Protein Kinase Translocation as an Early Event in the Hormonal Control of Uterine Contraction

Science ◽  
1974 ◽  
Vol 183 (4123) ◽  
pp. 430-432 ◽  
Author(s):  
S. G. Korenman ◽  
R. C. Bhalla ◽  
B. M. Sanborn ◽  
R. H. Stevens
Keyword(s):  
Protein Kinase ◽  
Uterine Contraction ◽  
Hormonal Control ◽  
Early Event

scholarly journals Selective Protein Kinase C Isoforms Are Involved in Endothelin-1-Induced Human Uterine Contraction at the End of Pregnancy

2000 ◽  
Vol 63 (5) ◽  
pp. 1567-1573 ◽  
Author(s):  
Isabelle Eude ◽  
Brigitte Paris ◽  
Dominique Cabrol ◽  
Françoise Ferré ◽  
Michelle Breuiller-Fouché
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Uterine Contraction ◽  
Endothelin 1 ◽  
Kinase C ◽  
Protein Kinase C Isoforms

scholarly journals Integrin-mediated Protein Kinase A Activation at the Leading Edge of Migrating Cells

2008 ◽  
Vol 19 (11) ◽  
pp. 4930-4941 ◽  
Author(s):  
Chinten J. Lim ◽  
Kristin H. Kain ◽  
Eugene Tkachenko ◽  
Lawrence E. Goldfinger ◽  
Edgar Gutierrez ◽  
...  
Keyword(s):  
Cell Migration ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Leading Edge ◽  
Pi3 Kinase ◽  
Early Event ◽  
Type I ◽  
Cell Protrusion ◽  
Kinase A ◽  
Migrating Cells

cAMP-dependent protein kinase A (PKA) is important in processes requiring localized cell protrusion, such as cell migration and axonal path finding. Here, we used a membrane-targeted PKA biosensor to reveal activation of PKA at the leading edge of migrating cells. Previous studies show that PKA activity promotes protrusion and efficient cell migration. In live migrating cells, membrane-associated PKA activity was highest at the leading edge and required ligation of integrins such as α4β1 or α5β1 and an intact actin cytoskeleton. α4 integrins are type I PKA-specific A-kinase anchoring proteins, and we now find that type I PKA is important for localization of α4β1 integrin-mediated PKA activation at the leading edge. Accumulation of 3′ phosphorylated phosphoinositides [PtdIns(3,4,5)P3] products of phosphatidylinositol 3-kinase (PI3-kinase) is an early event in establishing the directionality of migration; however, polarized PKA activation did not require PI3-kinase activity. Conversely, inhibition of PKA blocked accumulation of a PtdIns(3,4,5)P3-binding protein, the AKT-pleckstrin homology (PH) domain, at the leading edge; hence, PKA is involved in maintaining cell polarity during migration. In sum, we have visualized compartment-specific PKA activation in migrating cells and used it to reveal that adhesion-mediated localized activation of PKA is an early step in directional cell migration.

scholarly journals Antizyme Restrains Centrosome Amplification by Regulating the Accumulation of Mps1 at Centrosomes

2010 ◽  
Vol 21 (22) ◽  
pp. 3878-3889 ◽  
Author(s):  
Christopher Kasbek ◽  
Ching-Hui Yang ◽  
Harold A. Fisk
Keyword(s):  
Protein Kinase ◽  
Tumor Suppressor ◽  
Centrosome Amplification ◽  
Centrosome Duplication ◽  
Early Event ◽  
Mitotic Spindles ◽  
Duplication Cycle

Extra centrosomes are found in many tumors, and their appearance is an early event that can generate aberrant mitotic spindles and aneuploidy. Because the failure to appropriately degrade the Mps1 protein kinase correlates with centrosome overproduction in tumor-derived cells, defects in the factors that promote Mps1 degradation may contribute to extra centrosomes in tumors. However, while we have recently characterized an Mps1 degradation signal, the factors that regulate Mps1 centrosomal Mps1 are unknown. Antizyme (OAZ), a mediator of ubiquitin-independent degradation and a suspected tumor suppressor, was recently shown to localize to centrosomes and modulate centrosome overproduction, but the known OAZ substrates were not responsible for its effect on centrosomes. We have found that OAZ exerts its effect on centrosomes via Mps1. OAZ promotes the removal of Mps1 from centrosomes, and centrosome overproduction caused by reducing OAZ activity requires Mps1. OAZ binds to Mps1 via the Mps1 degradation signal and modulates the function of Mps1 in centrosome overproduction. Moreover, OAZ regulates the canonical centrosome duplication cycle, and reveals a function for Mps1 in procentriole assembly. Together, our data suggest that OAZ restrains the assembly of centrioles by controlling the levels of centrosomal Mps1 through the Cdk2-regulated Mps1 degradation signal.

scholarly journals Stimulation of phosphoinositide metabolism in hamster brown adipocytes exposed to α1-adrenergic agents and its inhibition with phorbol esters

1986 ◽  
Vol 236 (3) ◽  
pp. 757-764 ◽  
Author(s):  
R J Schimmel ◽  
D Dzierzanowski ◽  
M E Elliott ◽  
T W Honeyman
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Time Course ◽  
Early Event ◽  
Phosphoinositide Metabolism ◽  
Adrenergic Stimulation ◽  
Brown Adipocytes ◽  
Adrenergic Agents ◽  
Kinase C ◽  
Stimulation Of

The present experiments were undertaken to investigate the role of the phosphoinositides phosphatidylinositol 4-phosphate (PtdIns-4-P) and phosphatidylinositol 4,5-biphosphate (PtdIns-4,5-P2) in the alpha 1-adrenergic stimulation of respiration in isolated hamster brown adipocytes. Exposure of isolated brown adipocytes to the alpha-adrenergic-receptor agonist phenylephrine provoked a breakdown of 30-50% of the PtdIns-4-P and PtdIns-4,5-P2 after prelabelling of the cells with [32P]Pi. Coincident with the breakdown of phosphoinositides was an accumulation of labelled phosphatidic acid, which continued for the duration of the cell incubation. The time course of phosphoinositide breakdown was defined more precisely by pulse-chase experiments. Under these conditions, phenylephrine caused radioactivity in phosphatidylinositol, PtdIns-4-P and PtdIns-4,5-P2 to fall by more than 50% within 30 s and to remain at the depressed value for the duration of the incubation (10 min). This phospholipid response to alpha-adrenergic stimulation was blocked by exposure of the cells to phorbol 12-myristate 13-acetate (PMA); likewise phenylephrine stimulation of respiration was prevented by PMA. beta-Adrenergic stimulation of respiration and inhibition of respiration by 2-chloroadenosine and insulin were, however, unaffected by treatment with PMA. On the assumption that PMA is acting in these cells as an activator of protein kinase C, these results suggest the selective interruption of alpha-adrenergic actions in brown adipocytes by activated protein kinase C. These findings suggest that breakdown of phosphoinositides is an early event in alpha-adrenergic stimulation of brown adipocytes which may be important for the subsequent stimulation of respiration. The results from the pulse-chase studies also suggest, however, that phenylephrine-stimulated breakdown of inositol phospholipids is a short-lived event which does not appear to persist for the entire period of exposure to the alpha 1-adrenergic ligand.

scholarly journals Cell Cycle and Hormonal Control of Nuclear-Cytoplasmic Localization of the Serum- and Glucocorticoid-inducible Protein Kinase, Sgk, in Mammary Tumor Cells

1999 ◽  
Vol 274 (11) ◽  
pp. 7253-7263 ◽  
Author(s):  
Patricia Buse ◽  
Susan H. Tran ◽  
Ed Luther ◽  
Phan T. Phu ◽  
Gregory W. Aponte ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Tumor Cells ◽  
Mammary Tumor ◽  
Hormonal Control ◽  
Cytoplasmic Localization ◽  
Mammary Tumor Cells ◽  
Inducible Protein

Nanomolar concentration of NSC606985, a camptothecin analog, induces leukemic-cell apoptosis through protein kinase Cδ–dependent mechanisms

Blood ◽  
2005 ◽  
Vol 105 (9) ◽  
pp. 3714-3721 ◽  
Author(s):  
Man-Gen Song ◽  
Shen-Meng Gao ◽  
Ke-Ming Du ◽  
Min Xu ◽  
Yun Yu ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Caspase 3 ◽  
Specific Inhibitor ◽  
Leukemic Cell ◽  
K562 Cells ◽  
Early Event ◽  
Apoptosis Induction ◽  
Proteolytic Activation ◽  
Induced Apoptosis ◽  
Protein Kinase Cδ

AbstractAs a promising new class of anticancer drugs, camptothecins have advanced to the forefront of several areas of therapeutic and developmental chemotherapy. In the present study, we report that NSC606985, a rarely studied camptothecin analog, induces apoptosis in acute myeloid leukemia (AML) cells NB4 and U937 and inhibits the proliferation without cell death in breakpoint cluster region–Abelson murine leukemia (bcr-abl) kinase-carrying leukemic K562 cells. For apoptosis induction or growth arrest, nanomolar concentrations of NSC606985 are sufficient. At such low concentrations, this agent also significantly inhibits the clonogenic activity of hematopoietic progenitors from patients with AML. For apoptosis induction, NSC606985 rapidly induces the proteolytic activation of protein kinase Cδ (PKCδ) with loss of mitochondrial transmembrane potential (ΔΨm) and caspase-3 activation. Cotreatment with rottlerin, a PKCδ-specific inhibitor, completely blocks NSC606985-induced mitochondrial ΔΨm loss and caspase-3 activation, while the inhibition of caspase-3 by z-DEVD-fluoromethyl ketone (Z-DEVD-fmk) only partially attenuates PKCδ activation and apoptosis. These data indicate that NSC606985-induced PKCδ activation is an early event upstream to mitochondrial ΔΨm loss and caspase-3 activation, while activated caspase-3 has an amplifying effect on PKCδ proteolysis. In addition, NSC606985-induced apoptosis by PKCδ also involves caspase-3–independent mechanisms. Taken together, our results suggest that NSC606985 is a potential agent for the treatment of AML.

scholarly journals Activation of the pp60c-src protein kinase is an early event in colonic carcinogenesis.

1990 ◽  
Vol 87 (2) ◽  
pp. 558-562 ◽  
Author(s):  
C. A. Cartwright ◽  
A. I. Meisler ◽  
W. Eckhart
Keyword(s):  
Protein Kinase ◽  
Early Event ◽  
Colonic Carcinogenesis

scholarly journals Mitogen-Activated Protein Kinase Cascade Is Involved in Endothelin-1-Induced Rat Puerperal Uterine Contraction

Endocrinology ◽  
1999 ◽  
Vol 140 (2) ◽  
pp. 722-731 ◽  
Author(s):  
Akiko Kimura ◽  
Masahide Ohmichi ◽  
Takashi Takeda ◽  
Hirohisa Kurachi ◽  
Hiromasa Ikegami ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Uterine Contraction ◽  
Mitogen Activated Protein Kinase ◽  
Endothelin 1 ◽  
Mitogen Activated Protein ◽  
Kinase Cascade ◽  
Protein Kinase Cascade
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