scholarly journals The Cyclin-Dependent Kinase 5 Activators p35 and p39 Interact with the α-Subunit of Ca2+/Calmodulin-Dependent Protein Kinase II and α-Actinin-1 in a Calcium-Dependent Manner

2002 ◽  
Vol 22 (18) ◽  
pp. 7879-7891 ◽  
Author(s):  
Rani Dhavan ◽  
Paul L. Greer ◽  
Maria A. Morabito ◽  
Lianna R. Orlando ◽  
Li-Huei Tsai
Keyword(s):  
Protein Kinase ◽  
Dependent Manner ◽  
Cyclin Dependent Kinase ◽  
Dependent Protein Kinase ◽  
Α Subunit ◽  
Calcium Dependent ◽  
Protein Kinase Ii ◽  
Dependent Protein ◽  
Cyclin Dependent Kinase 5

Enhanced activation of Ca2+/Calmodulin-dependent protein kinase II upon downregulation of cyclin-dependent kinase 5-p35

2006 ◽  
Vol 84 (4) ◽  
pp. 747-754 ◽  
Author(s):  
Tomohisa Hosokawa ◽  
Taro Saito ◽  
Akiko Asada ◽  
Toshio Ohshima ◽  
Makoto Itakura ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cyclin Dependent Kinase ◽  
Dependent Protein Kinase ◽  
Protein Kinase Ii ◽  
Dependent Protein ◽  
Cyclin Dependent Kinase 5

Calcium/calmodulin-dependent protein kinase II regulates IL-10 production by human T lymphocytes: A distinct target in the calcium dependent pathway

2012 ◽  
Vol 52 (2) ◽  
pp. 51-60 ◽  
Author(s):  
Stavroula Boubali ◽  
Kassiani Liopeta ◽  
Laura Virgilio ◽  
George Thyphronitis ◽  
George Mavrothalassitis ◽  
...  
Keyword(s):  
Protein Kinase ◽  
T Lymphocytes ◽  
Dependent Protein Kinase ◽  
Calcium Dependent ◽  
Human T Lymphocytes ◽  
Calcium Calmodulin Dependent ◽  
Protein Kinase Ii ◽  
Dependent Protein ◽  
Dependent Pathway

iNOS regulation by calcium/calmodulin-dependent protein kinase II in vascular smooth muscle

2007 ◽  
Vol 292 (6) ◽  
pp. H2634-H2642 ◽  
Author(s):  
Rachel J. Jones ◽  
David Jourd'heuil ◽  
John C. Salerno ◽  
Susan M. E. Smith ◽  
Harold A. Singer
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase ◽  
Vascular Smooth Muscle ◽  
Resting Cells ◽  
Dependent Manner ◽  
Dependent Protein Kinase ◽  
Cytokine Induction ◽  
Calcium Calmodulin Dependent ◽  
Protein Kinase Ii ◽  
Dependent Protein

Nitric oxide synthase (NOS) expression is regulated transcriptionally in response to cytokine induction and posttranslationally by palmitoylation and trafficking into perinuclear aggresome-like structures. We investigated the effects of multifunctional calcium/calmodulin-dependent protein kinase II protein kinase (CaMKII) on inducible NOS (iNOS) trafficking in cultured rat aortic vascular smooth muscle cells (VSMCs). Immunofluorescence and confocal microscopy demonstrated colocalization of iNOS and CaMKIIδ2 with a perinuclear distribution and concentration in aggresome-like structures identified by colocalization with γ-tubulin. Furthermore, CaMKIIδ2 coimmunoprecipitated with iNOS in a CaMKII activity-dependent manner. Addition of Ca2+-mobilizing stimuli expected to activate CaMKII; a purinergic agonist (UTP) or calcium ionophore (ionomycin) caused a general redistribution of iNOS from cytosolic to membrane and nuclear fractions. Similarly, adenoviral expression of a constitutively active CaMKIIδ2 mutant altered iNOS localization, shifting iNOS from the cytosolic fraction. Suppression of CaMKIIδ2 using an adenovirus expressing a short hairpin, small interfering RNA increased nuclear iNOS localization in resting cells but inhibited ionomycin-induced translocation of iNOS to the nucleus. Following addition of these chronic and acute CaMKII modulators, there were fewer aggresome-like structures containing iNOS. All of the treatments that chronically affected CaMKII activity or expression significantly inhibited iNOS-specific activity following cytokine induction. The results suggest that CaMKIIδ2 may be an important regulator of iNOS trafficking and activity in VSMCs.

scholarly journals Densin-180 Forms a Ternary Complex with the α-Subunit of Ca2+/Calmodulin-Dependent Protein Kinase II and α-Actinin

2001 ◽  
Vol 21 (2) ◽  
pp. 423-433 ◽  
Author(s):  
Randall S. Walikonis ◽  
Asako Oguni ◽  
Eugenia M. Khorosheva ◽  
Chung-Jiuan Jeng ◽  
Franklin J. Asuncion ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Ternary Complex ◽  
Dependent Protein Kinase ◽  
Α Subunit ◽  
Protein Kinase Ii ◽  
Dependent Protein

scholarly journals Conduction in the right and left ventricle is differentially regulated by protein kinases and phosphatases: implications for arrhythmogenesis

2019 ◽  
Vol 316 (6) ◽  
pp. H1507-H1527 ◽  
Author(s):  
Alexey V. Zaitsev ◽  
Natalia S. Torres ◽  
Keiko M. Cawley ◽  
Amira D. Sabry ◽  
Junco S. Warren ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Dependent Manner ◽  
Dependent Protein Kinase ◽  
Specific Expression ◽  
Stress Kinases ◽  
Calcium Calmodulin Dependent ◽  
Protein Kinase Ii ◽  
Dependent Protein ◽  
The Right ◽  
Ventricular Conduction

The “stress” kinases cAMP-dependent protein kinase (PKA) and calcium/calmodulin-dependent protein kinase II (CaMKII), phosphorylate the Na+ channel Nav1.5 subunit to regulate its function. However, how the channel regulation translates to ventricular conduction is poorly understood. We hypothesized that the stress kinases positively and differentially regulate conduction in the right (RV) and the left (LV) ventricles. We applied the CaMKII blocker KN93 (2.75 μM), PKA blocker H89 (10 μM), and broad-acting phosphatase blocker calyculin (30 nM) in rabbit hearts paced at a cycle length (CL) of 150-8,000 ms. We used optical mapping to determine the distribution of local conduction delays (inverse of conduction velocity). Control hearts exhibited constant and uniform conduction at all tested CLs. Calyculin (15-min perfusion) accelerated conduction, with greater effect in the RV (by 15.3%) than in the LV (by 4.1%; P < 0.05). In contrast, both KN93 and H89 slowed down conduction in a chamber-, time-, and CL-dependent manner, with the strongest effect in the RV outflow tract (RVOT). Combined KN93 and H89 synergistically promoted conduction slowing in the RV (KN93: 24.7%; H89: 29.9%; and KN93 + H89: 114.2%; P = 0.0016) but not the LV. The progressive depression of RV conduction led to conduction block and reentrant arrhythmias. Protein expression levels of both the CaMKII-δ isoform and the PKA catalytic subunit were higher in the RVOT than in the apical LV ( P < 0.05). Thus normal RV conduction requires a proper balance between kinase and phosphatase activity. Dysregulation of this balance due to pharmacological interventions or disease is potentially proarrhythmic. NEW & NOTEWORTHY We show that uniform ventricular conduction requires a precise physiological balance of the activities of calcium/calmodulin-dependent protein kinase II (CaMKII), PKA, and phosphatases, which involves region-specific expression of CaMKII and PKA. Inhibiting CaMKII and/or PKA activity elicits nonuniform conduction depression, with the right ventricle becoming vulnerable to the development of conduction disturbances and ventricular fibrillation/ventricular tachycardia.

Cytoskeletal-like Filaments of Ca2+-Calmodulin-Dependent Protein Kinase II Are Formed in a Regulated and Zn2+-Dependent Manner

Biochemistry ◽  
2017 ◽  
Vol 56 (15) ◽  
pp. 2149-2160 ◽  
Author(s):  
Laurel Hoffman ◽  
Lin Li ◽  
Emil Alexov ◽  
Hugo Sanabria ◽  
M. Neal Waxham
Keyword(s):  
Protein Kinase ◽  
Dependent Manner ◽  
Dependent Protein Kinase ◽  
Protein Kinase Ii ◽  
Dependent Protein

Guanylyl cyclase stimulatory coupling to KCachannels

2000 ◽  
Vol 279 (6) ◽  
pp. C1938-C1945 ◽  
Author(s):  
M. Nara ◽  
P. D. K. Dhulipala ◽  
G. J. Ji ◽  
U. R. Kamasani ◽  
Y.-X. Wang ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Protein Kinase ◽  
Guanylyl Cyclase ◽  
Phosphorylation Site ◽  
Nitric Oxide Donor ◽  
Dependent Manner ◽  
Dependent Protein Kinase ◽  
Α Subunit ◽  
Dependent Protein ◽  
Spermine Nonoate

We coexpressed the human large-conductance, calcium-activated K (KCa) channel (α- and β-subunits) and rat atrial natriuretic peptide (ANP) receptor genes in Xenopus oocytes to examine the mechanism of guanylyl cyclase stimulatory coupling to the channel. Exposure of oocytes to ANP stimulated whole cell KCa currents by 21 ± 3% (at 60 mV), without altering current kinetics. Similarly, spermine NONOate, a nitric oxide donor, increased KCa currents (20 ± 4% at 60 mV) in oocytes expressing the channel subunits alone. Stimulation of KCacurrents by ANP was inhibited in a concentration-dependent manner by a peptide inhibitor of cGMP-dependent protein kinase (PKG). Receptor/channel stimulatory coupling was not completely abolished by mutating the cAMP-dependent protein kinase phosphorylation site on the α-subunit (S869; Nars M, Dhulipals PD, Wang YX, and Kotlikoff MI. J Biol Chem 273: 14920–14924, 1998) or by mutating a neighboring consensus PKG site (S855), but mutation of both residues virtually abolished coupling. Spermine NONOate also failed to stimulate channels expressed from the double mutant cRNAs. These data indicate that nitric oxide donors stimulate KCa channels through cGMP-dependent phosphorylation and that two serine residues (855 and 869) underlie this stimulatory coupling.

scholarly journals Characterization of γ- and δ-subunits of Ca2+/calmodulin-dependent protein kinase II in rat gastric mucosal cell populations

1994 ◽  
Vol 297 (1) ◽  
pp. 157-162 ◽  
Author(s):  
P Mayer ◽  
M Möhlig ◽  
U Seidler ◽  
H Rochlitz ◽  
M Fährmann ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Signal Transmission ◽  
Specific Inhibitor ◽  
Protein Kinase Activity ◽  
Mucosal Cell ◽  
Specific Substrate ◽  
Dependent Manner ◽  
Dependent Protein Kinase ◽  
Protein Kinase Ii ◽  
Dependent Protein

We searched for the occurrence of a Ca2+/calmodulin-dependent protein kinase in rat gastric cell types as a likely member in the chain of gastrin- and muscarinic-receptor-mediated signal transmission. A Ca(2+)- and calmodulin-dependent phosphorylation of major 50, 60 and 100 kDa substrates was observed in parietal cell cytosol and a major 60 and 61 kDa protein doublet was found to bind 125I-calmodulin in 125I-calmodulin-gel overlays. A specific substrate of the multifunctional Ca2+/calmodulin-dependent protein kinase II, autocamtide II, was phosphorylated in a calmodulin-dependent manner. The specific inhibitor of this enzyme, KN-62, antagonized protein kinase activity. RNA extracted from gastric mucosal cells was shown to contain sequences of the gamma- and delta- but not alpha- and beta-subunits of the calmodulin-dependent kinase II, and mRNA of both subtypes was demonstrated in highly purified parietal, chief and mucous cells. A calmodulin-dependent kinase II composed of gamma- and delta-subunits is a likely mediator of Ca(2+)-dependent signal transmission in these populations of gastric cells.

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