Involvement of S6 kinase and p38 mitogen activated protein kinase pathways in strain-induced alignment and proliferation of bovine aortic smooth muscle cells

2003 ◽  
Vol 195 (2) ◽  
pp. 202-209 ◽  
Author(s):  
Wei Li ◽  
Quanhai Chen ◽  
Ira Mills ◽  
Bauer E. Sumpio
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Mitogen Activated Protein Kinase ◽  
S6 Kinase ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Mitogen Activated Protein

Effects of dehydroepiandrosterone on mitogen-activated protein kinase in human aortic smooth muscle cells

Life Sciences ◽  
1999 ◽  
Vol 65 (4) ◽  
pp. 431-440 ◽  
Author(s):  
Takayuki Yoshimata ◽  
Akihiko Yoneyama ◽  
Yasunari Jin-no ◽  
Nozomu Tamai ◽  
Yoshinobu Kamiya
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Mitogen Activated Protein Kinase ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Mitogen Activated Protein

scholarly journals Efficacy of agonist-stimulated MEK activation determines the susceptibility of mitogen-activated protein (MAP) kinase to inhibition in rat aortic smooth muscle cells

1996 ◽  
Vol 318 (2) ◽  
pp. 657-663 ◽  
Author(s):  
Robin PLEVIN ◽  
Pamela H SCOTT ◽  
Casper J. M. ROBINSON ◽  
Gwyn W. GOULD
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Map Kinase ◽  
Kinase Activity ◽  
Muscle Cells ◽  
Kinase Activation ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Mitogen Activated Protein

In rat aortic smooth muscle cells, platelet-derived growth factor (PDGF) stimulated a sustained activation of mitogen-activated protein kinase (MAP kinase) while the response to angiotensin II (AII) was transient. This was due to a relatively greater initial activation of MAP kinase kinase (MEK) and a correspondingly greater residual MEK activity at later time points. Pretreatment of cells with the novel MEK inhibitor PD 098059 reduced MEK activation at 5 min in response to each agonist by a similar proportion (70%); however, at this time point MAP kinase activation in response to PDGF was only marginally affected while the response to AII was substantially reduced. PD 098059 did, however, reduce PDGF-stimulated MEK activity after 30 min and this correlated with a loss in MAP kinase activity and DNA synthesis. Pretreatment with forskolin also caused a similar pattern of inhibition of agonist-stimulated MEK and MAP kinase activity. Only following protein kinase C down-regulation were both AII- and PDGF-stimulated MAP kinase activation substantially reduced and this correlated with the virtual loss of both MEK and c-Raf-1 activity in response to both agents. The differential inhibition of MAP kinase activation by forskolin was not due to specific activation of A-Raf by PDGF; both PDGF and AII stimulated A-Raf kinase and this activity was strongly inhibited by forskolin. These results suggest that the efficacy of MEK activation determines the duration of MAP kinase activation and the susceptibility of MAP kinase activation to inhibition by different agents. The results also argue against the selective activation of A-Raf by PDGF as a mechanism to explain the differences in the kinetics of MAP kinase activity stimulated by AII and PDGF.

scholarly journals Histamine induces activation of protein kinase D that mediates tissue factor expression and activity in human aortic smooth muscle cells

2012 ◽  
Vol 303 (11) ◽  
pp. H1344-H1352 ◽  
Author(s):  
Feng Hao ◽  
Daniel Dongwei Wu ◽  
Xuemin Xu ◽  
Mei-Zhen Cui
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Tissue Factor ◽  
Mapk Pathway ◽  
Muscle Cells ◽  
Mitogen Activated Protein Kinase ◽  
Protein Kinase D ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle

Histamine, an inflammatory mediator, has been shown to influence the pathogenesis of vascular wall cells. However, the molecular basis of its influence is not well understood. Our data reveal that histamine markedly induces protein kinase D (PKD) activation in human aortic smooth muscle cells. PKD belongs to a family of serine/threonine protein kinases, and its function in vascular disease is largely unknown. Our data show that histamine-induced PKD phosphorylation is dependent on the activation of histamine receptor 1 and protein kinase C (PKC). To determine the role of PKD in the histamine pathway, we employed a small-interfering RNA approach to downregulate PKD expression and found that PKD1 and PKD2 are key mediators for expression of tissue factor (TF), which is the key initiator of blood coagulation and is important for thrombosis. Our results show that PKD2 predominantly mediates histamine-induced TF expression via the p38 mitogen-activated protein kinase (MAPK) pathway, whereas PKD1 mediates histamine-induced TF expression through a p38 MAPK-independent pathway. We demonstrate that histamine induces TF expression via the PKC-dependent PKD activation. Our data provide the first evidence that PKD is a new component in histamine signaling in live cells and that PKD has a novel function in the histamine signaling pathway leading to gene expression, as evidenced by TF expression. Importantly, our data reveal a regulatory link from histamine to PKD and TF, providing new insights into the mechanisms of coagulation and the development of atherothrombosis.

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