scholarly journals Suppression of platelet-derived growth factor receptor tyrosine kinase activity by unsaturated fatty acids.

1993 ◽  
Vol 268 (7) ◽  
pp. 5317-5322
Author(s):  
L. Tomáska ◽  
R.J. Resnick
Keyword(s):  
Fatty Acids ◽  
Growth Factor ◽  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Kinase Activity ◽  
Unsaturated Fatty Acids ◽  
Growth Factor Receptor ◽  
Platelet Derived Growth Factor ◽  
Tyrosine Kinase Activity

scholarly journals Role of tyrosine kinase and membrane-spanning domains in signal transduction by the platelet-derived growth factor receptor.

1988 ◽  
Vol 8 (12) ◽  
pp. 5126-5131 ◽  
Author(s):  
J A Escobedo ◽  
P J Barr ◽  
L T Williams
Keyword(s):  
Growth Factor ◽  
Tyrosine Kinase ◽  
Kinase Activity ◽  
Growth Factor Receptor ◽  
Platelet Derived Growth Factor ◽  
Tyrosine Kinase Activity ◽  
Down Regulation ◽  
Atp Binding Site ◽  
Membrane Spanning ◽  
Membrane Spanning Domains

Three types of mutations were introduced into the platelet-derived growth factor (PDGF) receptor to cause a loss of PDGF-stimulated tyrosine kinase activity: (i) a point mutation of the ATP-binding site, (ii) a deletion of the carboxyl-terminal region, and (iii) replacement of the membrane-spanning sequences by analogous transmembrane sequences of other receptors. Transfectants expressing mutated receptors bind, 125I-labeled PDGF with a high affinity but had no PDGF-sensitive tyrosine kinase activity, phosphatidylinositol turnover, increase in the intracellular calcium concentration, change in cellular pH, or stimulation of DNA synthesis. However, PDGF-induced receptor down regulation was normal in the mutant cells. These results indicate that the transmembrane sequence has a specific signal-transducing function other than merely serving as a membrane anchor and that the receptor kinase activity is necessary for most responses to PDGF but is not required for receptor down regulation.

Inhibition of the epidermal growth factor receptor tyrosine kinase activity by leflunomide

FEBS Letters ◽  
1993 ◽  
Vol 334 (2) ◽  
pp. 161-164 ◽  
Author(s):  
Thomas Mattar ◽  
Kulvinder Kochhar ◽  
Robert Bartlett ◽  
Eric G. Bremer ◽  
Alison Finnegan
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Kinase Activity ◽  
Growth Factor Receptor ◽  
Tyrosine Kinase Activity ◽  
Epidermal Growth

Role of tyrosine kinase and membrane-spanning domains in signal transduction by the platelet-derived growth factor receptor

1988 ◽  
Vol 8 (12) ◽  
pp. 5126-5131
Author(s):  
J A Escobedo ◽  
P J Barr ◽  
L T Williams
Keyword(s):  
Growth Factor ◽  
Tyrosine Kinase ◽  
Kinase Activity ◽  
Growth Factor Receptor ◽  
Platelet Derived Growth Factor ◽  
Tyrosine Kinase Activity ◽  
Down Regulation ◽  
Atp Binding Site ◽  
Membrane Spanning ◽  
Membrane Spanning Domains

Three types of mutations were introduced into the platelet-derived growth factor (PDGF) receptor to cause a loss of PDGF-stimulated tyrosine kinase activity: (i) a point mutation of the ATP-binding site, (ii) a deletion of the carboxyl-terminal region, and (iii) replacement of the membrane-spanning sequences by analogous transmembrane sequences of other receptors. Transfectants expressing mutated receptors bind, 125I-labeled PDGF with a high affinity but had no PDGF-sensitive tyrosine kinase activity, phosphatidylinositol turnover, increase in the intracellular calcium concentration, change in cellular pH, or stimulation of DNA synthesis. However, PDGF-induced receptor down regulation was normal in the mutant cells. These results indicate that the transmembrane sequence has a specific signal-transducing function other than merely serving as a membrane anchor and that the receptor kinase activity is necessary for most responses to PDGF but is not required for receptor down regulation.

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