Adrenomedullin Increases AP-1 Expression in Rat Mesangial Cells via Activation of Protein Kinase-A and p38 MAPK

2003 ◽  
Vol 13 (6) ◽  
pp. 367-374 ◽  
Author(s):  
Narayanan Parameswaran ◽  
Carolyn Hall ◽  
Laura McCabe ◽  
William Spielman
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
P38 Mapk ◽  
Mesangial Cells ◽  
Kinase A

scholarly journals Adenosine pretreatment attenuates angiotensin II-mediated p38 MAPK activation in a protein kinase A dependent manner

2010 ◽  
Vol 4 (5) ◽  
pp. 721-729
Author(s):  
Hamid Yaghooti ◽  
Mohsen Firoozrai ◽  
Soudabeh Fallah ◽  
Mohammad Reza Khorramizadeh
Keyword(s):  
Angiotensin Ii ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
P38 Mapk ◽  
Inflammatory Mediators ◽  
Endothelial Permeability ◽  
Renin Angiotensin System ◽  
Inhibitory Effect ◽  
Dependent Manner ◽  
Kinase A

Abstract Background: Adenosine is known as a protective and anti-inflammatory nucleoside. Angiotensin II is the main hormone of the renin-angiotensin system. It is associated with endothelial permeability, recruitment, and activation of the immune cells through induction of inflammatory mediators. Matrix metalloproteinase-9 (MMP-9) plays an important role in inflammatory processes mediated by macrophages. Objectives: Investigate whether adenosine pretreatment modulates angiotensin II-induced MMP-9 expression and activation of signaling molecules. Methods: Human monocytic U-937 cells were treated with either adenosine or angiotensin II alone or angiotensin II following a pretreatment with adenosine. Supernatants were analyzed for MMP-9 activity by zymography method. MMP-9 gene expression was analyzed using real-time PCR. Activation of inflammatory mediators IκB-α, NF-κB, JNK, p38 MAPK, and STAT3 were analyzed by a multi-target ELISA kit. Association of Protein kinase A (PKA) in adenosine effects was studied by pre-incubation with H89, a selective PKA inhibitor. Results: Treatment of the cells with angiotensin II significantly increased MMP-9 production (p <0.05). Adenosine pretreatment did not attenuate this angiotensin II effect. Angiotensin II treatment induced NF-κB, JNK and p38 activation. Pretreatment with adenosine prior to angiotensin II stimulation showed a 40% inhibitory effect on p38 induction (p <0.05). This effect was reversed by PKA inhibition. Conclusion: The present data confirmed that monocytic MMP-9 was a target gene for angiotensin II. Adenosine pretreatment did not inhibit MMP-9 increase in response to angiotensin II. However, it showed a potential inhibitory effect on angiotensin II inflammatory signaling.

Cytokines induce protein kinase A-mediated signalling by a redox-dependent mechanism in rat renal mesangial cells

2015 ◽  
Vol 93 (3) ◽  
pp. 362-369 ◽  
Author(s):  
Karl-Friedrich Beck ◽  
Johannes Euler ◽  
Florian Eisel ◽  
Martina Beck ◽  
Yvette Köhler ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Mesangial Cells ◽  
Kinase A ◽  
Dependent Mechanism

scholarly journals Catecholamine activation of p38 MAPK in S49 T lymphosarcoma cells is dependent on Protein Kinase A

2008 ◽  
Vol 22 (S1) ◽  
Author(s):  
Melissa Dawn LaJevic ◽  
Samia Suleiman ◽  
Rhonna L. Cohen ◽  
Donald A. Chambers
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
P38 Mapk ◽  
Kinase A

scholarly journals Phosphorylation of cAMP-specific PDE4A5 (phosphodiesterase-4A5) by MK2 (MAPKAPK2) attenuates its activation through protein kinase A phosphorylation

2011 ◽  
Vol 435 (3) ◽  
pp. 755-769 ◽  
Author(s):  
Kirsty F. MacKenzie ◽  
Derek A. Wallace ◽  
Elaine V. Hill ◽  
Diana F. Anthony ◽  
David J. P. Henderson ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
P38 Mapk ◽  
Stress Responses ◽  
Mammalian Cells ◽  
Signal Transduction Pathway ◽  
Mitogen Activated Protein Kinase ◽  
Intracellular Camp ◽  
Camp Accumulation ◽  
Kinase A

cAMP-specific PDE (phosphodiesterase) 4 isoforms underpin compartmentalized cAMP signalling in mammalian cells through targeting to specific signalling complexes. Their importance is apparent as PDE4 selective inhibitors exert profound anti-inflammatory effects and act as cognitive enhancers. The p38 MAPK (mitogen-activated protein kinase) signalling cascade is a key signal transduction pathway involved in the control of cellular immune, inflammatory and stress responses. In the present study, we show that PDE4A5 is phosphorylated at Ser147, within the regulatory UCR1 (ultraconserved region 1) domain conserved among PDE4 long isoforms, by MK2 (MAPK-activated protein kinase 2, also called MAPKAPK2). Phosphorylation by MK2, although not altering PDE4A5 activity, markedly attenuates PDE4A5 activation through phosphorylation by protein kinase A. This modification confers the amplification of intracellular cAMP accumulation in response to adenylate cyclase activation by attenuating a major desensitization system to cAMP. Such reprogramming of cAMP accumulation is recapitulated in wild-type primary macrophages, but not MK2/3-null macrophages. Phosphorylation by MK2 also triggers a conformational change in PDE4A5 that attenuates PDE4A5 interaction with proteins whose binding involves UCR2, such as DISC1 (disrupted in schizophrenia 1) and AIP (aryl hydrocarbon receptor-interacting protein), but not the UCR2-independent interacting scaffold protein β-arrestin. Long PDE4 isoforms thus provide a novel node for cross-talk between the cAMP and p38 MAPK signalling systems at the level of MK2.

scholarly journals β2-Adrenergic Receptor-induced p38 MAPK Activation Is Mediated by Protein Kinase A Rather than by Gior Gβγ in Adult Mouse Cardiomyocytes

2000 ◽  
Vol 275 (51) ◽  
pp. 40635-40640 ◽  
Author(s):  
Ming Zheng ◽  
Sheng-Jun Zhang ◽  
Wei-Zhong Zhu ◽  
Bruce Ziman ◽  
Brian K. Kobilka ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
P38 Mapk ◽  
Adrenergic Receptor ◽  
Adult Mouse ◽  
Mapk Activation ◽  
Β2 Adrenergic Receptor ◽  
Kinase A

Angiotensin-(1–7)-induced activation of ERK1/2 is cAMP/protein kinase A-dependent in glomerular mesangial cells

2012 ◽  
Vol 302 (6) ◽  
pp. F784-F790 ◽  
Author(s):  
George C. Liu ◽  
Gavin Y. Oudit ◽  
Fei Fang ◽  
Joyce Zhou ◽  
James W. Scholey
Keyword(s):  
Protein Kinase ◽  
Nadph Oxidase ◽  
Protein Kinase A ◽  
Egf Receptor ◽  
Mesangial Cells ◽  
Renal Physiology ◽  
Intracellular Camp ◽  
Ang Ii ◽  
Glomerular Mesangial Cells ◽  
Kinase A

The renin-angiotensin system (RAS) plays an important role in renal physiology and kidney injury. Although the cellular effects of the RAS activation are generally attributed to angiotensin II (ANG II), the recent identification of angiotensin-converting enzyme 2 has shifted the focus to other peptides including Ang-(1–7). The G protein-coupled receptor for Ang-(1–7), mas, is expressed by mesangial cells (MC) but the signal transduction pathways activated by Ang-(1–7) in MC have not been fully elucidated. Accordingly, we studied the effect of Ang-(1–7) on extracellular signal-related kinase (ERK)1/2 activation in rat MC. Ang-(1–7)-induced ERK1/2 phosphorylation in MC is time- and concentration-dependent. Pretreatment of MC with the mas receptor antagonist A-779 but not the AT1 antagonist losartan or the AT2 antagonist PD123319 abrogated ERK1/2 activation. Neither pretreatment with the NADPH oxidase inhibitors diphenyleneiodonium and apocynin nor pretreatment with the epidermal growth factor (EGF) receptor antagonists AG1478 and PD158780 attenuated Ang-(1–7)-induced activation of ERK1/2. Even though each of these compounds abolished ANG II-induced activation of ERK1/2. Ang-(1–7) increased intracellular cAMP levels and activated protein kinase A (PKA) and inhibition of either adenylyl cyclase or PKA activity attenuated Ang-(1–7)-induced ERK1/2 activation. In conclusion, Ang-(1–7)-induced activation of ERK1/2 is cAMP/PKA-dependent in MC, but independent of NADPH oxidase and the EGF receptor.

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