Effects of 8-(N,N-diethylamino)octyl 3,4,5-trimethoxybenzoate (TMB8) on rat atrial muscle

Northover, B. J.

doi:10.1016/0006-2952(92)90432-i

Cited by 6 publications

(2 citation statements)

References 26 publications

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“…To understand the signaling pathways involved in pORF3-mediated ERK activation, we used inhibitors of various pathways. These included U0126, an inhibitor of the Raf/MEK/ERK pathway (33); LY294002, an inhibitor of the PI3K/Akt pathway (34); calphostin C, an inhibitor of protein kinase C (35); TMB-8, an inhibitor of intracellular calcium mobilization (36); and Genistein, a general protein-tyrosine kinase inhibitor (37). To ensure that the various inhibitors functioned properly, their effects were evaluated as follows (data not shown).…”

Section: Resultsmentioning

confidence: 99%

The Hepatitis E Virus Open Reading Frame 3 Protein Activates ERK through Binding and Inhibition of the MAPK Phosphatase

Kar-Roy

Korkaya

Oberoi

et al. 2004

Journal of Biological Chemistry

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The hepatitis E virus causes acute viral hepatitis endemic in much of the developing world and is a serious public health problem. However, due to the lack of an in vitro culture system or a small animal model, its biology and pathogenesis are poorly understood. We have shown earlier that the ORF3 protein (pORF3) of hepatitis E virus activates ERK, a member of the MAPK superfamily. Here we have explored the mechanism of pORF3-mediated ERK activation and demonstrated it to be independent of the Raf/MEK pathway. Using biochemical assays, yeast two-hybrid analysis, and intracellular fluorescence resonance energy transfer we showed that pORF3 binds Pyst1, a prototypic member of the ERKspecific MAPK phosphatase. The binding regions in the two proteins were mapped to the N terminus of pORF3 and a central portion of Pyst1. Expression of pORF3 protected ERK from the inhibitory effects of ectopically expressed Pyst1. This is the first example of a viral protein regulating ERK activation by inhibition of its cognate dual specificity phosphatase.

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Section: Resultsmentioning

confidence: 99%

The Hepatitis E Virus Open Reading Frame 3 Protein Activates ERK through Binding and Inhibition of the MAPK Phosphatase

Kar-Roy

Korkaya

Oberoi

et al. 2004

Journal of Biological Chemistry

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“…As high concentrations of TMB-8 have several actions, including depression of protein kinase C and tyrosine kinase, 17) the culture was exposed for 30 minutes at a concentration of 1 µM TMB-8 in this study. W-7 has been reported to increase the release from the SR by interfering with the binding between the calmodulin receptor and Ca…”

Section: Vol 44 Nomentioning

confidence: 99%

<b>Norepinephrine-induced Inositol 1,4,5-Trisphosphate Formation in Atrial Myocytes is Regulated by Extracellular Calcium, Protein Kinase C, and Calmodulin</b>

Kudoh

Katagai

et al. 2003

Jpn Heart J

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SUMMARYWe investigated whether alteration of extracellular and intracellular Ca 2+ concentrations, protein kinase C, and calmodulin modulate norepinephrine(NE)-induced inositol 1,4,5-trisphosphate (IP 3 ) formation in neonatal rat atrial myocytes. NE-induced IP 3 production in atrial myocytes was stimulated by elevation of extracellular Ca 2+ in a dosedependent manner. However, TMB-8 (an intracellular calcium antagonist) and A23187 (an intracellular calcium agonist) did not significantly affect NE-induced IP 3 production. PMA (a protein kinase C agonist) significantly decreased and staurosporine (a protein kinase C antagonist) significantly stimulated NE-induced IP 3 production. W7 (a calmodulin antagonist) significantly increased the NE-induced IP 3 . In conclusion, elevation of extracellular Ca 2+ concentrations affects NE-induced IP 3 formation in atrial myocytes. Protein kinase C and calmodulin may control the IP 3 response to NE by a negative feedback mechanism. ( 2) The signal transduction of NE occurs through activation of phospholipase C (PLC), which leads to release of IP 3 . On the other hand, release of IP 3 by NE in atrial cells is also associated with the development of arrhythmias.3) Thus, NE-stimulated IP 3 plays an important role in atrial cells, however, intracellular regulation of NE-stimulated IP 3 formation in atrial myocytes remains unclear.

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Phorbol 12,13-dibutyrate produces negative inotropism and selective antagonism of responses to adrenoceptor agonists in rat atria

Northover

1993

Biochemical Pharmacology

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Effects of 8-(N,N-diethylamino)octyl 3,4,5-trimethoxybenzoate (TMB8) on rat atrial muscle

Cited by 6 publications

References 26 publications

The Hepatitis E Virus Open Reading Frame 3 Protein Activates ERK through Binding and Inhibition of the MAPK Phosphatase

The Hepatitis E Virus Open Reading Frame 3 Protein Activates ERK through Binding and Inhibition of the MAPK Phosphatase

<b>Norepinephrine-induced Inositol 1,4,5-Trisphosphate Formation in Atrial Myocytes is Regulated by Extracellular Calcium, Protein Kinase C, and Calmodulin</b>

Phorbol 12,13-dibutyrate produces negative inotropism and selective antagonism of responses to adrenoceptor agonists in rat atria

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