Uniaxial Cyclic Stretch Induces Focal Adhesion Kinase (FAK) Tyrosine Phosphorylation Followed by Mitogen-Activated Protein Kinase (MAPK) Activation

2001 ◽  
Vol 288 (2) ◽  
pp. 356-361 ◽  
Author(s):  
Ju Guang Wang ◽  
Motoi Miyazu ◽  
Etsushi Matsushita ◽  
Masahiro Sokabe ◽  
Keiji Naruse
Keyword(s):  
Protein Kinase ◽  
Focal Adhesion Kinase ◽  
Tyrosine Phosphorylation ◽  
Focal Adhesion ◽  
Cyclic Stretch ◽  
Mitogen Activated Protein Kinase ◽  
Mapk Activation ◽  
Mitogen Activated Protein

Focal adhesion kinase, RhoA, and p38 mitogen‐activated protein kinase modulates apoptosis mediated by angiotensin II AT 2 receptors

2018 ◽  
Vol 120 (2) ◽  
pp. 1835-1849 ◽  
Author(s):  
María J. Manzur ◽  
Milton O. Aguilera ◽  
Mónica L. Kotler ◽  
Walter Berón ◽  
Gladys M. Ciuffo
Keyword(s):  
Angiotensin Ii ◽  
Protein Kinase ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein

scholarly journals Dissociation of mitogen-activated protein kinase activation from p125 focal adhesion kinase tyrosine phosphorylation in Swiss 3T3 cells stimulated by bombesin, lysophosphatidic acid, and platelet-derived growth factor.

1996 ◽  
Vol 7 (12) ◽  
pp. 1865-1875 ◽  
Author(s):  
T Seufferlein ◽  
D J Withers ◽  
D Mann ◽  
E Rozengurt
Keyword(s):  
Protein Kinase ◽  
Tyrosine Phosphorylation ◽  
Focal Adhesion ◽  
Lysophosphatidic Acid ◽  
Mitogen Activated Protein Kinase ◽  
Platelet Derived Growth Factor ◽  
3T3 Cells ◽  
Kinase C ◽  
Mitogen Activated Protein ◽  
Swiss 3T3

The experiments presented here were designed to examine the contribution of p125 focal adhesion kinase (p125FAK) tyrosine phosphorylation to the activation of the mitogen-activated protein kinase cascade induced by bombesin, lysophosphatidic acid (LPA), and platelet-derived growth factor (PDGF) in Swiss 3T3 cells. We found that tyrosine phosphorylation of p125FAK in response to these growth factors is completely abolished in cells treated with cytochalasin D or in cells that were suspended in serum-free medium for 30 min. In marked contrast, the activation of p42mapk by these factors was independent of the integrity of the actin cytoskeleton and of the interaction of the cells with the extracellular matrix. The protein kinase C inhibitor GF 109203X and down-regulation of protein kinase C by prolonged pretreatment of cells with phorbol esters blocked bombesin-stimulated activation of p42mapk, p90rsk, and MAPK kinase-1 but did not prevent bombesin-induced tyrosine phosphorylation of p125FAK. Furthermore, LPA-induced p42mapk activation involved a pertussis toxin-sensitive guanylate nucleotide-binding protein, whereas tyrosine phosphorylation of p125FAK in response to LPA was not prevented by pretreatment with pertussis toxin. Finally, PDGF induced maximum p42mapk activation at concentrations (30 ng/ml) that failed to induce tyrosine phosphorylation of p125FAK. Thus, our results demonstrate that p42mapk activation in response to bombesin, LPA, and PDGF can be dissociated from p125FAK tyrosine phosphorylation in Swiss 3T3 cells.

Mitogen-activated protein kinase and proliferation of human vascular smooth muscle cells

1996 ◽  
Vol 270 (1) ◽  
pp. H142-H150 ◽  
Author(s):  
S. Mii ◽  
R. A. Khalil ◽  
K. G. Morgan ◽  
J. A. Ware ◽  
K. C. Kent
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase ◽  
Tyrosine Phosphorylation ◽  
Vascular Smooth Muscle Cells ◽  
Early Phase ◽  
Nuclear Translocation ◽  
Mitogen Activated Protein Kinase ◽  
Mapk Activation ◽  
Mitogen Activated Protein ◽  
Mitogenic Potential

The intracellular messenger mitogen-activated protein kinase (MAPK) is activated in vascular smooth muscle cells (SMC) by various growth factors as well as by agonists that have no proliferative effect. We explored the hypotheses that SMC proliferation is associated with a specific pattern of MAPK activation by evaluating the kinetics of MAPK activation and tyrosine phosphorylation and the intracellular location of MAPK in SMC following addition of agonists of varying mitogenic potential. A peak in MAPK activation and tyrosine phosphorylation occurred 3-10 min after the addition of agonists to SMC derived from human saphenous vein (early phase), followed by a plateau of activity, which was variable in duration (late phase). A correlation was not found between mitogenicity and the degree to which MAPK became activated or tyrosine phosphorylated in the early phase. However, the duration of MAPK activation and tyrosine phosphorylation correlated strongly with the ability of agonists to stimulate SMC proliferation. Nuclear translocation of MAPK was associated with SMC proliferation, although the degree to which each agonist induced nuclear translocation did not parallel its mitogenic potential. The relative dependency of all three events on protein kinase C differed for each agonist and was greater in the late versus the early phase. Thus, in human SMC, nuclear translocation of MAPK and prolonged activation and tyrosine phosphorylation of MAPK are associated with growth factor-induced mitogenesis.

scholarly journals Ca2+ and protein kinase C-dependent mechanisms involved in gastrin-induced Shc/Grb2 complex formation and P44-mitogen-activated protein kinase activation

1997 ◽  
Vol 325 (2) ◽  
pp. 383-389 ◽  
Author(s):  
Laurence DAULHAC ◽  
Aline KOWALSKI-CHAUVEL ◽  
Lucien PRADAYROL ◽  
Nicole VAYSSE ◽  
Catherine SEVA
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tyrosine Phosphorylation ◽  
Phorbol Esters ◽  
Receptor Occupancy ◽  
Mitogen Activated Protein Kinase ◽  
Free Calcium ◽  
Mapk Activation ◽  
Kinase C ◽  
Mitogen Activated Protein

The proliferative effects of gastrin on normal and neoplastic gastro-intestinal tissues have been shown to be mediated by the gastrin/CCKB (G/CCKB) G-protein-coupled receptors. We have recently reported that gastrin stimulates the tyrosine phosphorylation of Shc proteins and their subsequent association with the Grb2/Sos complex, leading to mitogen-activated protein kinase (MAPK) activation, a pathway known to play an important role in cell proliferation. We undertook the present study to characterize the signalling pathways used by this receptor to mediate the activation of the Shc/Grb2 complex. Since G/CCKB receptor occupancy leads to the activation of the phospholipase C (PLC)/protein kinase C (PKC) pathway, we examined whether PKC stimulation and Ca2+ mobilization contribute to the phosphorylation of Shc proteins and their association with Grb2 in response to gastrin. Our results indicate that Shc proteins are tyrosine phosphorylated and associate with Grb2 in response to phorbol esters, suggesting that activation of PKC is a potential signalling pathway leading to activation of the Shc/Grb2 complex. Inhibition of PKC by GF109203X completely blocked the effect of PMA on Shc tyrosine phosphorylation and its subsequent association with Grb2, but had a partial inhibitory effect on the response to gastrin. Depletion of the intracellular Ca2+ pools by treatment with thapsigargin blocked the increase in intracellular free calcium concentration induced by gastrin and diminished the ability of the peptide to stimulate Shc phosphorylation and recruitment of Grb2. In addition, removal of extracellular Ca2+ partially inhibited the effect of gastrin on Shc phosphorylation as well as its association with Grb2, indicating that the effects of gastrin are also mediated by Ca2+-dependent mechanisms. Furthermore, we show that blockage of the two major early signals generated by activation of PLC, which induced the activation of the Shc/Grb2 complex, also blocked gastrin-induced MAPK activation.

scholarly journals Divergent Signaling Pathways Link Focal Adhesion Kinase to Mitogen-activated Protein Kinase Cascades

1999 ◽  
Vol 274 (43) ◽  
pp. 30738-30746 ◽  
Author(s):  
Tadashi Igishi ◽  
Shigetomo Fukuhara ◽  
Vyomesh Patel ◽  
Ben-Zion Katz ◽  
Kenneth M. Yamada ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Focal Adhesion Kinase ◽  
Signaling Pathways ◽  
Focal Adhesion ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein
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