The intrinsic ATPase activity of protein kinase C is catalyzed at the active site of the enzyme

Biochemistry ◽  
1992 ◽  
Vol 31 (25) ◽  
pp. 5905-5911 ◽  
Author(s):  
Nancy E. Ward ◽  
Catherine A. O'Brian
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Atpase Activity ◽  
Active Site ◽  
Kinase C

scholarly journals Protein kinase C-α inhibits the repair of oxidative phosphorylation after S-(1,2-dichlorovinyl)-l-cysteine injury in renal cells

2004 ◽  
Vol 287 (1) ◽  
pp. F64-F73 ◽  
Author(s):  
Xiuli Liu ◽  
Malinda L. Godwin ◽  
Grażyna Nowak
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Oxidative Phosphorylation ◽  
Atpase Activity ◽  
Mitochondrial Function ◽  
Recovery Period ◽  
Β Subunit ◽  
Atp Production ◽  
Kinase C ◽  
Mitochondrial Functions

Previously, we showed that physiological functions of renal proximal tubular cells (RPTC) do not recover following S-(1,2-dichlorovinyl)-l-cysteine (DCVC)-induced injury. This study investigated the role of protein kinase C-α (PKC-α) in the lack of repair of mitochondrial function in DCVC-injured RPTC. After DCVC exposure, basal oxygen consumption (Qo2), uncoupled Qo2, oligomycin-sensitive Qo2, F1F0-ATPase activity, and ATP production decreased, respectively, to 59, 27, 27, 57, and 68% of controls. None of these functions recovered. Mitochondrial transmembrane potential decreased 53% after DCVC injury but recovered on day 4. PKC-α was activated 4.3- and 2.5-fold on days 2 and 4, respectively, of the recovery period. Inhibition of PKC-α activation (10 nM Go6976) did not block DCVC-induced decreases in mitochondrial functions but promoted the recovery of uncoupled Qo2, oligomycin-sensitive Qo2, F1F0-ATPase activity, and ATP production. Protein levels of the catalytic β-subunit of F1F0-ATPase were not changed by DCVC or during the recovery period. Amino acid sequence analysis revealed that α-, β-, and ε-subunits of F1F0-ATPase have PKC consensus motifs. Recombinant PKC-α phosphorylated the β-subunit and decreased F1F0-ATPase activity in vitro. Serine but not threonine phosphorylation of the β-subunit was increased during late recovery following DCVC injury, and inhibition of PKC-α activation decreased this phosphorylation. We conclude that during RPTC recovery following DCVC injury, 1) PKC-α activation decreases F0F1-ATPase activity, oxidative phosphorylation, and ATP production; 2) PKC-α phosphorylates the β-subunit of F1F0-ATPase on serine residue; and 3) PKC-α does not mediate depolarization of RPTC mitochondria. This is the first report showing that PKC-α phosphorylates the catalytic subunit of F1F0-ATPase and that PKC-α plays an important role in regulating repair of mitochondrial function.

Endothelin stimulates Na(+)-K(+)-ATPase activity by a protein kinase C-dependent pathway in rabbit aorta

1991 ◽  
Vol 261 (1) ◽  
pp. H38-H45 ◽  
Author(s):  
S. Gupta ◽  
N. B. Ruderman ◽  
E. J. Cragoe ◽  
I. Sussman
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Atpase Activity ◽  
Rabbit Aorta ◽  
Effective Concentration ◽  
Kinase C ◽  
Exchange Inhibitor ◽  
Half Maximal Effective Concentration ◽  
Dependent Pathway ◽  
Stimulation Of

Incubation with endothelin (Endo) caused a time- and concentration-dependent increase in both ouabain-sensitive (OS) and ouabain-insensitive (OI) 86Rb+ uptake [half-maximal effective concentration (EC50) for OS component = 11 nM] in the rabbit aorta. Increase in the OS component [Na(+)-K(+)-adenosine triphosphatase (ATPase) activity] accounted for 70% of the 110% increase in total 86Rb+ uptake at a maximally effective concentration of Endo (100 nM). Protein kinase C (PKC) activator phorbol 12,13-dibutyrate (PDBU; 100 nM) increased total 86Rb+ uptake by 69%, with 42% of the increase in the OS component. Stimulation by Endo and PDBU was not additive. Staurosporine (STA; 100 nM) inhibited stimulation of total 86Rb+ uptake by Endo and PDBU by approximately 60%. With ouabain and STA added together, inhibition of Endo-stimulated total 86Rb+ uptake (90%) was greater than with either agent alone, suggesting that STA inhibits an OS as well as an OI component of 86Rb+ uptake. Stimulation of total 86Rb+ uptake by both Endo and PDBU were also inhibited by approximately 60% by the Na(+)-H+ exchange inhibitor 5-(N-ethyl-N-isopropyl)amiloride (EIPA). Endo-stimulated total 86Rb+ uptake was not further inhibited when ouabain was added together with EIPA, suggesting that Na(+)-H+ exchange is primarily linked to the OS component of 86Rb+ uptake. In contrast, Na(+)-K(+)-Cl- cotransport inhibitor bumetanide inhibited increases in total 86Rb+ uptake caused by Endo (30%) and PDBU (56%) due solely to its effects on OI 86Rb+ uptake. Results suggest that Endo stimulates Na(+)-K(+)-ATPase activity in rabbit aorta by activating PKC and Na(+)-H+ exchange.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Aldosterone stimulates vacuolar H+-ATPase activity in renal acid-secretory intercalated cells mainly via a protein kinase C-dependent pathway

2011 ◽  
Vol 301 (5) ◽  
pp. C1251-C1261 ◽  
Author(s):  
Christian Winter ◽  
Nicole B. Kampik ◽  
Luca Vedovelli ◽  
Florina Rothenberger ◽  
Teodor G. Păunescu ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Atpase Activity ◽  
Intracellular Signaling ◽  
Collecting Duct ◽  
Intercalated Cells ◽  
Nongenomic Action ◽  
Kinase C ◽  
Urinary Acidification ◽  
Stimulation Of

Urinary acidification in the collecting duct is mediated by the activity of H+-ATPases and is stimulated by various factors including angiotensin II and aldosterone. Classically, aldosterone effects are mediated via the mineralocorticoid receptor. Recently, we demonstrated a nongenomic stimulatory effect of aldosterone on H+-ATPase activity in acid-secretory intercalated cells of isolated mouse outer medullary collecting ducts (OMCD). Here we investigated the intracellular signaling cascade mediating this stimulatory effect. Aldosterone stimulated H+-ATPase activity in isolated mouse and human OMCDs. This effect was blocked by suramin, a general G protein inhibitor, and GP-2A, a specific Gαq inhibitor, whereas pertussis toxin was without effect. Inhibition of phospholipase C with U-73122, chelation of intracellular Ca2+ with BAPTA, and blockade of protein kinase C prevented the stimulation of H+-ATPases. Stimulation of PKC by DOG mimicked the effect of aldosterone on H+-ATPase activity. Similarly, aldosterone and DOG induced a rapid translocation of H+-ATPases to the luminal side of OMCD cells in vivo. In addition, PD098059, an inhibitor of ERK1/2 activation, blocked the aldosterone and DOG effects. Inhibition of PKA with H89 or KT2750 prevented and incubation with 8-bromoadenosine-cAMP mildly increased H+-ATPase activity. Thus, the nongenomic modulation of H+-ATPase activity in OMCD-intercalated cells by aldosterone involves several intracellular pathways and may be mediated by a Gαq protein-coupled receptor and PKC. PKA and cAMP appear to have a modulatory effect. The rapid nongenomic action of aldosterone may participate in the regulation of H+-ATPase activity and contribute to final urinary acidification.

Protein kinase C-dependent phosphorylation of Na(+)-K(+)-ATPase alpha-subunit in rat kidney cortical tubules

1996 ◽  
Vol 271 (1) ◽  
pp. C136-C143 ◽  
Author(s):  
M. L. Carranza ◽  
E. Feraille ◽  
H. Favre
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Atpase Activity ◽  
Rat Kidney ◽  
Cation Transport ◽  
Dose Dependence ◽  
Alpha Subunit ◽  
Transport Activity ◽  
Kinase C ◽  
Gf 109203X

We have previously shown that, in oxygenated rat kidney proximal convoluted tubules (PCT), activation of protein kinase C (PKC) by phorbol 12,13-dibutyrate (PDBu) directly stimulates Na(+)-K(+)-adenosinetriphosphatase (ATPase) activity. PKC modulation of Na(+)-K(+)-ATPase activity by phosphorylation of its alpha-subunit was the postulated mechanism. The present study was therefore designed to investigate the relationship between PKC-mediated phosphorylation of the catalytic alpha-subunit and the cation transport activity of the Na(+)-K(+)-ATPase. In a suspension of rat kidney cortical tubules, activation of PKC by 10(-7) M PDBu increased the level of phosphorylation of the Na(+)-K(+)-ATPase alpha-subunit and stimulated the ouabain-sensitive 86Rb uptake by 47 and 42%, respectively. Time and dose dependence of the PDBu-induced increase in Na(+)-K(+)-ATPase activity and phosphorylation was strongly linearly correlated. The effects of PDBu on phosphorylation and activity of Na(+)-K(+)-ATPase were prevented by GF-109203X, a specific PKC inhibitor, whereas H-89, a specific PKA inhibitor, was ineffective. These results demonstrate that PKC activation induces phosphorylation of the catalytic alpha-subunit of Na(+)-K(+)-ATPase, which may participate in the stimulation of its cation transport activity in the rat PCT.

Leishmania amazonensis: Heme stimulates (Na++K+)ATPase activity via phosphatidylinositol-specific phospholipase C/protein kinase C-like (PI-PLC/PKC) signaling pathways

2010 ◽  
Vol 124 (4) ◽  
pp. 436-441 ◽  
Author(s):  
Elmo Eduardo Almeida-Amaral ◽  
Viviane Carrozino Cardoso ◽  
Fernanda Gomes Francioli ◽  
José Roberto Meyer-Fernandes
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Atpase Activity ◽  
Signaling Pathways ◽  
Phospholipase C ◽  
Leishmania Amazonensis ◽  
C Protein ◽  
Kinase C ◽  
Pkc Signaling
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