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  • Subject Name : Biology

Effects of EPAC Inhibition on Isoprenaline and NECA Stimulated P38 Phosphorylation

The cellular response to p38 MAPK activation is difficult to predict because it is dependent on many factors, include the cell type, stage of growth and experimental condition [96]. In addition, EPAC effects each cell differently. It demonstrates the diverse activities of EPAC, a cAMP-activated exchange protein and a different cAMP signalling effector molecule, in controlling apoptosis in each cell. It basically explains the restoration of EPAC with various impacts on apoptosis in neuronal cells and myocytes. To examine effects of EPAC on p38 phosphorylation cellswere pre-incubated for 20 min with the EPAC inhibitor (ESI09, 5 mM), before the addition of either isoprenaline or NECA. The presence of ESI09 began to increase the high level of isoprenaline-stimulated p38 phosphorylation from 10 min, reaching the peak phase at 60 min (Fig 11A, C). In contrast, the presence of ESI09 started to increase the level of NECA-stimulated p38 phosphorylation from 5 min with a gradual decrease from 10 to 45 min, which then increased and reached to peak phase at 60 min (Fig 11B, D).

Effects SRC Inhibition (PP1) on NECA Stimulated P38 Phosphorylation in Arterial Smooth Muscle

PP1(4-Amino-5-(4-methylphenyl)-7-(t-butyl) pyrazolo[3,4-d]- pyrimidine) has been identified as an Src-selective tyrosine kinase inhibitor and has been used extensively to investigate signalling pathways involving Src kinases [84]. Adenosine A2B receptors also have been suggested to influence cell differentiation and proliferation[101],p38. MAPK has been introduced for monitoring cell proliferation, division, motility and survival in a synchronized way. and transmission of a message from a reporter on the cell membrane to the DNA in the nucleus of the cell. In these experiments we examined whether Src inhibition could affect stimulated NECA induced P38 signalling. To examine this possibility cells were pre-incubated for 20 min with the Src kinase inhibitor PP1 (20 µM) before addition NECA (10 µM). PP1 had no effect upon NECA-stimulated p38 phosphorylation (Fig. 9).

Effects MAPK Inhibition on NECA Stimulated ERK Phosphorylation In arterial Smooth Muscle

The extracellular-signal-regulated kinase (ERK) pathway is one of the most important sensing cassettes of the mitogen activated protein kinase (MAPK) signalling pathway. It is also responsible for controlling various cellular processes, such as proliferation, and was the first MAPK to be discovered[28].

The ERK cascade is triggered by a range of epithelial factors, including growth factors, hormones and also cellular pressures, to promote cellular processes, which mostly involve proliferation and differentiation but under certain circumstances. The VSMC of typical cardiovascular threat factors such as hyperlipidaemia, hypertension and obesity has been studied. This indicate the lack of the content and functionality of CREB is a typical pathogenic approach of VSMC to cardiovascular risk factors [1]. It has been studied that a non-classical transcription factor (Ras/MEK1/ERK/RSK) has been revealed from Ang II to NF-κB stimulation, a process by which Ang II induces RSK-mediated p65 phosphorylation to indulge in vascular inflammation. Instead, we discovered a non-classical signalling pathway, Ras/MEK1/ERK/RSK, which triggered NF-κB through p65 phosphorylation, resulting to the development of IL-6 and proposing a framework by which Ang II causes vascular inflammation.

The results obtained from these experiments showed that NECA did not stimulate ERK phosphorylation but PD98059 blocked basal ERK phosphorylation (Fig.10), supporting the correct use of PD98059 in these experiments asan inhibitor of MAP kinase kinases (MAPKK), MEK1 and MEK2[29].

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