scholarly journals p38 MAP Kinase Is Required for Vasopressin-Stimulated HSP27 Induction in Aortic Smooth Muscle Cells

Hypertension ◽  
2000 ◽  
Vol 35 (2) ◽  
pp. 673-678 ◽  
Author(s):  
Takeshi Ito ◽  
Osamu Kozawa ◽  
Kumiko Tanabe ◽  
Masayuki Niwa ◽  
Hiroyuki Matsuno ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Map Kinase ◽  
Muscle Cells ◽  
P38 Map Kinase ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle

Akt regulates thrombin-induced HSP27 phosphorylation in aortic smooth muscle cells: Function at a point downstream from p38 MAP kinase

Life Sciences ◽  
2005 ◽  
Vol 77 (1) ◽  
pp. 96-107 ◽  
Author(s):  
Keiichi Nakajima ◽  
Kouseki Hirade ◽  
Akira Ishisaki ◽  
Hiroyuki Matsuno ◽  
Hidetaka Suga ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Map Kinase ◽  
Muscle Cells ◽  
P38 Map Kinase ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Hsp27 Phosphorylation

Involvement of p38 MAP kinase in TGF-?-stimulated VEGF synthesis in aortic smooth muscle cells

2001 ◽  
Vol 82 (4) ◽  
pp. 591-598 ◽  
Author(s):  
Takuji Yamamoto ◽  
Osamu Kozawa ◽  
Kumiko Tanabe ◽  
Shigeru Akamatsu ◽  
Hiroyuki Matsuno ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Map Kinase ◽  
Muscle Cells ◽  
P38 Map Kinase ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle

scholarly journals Phytoestrogens Inhibit Growth and MAP Kinase Activity in Human Aortic Smooth Muscle Cells

Hypertension ◽  
1999 ◽  
Vol 33 (1) ◽  
pp. 177-182 ◽  
Author(s):  
Raghvendra K. Dubey ◽  
Delbert G. Gillespie ◽  
Bruno Imthurn ◽  
Marinella Rosselli ◽  
Edwin K. Jackson ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Map Kinase ◽  
Kinase Activity ◽  
Muscle Cells ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle

Midazolam Stimulates Vascular Endothelial Growth Factor Release in Aortic Smooth Muscle Cells

2003 ◽  
Vol 98 (5) ◽  
pp. 1147-1154 ◽  
Author(s):  
Kumiko Tanabe ◽  
Shuji Dohi ◽  
Hiroyuki Matsuno ◽  
Kouseki Hirade ◽  
Osamu Kozawa
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Map Kinase ◽  
Muscle Cells ◽  
Rat Plasma ◽  
Vascular Endothelial ◽  
Intravenous Anesthetics ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Vegf Release

Background Intravenous anesthetics used during perioperative periods affect the vascular signaling molecules and the vascular reactivity. Vascular endothelial growth factor (VEGF), an angiogenesis factor produced in and secreted from aortic smooth muscle cells, is a specific mitogen for vascular endothelial cells. This study investigated the effects of various intravenous anesthetics on VEGF release, and the underlying mechanism, in a rat aortic smooth muscle cell line, A10 cells. Methods Intravenous anesthetics (midazolam and propofol) were continuously administered to rats by infusion. Cultured A10 cells were stimulated by intravenous anesthetics (midazolam, propofol, and ketamine). VEGF was evaluated by immunoassay. The phosphorylation of mitogen-activated protein (MAP) kinases was evaluated by Western blotting. Results Continuous infusion of midazolam, but not propofol, increased the VEGF concentration in rat plasma. In cultured cells, midazolam stimulated VEGF release, but propofol and ketamine did not. Midazolam induced phosphorylation of p44/p42 MAP kinase and stress-activated protein kinase (SAPK)/c-Jun N-terminal kinase (JNK), without affecting p38 MAP kinase. PD98059 and U0126, specific inhibitors of MAP kinase kinase, significantly reduced the midazolam-stimulated release of VEGF. SP600125, a specific inhibitor of SAPK/JNK, significantly reduced midazolam-stimulated VEGF release. Applied together, PD98059 and SP600125 produced an additive reduction in midazolam-stimulated VEGF release. Moreover, a bolus injection of PD98059 truly inhibited the midazolam-increased VEGF concentration in rat plasma in vivo. Conclusions Midazolam, but not propofol or ketamine, stimulates VEGF release in aortic smooth muscle cells. Its effect is mediated at least in part via activation of p44/p42 MAP kinase and SAPK/JNK.

Homocysteine stimulates MAP kinase in bovine aortic smooth muscle cells

Surgery ◽  
2000 ◽  
Vol 128 (1) ◽  
pp. 59-66 ◽  
Author(s):  
Daniel K. Woo ◽  
Stanley J. Dudrick ◽  
Bauer E. Sumpio
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Map Kinase ◽  
Muscle Cells ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle

7β-Hydroxycholesterol induces Ca2+ oscillations, MAP kinase activation and apoptosis in human aortic smooth muscle cells

2000 ◽  
Vol 153 (1) ◽  
pp. 23-35 ◽  
Author(s):  
Mikko P.S Ares ◽  
M.Isabella Pörn-Ares ◽  
Sara Moses ◽  
Johan Thyberg ◽  
Lisa Juntti-Berggren ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Map Kinase ◽  
Muscle Cells ◽  
Kinase Activation ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle

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.

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