Gsα, protein kinase C, cathepsin D, growth factors, estrogen receptor-related protein, and p53 in prolactin cell adenomas and null cell adenomas of the pituitary

1998 ◽  
Vol 9 (2) ◽  
pp. 135-148
Author(s):  
Lars Wellhausen ◽  
Wolfgang Saeger ◽  
Wolf Müller ◽  
Michael Derwahl ◽  
Christiane Hamacher ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Protein Kinase C ◽  
Growth Factors ◽  
Protein Kinase ◽  
Cathepsin D ◽  
Related Protein ◽  
Null Cell ◽  
Prolactin Cell ◽  
Kinase C ◽  
Null Cell Adenomas

Growth Factors, Oncogenes, and Protein Kinase C

1989 ◽  
pp. 249-254
Author(s):  
Ian G. Macara ◽  
George Gray ◽  
James Gaut ◽  
Anna Coco ◽  
Theresa Wingrove ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Growth Factors ◽  
Protein Kinase ◽  
Kinase C

scholarly journals Neuroprotection by Peptide Growth Factors against Anoxia and Nitric Oxide Toxicity Requires Modulation of Protein Kinase C

1995 ◽  
Vol 15 (3) ◽  
pp. 440-449 ◽  
Author(s):  
Kenneth Maiese ◽  
Lauraine Boccone
Keyword(s):  
Nitric Oxide ◽  
Signal Transduction ◽  
Protein Kinase C ◽  
Growth Factors ◽  
Growth Factor ◽  
Protein Kinase ◽  
Neuronal Degeneration ◽  
Kinase C ◽  
Peptide Growth Factors ◽  
Pkc Activation

Basic fibroblast growth factor (bFGF) and epidermal growth factor (EGF) are neuroprotective during anoxia and nitric oxide (NO) toxicity. Signal transduction systems that modulate protein kinase C (PKC) also can modulate the toxic effects of anoxia and NO. We therefore examined whether PKC was involved in the protective effects of bFGF and EGF during anoxia and NO toxicity. Down-regulation or inhibition of PKC activity before anoxia or NO exposure prevented hippocampal neuronal degeneration. Yet, this protective effect of inhibition of PKC activity was not present with the coadministration of growth factors. Combined inhibition of PKC activity and application of bFGF or EGF lessened the protective mechanisms of the growth factors. In addition, the protective ability of the growth factors was lost during anoxia and NO exposure with the activation of PKC, suggesting that at least a minimal degree of PKC activation is necessary for growth factor protection. Although modulation of PKC activity may be a necessary prerequisite for protection against anoxia and NO toxicity by bFGF and EGF, only inhibition of PKC activity, rather than application of the growth factors, was protective following exposure to NO. These results suggest that the mechanism of protection by bFGF and EGF during anoxia and NO toxicity appears initially to be dependent on a minimum degree of PKC activation, but that other signal transduction pathways independent of PKC also may mediate protection by peptide growth factors.

scholarly journals Rapid Signaling of Estrogen in Hypothalamic Neurons Involves a Novel G-Protein-Coupled Estrogen Receptor that Activates Protein Kinase C

2003 ◽  
Vol 23 (29) ◽  
pp. 9529-9540 ◽  
Author(s):  
Jian Qiu ◽  
Martha A. Bosch ◽  
Sandra C. Tobias ◽  
David K. Grandy ◽  
Thomas S. Scanlan ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
G Protein ◽  
Hypothalamic Neurons ◽  
Kinase C ◽  
Rapid Signaling ◽  
G Protein Coupled

Cross-talk between receptors with intrinsic tyrosine kinase activity and α1b-adrenoceptors

2000 ◽  
Vol 350 (2) ◽  
pp. 413-419 ◽  
Author(s):  
Luz DEL CARMEN MEDINA ◽  
José VÁZQUEZ-PRADO ◽  
J. Adolfo GARCÍA-SÁINZ
Keyword(s):  
Protein Kinase C ◽  
Growth Factors ◽  
Growth Factor ◽  
Protein Kinase ◽  
Tyrosine Kinase ◽  
Functional Coupling ◽  
Kinase C ◽  
Epidermal Growth ◽  
Phosphoinositide 3 Kinase ◽  
And Function

The effect of epidermal growth factor (EGF) and platelet-derived growth factor (PDGF) on the phosphorylation and function of α1b-adrenoceptors transfected into Rat-1 fibroblasts was studied. EGF and PDGF increased the phosphorylation of these adrenoceptors. The effect of EGF was blocked by tyrphostin AG1478 and that of PDGF was blocked by tyrphostin AG1296, inhibitors of the intrinsic tyrosine kinase activities of the receptors for these growth factors. Wortmannin, an inhibitor of phosphoinositide 3-kinase, blocked the α1b-adrenoceptor phosphorylation induced by EGF but not that induced by PDGF. Inhibition of protein kinase C blocked the adrenoceptor phosphorylation induced by EGF and PDGF. The ability of noradrenaline to increase [35S]guanosine 5´-[γ-thio]triphosphate ([35S]GTP[S]) binding in membrane preparations was used as an index of the functional coupling of the α1b-adrenoceptors and G-proteins. Noradrenaline-stimulated [35S]GTP[S] binding was markedly decreased in membranes from cells pretreated with EGF or PDGF. Our data indicate that: (i) activation of EGF and PDGF receptors induces phosphorylation of α1b-adrenoceptors, (ii) phosphatidylinositol 3-kinase is involved in the EGF response, but does not seem to play a major role in the action of PDGF, (iii) protein kinase C mediates this action of both growth factors and (iv) the phosphorylation of α1b-adrenoceptors induced by EGF and PDGF is associated with adrenoceptor desensitization.

Investigating the Protein Kinase C Polarized Growth‐Related Protein Complex in Aspergillus nidulans

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Loretta Jackson-Hayes ◽  
Alexis Craft ◽  
Muhammad Hameed ◽  
Zariah Hines ◽  
W. Toler Freyaldenhoven ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Aspergillus Nidulans ◽  
Protein Complex ◽  
Polarized Growth ◽  
Related Protein ◽  
Kinase C
Sign in / Sign up

Export Citation Format

Share Document