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P38 MAPK mediates myocardial proinflammatory cytokine production and endotoxin-induced contractile suppression
Meijing Wang1, Rajakumar Sankula, Ben M Tsai
1Department of Surgery, Section of Cardiothoracic Surgery, Indiana Center for Vascular Biology and Medicine, Indiana University Medical Center, Indianapolis, Indiana 46202, USA.
Abstract:
Cardiac myocytes are capable of synthesizing tumor necrosis factor alpha (TNF-alpha), interleukin-1, and interleukin-6 (IL-1 and IL-6). p38 mitogen-activated protein kinase (MAPK) has been implicated in oxidant-stress-induced myocardial TNF-alpha production; however, the extent to which this kinase contributes to endotoxin-induced contractile dysfunction, as well as TNF-alpha, IL-1alpha, IL-1beta, and IL-6 production, in a bloodless model of endotoxin-induced myocardial dysfunction is unknown. Isolated rat hearts were perfused (Langendorff), and myocardial contractile function continuously recorded, during direct antegrade endotoxin infusion, with and without prior p38 MAPK inhibition. Ventricular p38 MAPK activation (phospho-p38 MAPK Western), cytokine mRNA (RT-PCR), and protein (ELISA) were determined. Endotoxin resulted in progressive decline in left ventricular developed pressure and coronary flow that was attenuated with prior p38 MAPK inhibition (SB 203580). p38 MAPK inhibition significantly decreased endotoxin-induced cardiac TNF-alpha, IL-1alpha, IL-1beta, and IL-6 mRNA levels. To determine the relative effect of TNF-alpha in inducing IL-1alpha, IL-1beta, and IL-6 production, TNF-alpha was sequestered during endotoxin infusion, and TNF-alpha, IL-1beta, and IL-6 protein levels were measured. Interestingly, TNF-alpha sequestration alone significantly decreased myocardial IL-1beta and IL-6 production. We conclude that p38 MAPK is involved in endotoxin-induced myocardial contractile dysfunction and myocardial TNF-alpha production; however, p38 MAPK's involvement in IL-1 and IL-6 production may be indirectly mediated by TNF-alpha.
Insights
p38 mitogen-activated protein kinase (MAPK) inhibition attenuated endotoxin-induced heart dysfunction and cytokine production. Tumor necrosis factor alpha (TNF-alpha) plays a key role in mediating these effects, particularly for IL-1 and IL-6.
Area of Science:
- Cardiovascular Physiology
- Molecular Cardiology
- Inflammation Research
Background:
- Cardiac myocytes produce pro-inflammatory cytokines like TNF-alpha, IL-1, and IL-6.
- p38 MAPK is linked to oxidant-stress-induced TNF-alpha production in the heart.
- The role of p38 MAPK in endotoxin-induced myocardial dysfunction and cytokine release remains unclear.
Purpose of the Study:
- To investigate the contribution of p38 MAPK to endotoxin-induced myocardial contractile dysfunction.
- To determine the role of p38 MAPK in the production of TNF-alpha, IL-1alpha, IL-1beta, and IL-6 in a bloodless endotoxin model.
- To elucidate the relationship between TNF-alpha and other cytokine productions during endotoxin challenge.
Main Methods:
- Isolated rat hearts were perfused using the Langendorff method.
- Myocardial contractile function was continuously monitored during endotoxin infusion.
- p38 MAPK activation, cytokine mRNA, and protein levels were assessed with and without p38 MAPK inhibition (SB 203580).
- TNF-alpha sequestration was used to determine its role in mediating other cytokine production.
Main Results:
- Endotoxin infusion progressively reduced left ventricular developed pressure and coronary flow.
- Prior p38 MAPK inhibition significantly attenuated these declines.
- p38 MAPK inhibition markedly decreased endotoxin-induced mRNA levels for TNF-alpha, IL-1alpha, IL-1beta, and IL-6.
- TNF-alpha sequestration alone reduced myocardial IL-1beta and IL-6 protein levels.
Conclusions:
- p38 MAPK activation is critical for endotoxin-induced myocardial contractile dysfunction and TNF-alpha production.
- While p38 MAPK influences IL-1 and IL-6 production, this effect appears to be largely mediated by TNF-alpha.
- Targeting p38 MAPK may offer a therapeutic strategy for endotoxin-induced cardiac dysfunction.
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