Bombesin, Bradykinin, Vasopressin, and Phorbol Esters Rapidly and Transiently Activate Src Family Tyrosine Kinases in Swiss 3T3 Cells

@article{RodriguezFernndez1996BombesinBV,
  title={Bombesin, Bradykinin, Vasopressin, and Phorbol Esters Rapidly and Transiently Activate Src Family Tyrosine Kinases in Swiss 3T3 Cells},
  author={Jos{\'e}Luis Rodriguez-Fern{\'a}ndez and E. Rozengurt},
  journal={The Journal of Biological Chemistry},
  year={1996},
  volume={271},
  pages={27895 - 27901}
}
Treatment of quiescent Swiss 3T3 cells with bombesin induces a rapid (≤40 s) and transient increase in the kinase activity of the Src family of tyrosine kinases, as determined by autophosphorylation in immune complex kinase assays (4.6 ± 0.2-fold stimulation, n = 44) and phosphorylation of exogenous substrates. Phorbol 12,13-dibutyrate increased the activity of Src family kinases with similar kinetics but was less effective than bombesin. However, Src family kinase activation by bombesin is not… Expand
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References

SHOWING 1-10 OF 61 REFERENCES
Bombesin, vasopressin, and endothelin rapidly stimulate tyrosine phosphorylation of the focal adhesion-associated protein paxillin in Swiss 3T3 cells.
Treatment of Swiss 3T3 cells with bombesin caused a striking increase (21-fold) in the tyrosine phosphorylation of the cytoskeleton-associated protein paxillin, as judged by anti-phosphotyrosineExpand
Tyrphostin inhibits bombesin stimulation of tyrosine phosphorylation, c-fos expression, and DNA synthesis in Swiss 3T3 cells.
TLDR
Evidence that tyrosine phosphorylation is a mitogenic signal for bombesin is provided by treatment of intact Swiss 3T3 cells with 20 microM tyrphostin. Expand
Bombesin stimulation of p125 focal adhesion kinase tyrosine phosphorylation. Role of protein kinase C, Ca2+ mobilization, and the actin cytoskeleton.
TLDR
It is demonstrated that neither the PKC nor Ca2+ pathways are responsible for the rapid stimulation of p125FAK tyrosine phosphorylation by neuropeptide growth factors, and the integrity of the actin cytoskeleton is essential for the effects of both PDB and bombesin. Expand
Bombesin, vasopressin, and endothelin rapidly stimulate tyrosine phosphorylation in intact Swiss 3T3 cells.
TLDR
It is demonstrated that neuropeptides, acting through receptors linked to GTP-binding proteins, stimulate tyrosine phosphorylation of a common set of substrates in quiescent Swiss 3T3 cells and suggest the existence of an additional signal transduction pathway in neuropeptic-induced mitogenesis. Expand
Bombesin, vasopressin, and endothelin stimulation of tyrosine phosphorylation in Swiss 3T3 cells. Identification of a novel tyrosine kinase as a major substrate.
TLDR
The finding that one of these substrates is a tyrosine kinase suggests the existence of a novel signal transduction pathway in the action of mitogenic neuropeptides. Expand
Bradykinin and bombesin rapidly stimulate tyrosine phosphorylation of a 120-kDa group of proteins in Swiss 3T3 cells.
TLDR
It is shown that an increase in tyrosine phosphorylation of a 120-kDa group of proteins is an early protein kinase C-independent cellular signal elicited by both bradykinin and bombesin. Expand
Bombesin, diacylglycerols, and phorbol esters rapidly stimulate the phosphorylation of an Mr = 80,000 protein kinase C substrate in permeabilized 3T3 cells. Effect of guanine nucleotides.
TLDR
These results demonstrate for the first time a growth factor receptor-mediated activation of protein kinase C in permeabilized cells and provide functional evidence for the involvement of a G protein in the transmembrane signaling pathway that mediates the stimulation of protein Kinase C by bombesin in Swiss 3T3 cells. Expand
Stimulation of tyrosine kinase activity in anti-phosphotyrosine immune complexes of Swiss 3T3 cell lysates occurs rapidly after addition of bombesin, vasopressin, and endothelin to intact cells.
TLDR
Results provide direct evidence for neuropeptide activation of a tyrosine kinase in cell-free preparations and identify a novel event in the action of this class of growth factors in intact Swiss 3T3 cells. Expand
Lysophosphatidic acid stimulates tyrosine phosphorylation of focal adhesion kinase, paxillin, and p130. Signaling pathways and cross-talk with platelet-derived growth factor.
TLDR
The integrity of the actin cytoskeleton is essential for LPA-induced tyrosine phosphorylation and a novel cross-talk between LPA and platelet-derived growth factor on p125FAK tyrosines is revealed. Expand
Early events elicited by bombesin and structurally related peptides in quiescent Swiss 3T3 cells. I. Activation of protein kinase C and inhibition of epidermal growth factor binding
TLDR
The activation of protein kinase C in intact Swiss 3T3 cells by peptides of the bombesin family may lead to rapid inhibition of the binding of 125I-EGF to its cellular receptor. Expand
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