb and Anti-ACTIVE® JNK pAb were used to examine whether or not the kinases were activated by glutamate in rat striatal slices via Western blotting. Both were activated and at least MAPK activation could be blocked with MEK inhibitors. CaM KII was also shown to be activated by the glutamate treatment as judged by Western blotting with the Anti-ACTIVE® CaM KII pAb. Interestingly, inhibition of CaM KII activation by the specific inhibitor KN62 also decreased activation of Erk 1 and 2 above control levels in the presence of glutamate. This suggests that CaM KII plays a role in calcium signaling to activate Erk's in this tissue. (0218)

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J. Neurosci. 19, 928-939. Identification of microglial signal transduction pathways mediating a neurotoxic response to amyloidogenic fragments of beta-amyloid and prion proteins. 1999

Combs, C. K. , Johnson, D. E. , Cannady, S. B. , Lehman, T. M. , Landreth, G. E.

Notes: The Anti-ACTIVE® MAPK pAb was used for western analysis of a THP-1 monocytic cell line that had been stimulated with either fibrillar beta amyloid or prion peptides. (1321)

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J. Biol. Chem. 274, 6168-6174. Nuclear localization of mitogen-activated protein kinase kinase 1 (MKK1) is promoted by serum stimulation and G2-M progression. Requirement for phosphorylation at the activation lip and signaling downstream of MKK. 1999

Tolwinski, N.S., Shapiro, P.S., Goueli, S., and Ahn, N.G.

Notes: Authors used the Anti-ERK 1/2 pAb and MEK Inhibitor U0126 to study localization of Erk1 and Erk2 in NIH 3T3 cells.  The Anti-ERK 1/2 pAb was used on Western blots to analyze total Erk1 and Erk2 present in various stimulated cell extracts.  Researchers also used the MEK Inhibitor U0126 demonstrate a direct inhibition of MEK.  Phospho-Erks from MEK Inhibitor U0126 studies were examined on Western blots. (0274)

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J. Biol. Chem. 274, 37329-37334. Spontaneous neutrophil apoptosis involves caspase-3-mediated activation of protein kinase C-delta. 1999

Pongracz, J., Webb, P., Wang, K., Deacon, E., Lunn, O.J. and Lord, J.M.

Notes: Spontaneously apoptotic human peripheral blood neutrophil extracts were assayed by Western blot for the cleavage of protein kinase C-isoforms. Cleavage was inhibited by addition of the caspase-3 inhibitor DEVD-FMK. The CaspACE™ Assay System, Fluorometric, was used to confirm that caspase-3 activity was present in these extracts. Researchers verified the results by inhibiting Caspase 3 with the DEVD-FMK inhibitor. The Anti-ACTIVE® MAPK pAb was used in a Western blot assay to demonstrate that neutrophil apoptosis did not require activation of Erk1 or Erk2. Total Erk1 and Erk2 levels were also assessed using the Anti-ERK 1/2 pAb. (0540)

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