scholarly journals The cAMP-Dependent Protein Kinase A and Protein Kinase C-β Pathways Synergistically Interact to Activate HIV-1 Transcription in Latently Infected Cells of Monocyte/Macrophage Lineage

Virology ◽  
1998 ◽  
Vol 245 (2) ◽  
pp. 257-269 ◽  
Author(s):  
Mohammed F. Rabbi ◽  
Lena Al-Harthi ◽  
Mohammed Saifuddin ◽  
Kenneth A. Roebuck
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Dependent Protein Kinase ◽  
Kinase C ◽  
Latently Infected ◽  
Dependent Protein ◽  
Infected Cells ◽  
Hiv 1 ◽  
Macrophage Lineage ◽  
Kinase A

scholarly journals Nonclassical Mechanisms of Progesterone Action in the Brain: II. Role of Calmodulin-Dependent Protein Kinase II in Progesterone-Mediated Signaling in the Hypothalamus of Female Rats

Endocrinology ◽  
2008 ◽  
Vol 149 (11) ◽  
pp. 5518-5526 ◽  
Author(s):  
Bhuvana Balasubramanian ◽  
Wendy Portillo ◽  
Andrea Reyna ◽  
Jian Zhong Chen ◽  
Anthony N. Moore ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Kinase Activity ◽  
Female Rats ◽  
Dependent Protein Kinase ◽  
Kinase C ◽  
Dependent Protein ◽  
The Brain ◽  
Kinase A

In addition to the activation of classical progestin receptor-dependent genomic pathway, progesterone (P) can activate nonclassical, membrane-initiated signaling pathways in the brain. We recently demonstrated rapid P activation of second-messenger kinases, protein kinase A, and protein kinase C in the ventromedial nucleus (VMN) and preoptic area (POA) of rat brain. To determine whether P can activate yet another Ca+2dependent kinase, we examined the rapid P modulation of calcium and calmodulin-dependent protein kinase II (CaMKII) in the VMN and POA in female rats. A rapid P-initiated activation of CaMKII basal activity was observed in the VMN but not the POA at 30 min. Estradiol benzoate (EB) priming enhanced this CaMKII basal activity in both the VMN and POA. CaMKII protein levels and phosphorylation of Thr-286 moiety on CaMKII, however, remained unchanged with EB and/or P treatments, suggesting that the changes in the CaMKII kinase activity are due to rapid P modulation of the kinase activity and not its synthesis or autoactivation. Furthermore, intracerebroventricular (icv) administration of a CaMKII-specific inhibitor, KN-93, 30 min prior to the P infusion, in EB-primed, ovariectomized female rats inhibited CaMKII activation but not protein kinase A and protein kinase C activities. Interestingly, icv administration of KN-93 30 min prior to P infusion (icv) resulted in a reduction but not total inhibition of P-facilitated lordosis response in EB-primed female rats. These observations suggest a redundancy or, alternately, a hierarchy in the P-regulated activation of kinase signaling cascades in female reproductive behavior.

scholarly journals v-ras and protein kinase C dedifferentiate thyroid cells by down-regulating nuclear cAMP-dependent protein kinase A.

1992 ◽  
Vol 6 (9) ◽  
pp. 1621-1630 ◽  
Author(s):  
A Gallo ◽  
E Benusiglio ◽  
I M Bonapace ◽  
A Feliciello ◽  
S Cassano ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Dependent Protein Kinase ◽  
Thyroid Cells ◽  
Camp Dependent Protein Kinase ◽  
Kinase C ◽  
Dependent Protein ◽  
Kinase A

Novel indolocarbazole protein kinase C inhibitors prevent reactivation of HIV-1 in latently infected cells

1993 ◽  
Vol 22 (4) ◽  
pp. 273-283 ◽  
Author(s):  
Susanne Pätzold ◽  
Josef Schneider ◽  
Claus Rudolph ◽  
Dieter Marme ◽  
Christoph Schächtele
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase C Inhibitors ◽  
Kinase C ◽  
Latently Infected ◽  
Infected Cells ◽  
Hiv 1

Distinct voltage-dependent regulation of a heart-delayed IK by protein kinases A and C

1991 ◽  
Vol 261 (6) ◽  
pp. C1081-C1090 ◽  
Author(s):  
K. B. Walsh ◽  
R. S. Kass
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Dependent Protein Kinase ◽  
Kinase C ◽  
Voltage Dependent ◽  
Dependent Protein ◽  
Kinetics Of ◽  
Kinase A ◽  
Stimulation Of

We have investigated the effects of stimulation of adenosine 3',5'-cyclic monophosphate-dependent protein kinase (protein kinase A) and Ca(2+)-diacylglycerol-dependent protein kinase (protein kinase C) on the delayed rectifier K+ current (IK) in guinea pig ventricular cells using a whole cell arrangement of the patch-clamp procedure. Stimulation of either protein kinase C or A resulted in enhanced IK activity. Augmentation of IK observed during stimulation of protein kinase A occurred in a markedly voltage-dependent manner, with the largest increases occurring at potentials near the threshold for IK activation. Enhancement of IK during stimulation of protein kinase C followed a different pattern, with minimal effects of the enzyme near IK threshold. Neither protein kinase A nor C altered the kinetics of IK activation, although both kinases slightly changed the kinetics of deactivation. Both kinases increased IK maximal conductance, but the effects of each kinase on the voltage-dependence of activation differed. Protein kinase A shifted IK activation toward more negative voltages but did not affect the slope of the activation curve. Protein kinase C, in contrast, changed the slope of the IK activation curve, with only a small effect on the half-maximal voltage of activation. These contrasting effects on the voltage dependence of IK activation are consistent with actions of the kinases at distinct sites on or near the IK channel protein.

Regulation of the renal Na-HCO3 cotransporter by cAMP and Ca-dependent protein kinases

1992 ◽  
Vol 262 (4) ◽  
pp. F560-F565 ◽  
Author(s):  
O. S. Ruiz ◽  
J. A. Arruda
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinases ◽  
Inhibitory Effect ◽  
Dependent Protein Kinase ◽  
Basolateral Membranes ◽  
Kinase C ◽  
Dependent Protein ◽  
22Na Uptake ◽  
Kinase A

Changes in the activity of the brush-border Na-H antiporter are accompanied by parallel changes in the activity of the Na-HCO3 cotransporter. Adenosine 3',5'-cyclic monophosphate (cAMP) and calmodulin inhibit the Na-H antiporter, whereas protein kinase C (PKC) stimulates it. We hypothesized that cAMP, calmodulin, and PKC should have similar effects on the Na-HCO3 cotransporter activity. Phosphorylated renal basolateral membranes were treated with either cAMP, calmodulin, or phorbol ester. cAMP, 1 microM, inhibited HCO3-dependent 22Na uptake without affecting 22Na uptake in presence of gluconate, suggesting that cAMP inhibits Na-HCO3 cotransporter activity without altering diffusive 22Na uptake. The effect of cAMP to inhibit the Na-HCO3 cotransporter could also be elicited by the catalytic subunit of cAMP, and this inhibitory effect was prevented by the protein kinase A (PKA) inhibitor. Calmodulin (1 microM), in presence of Ca, also inhibited HCO3-dependent 22Na uptake in presence of HCO3, whereas 22Na uptake in the presence of gluconate was unchanged. The inhibitory effect of calmodulin on HCO3-dependent 22Na uptake was prevented by N-(4-aminobutyl)-5-chloro-2-naphthalene sulfonamide (W-13), an inhibitor of calmodulin. Phorbol 12-myristate 13-acetate and PKC stimulated Na-HCO3 cotransporter activity, whereas the inactive analogue, 4 alpha-phorbol, failed to elicit such a stimulation. Basolateral membranes displayed cAMP-dependent and Ca-dependent protein kinase activities. Thus PKA and Ca-dependent protein kinases regulate the activity of the Na-HCO3 cotransporter and suggest that hormones that act through these systems modulate the activity of the Na-HCO3 cotransporter.

scholarly journals Synthetic Ingenols Maximize Protein Kinase C-Induced HIV-1 Latency Reversal

2018 ◽  
Vol 62 (11) ◽  
Author(s):  
Adam M. Spivak ◽  
Racheal A. Nell ◽  
Mark Petersen ◽  
Laura Martins ◽  
Paul Sebahar ◽  
...  
Keyword(s):  
T Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Hydroxyl Group ◽  
Cellular Activation ◽  
Reversal Agents ◽  
Kinase C ◽  
Latently Infected ◽  
Infected Cells ◽  
Hiv 1

ABSTRACT Antiretroviral therapy (ART) does not cure HIV-1 infection due to the persistence of proviruses in long-lived resting T cells. Strategies targeting these latently infected cells will be necessary to eradicate HIV-1 in infected individuals. Protein kinase C (PKC) activation is an effective mechanism to reactivate latent proviruses and allows for recognition and clearance of infected cells by the immune system. Several ingenol compounds, naturally occurring PKC agonists, have been described to have potent latency reversal activity. We sought to optimize this activity by synthesizing a library of novel ingenols via esterification of the C-3 hydroxyl group of the ingenol core, which itself is inactive for latency reversal. Newly synthesized ingenol derivatives were evaluated for latency reversal activity, cellular activation, and cytotoxicity alongside commercially available ingenols (ingenol-3,20-dibenzoate, ingenol 3-hexanoate, and ingenol-3-angelate) in HIV latency cell lines and resting CD4+ T cells from aviremic participants. Among the synthetic ingenols that we produced, we identified several compounds that demonstrate high efficacy and represent promising leads as latency reversal agents for HIV-1 eradication.

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