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Stimulation of the Plasma Membrane Na+/H+ Exchanger NHE1 by Sustained Intracellular Acidosis
- R. Haworth, Caroline McCann, A. K. Snabaitis, Neil A Roberts, M. Avkiran
- Medicine, BiologyJournal of Biological Chemistry
- 22 August 2003
The data suggest that the stimulatory effect of sustained intracellular acidosis occurs through a novel mechanism mediated by activation of the ERK pathway and NHE stimulatory effects of sustained acidosis were observed in adult rat ventricular myocytes and COS-7 cells.
Expression and activity of protein kinase D/protein kinase C mu in myocardium: evidence for alpha1-adrenergic receptor- and protein kinase C-mediated regulation.
- R. Haworth, M. W. Goss, E. Rozengurt, M. Avkiran
- Biology, MedicineJournal of molecular and cellular cardiology
- 1 June 2000
Protein kinase D is expressed in rat ventricular myocardium, where its expression is subject to developmental control, and that PKD activity in Ventricular myocytes is regulated through alpha1-AR- and PKC-mediated pathways.
Ca2+/Calmodulin-Dependent Protein Kinase II&dgr; and Protein Kinase D Overexpression Reinforce the Histone Deacetylase 5 Redistribution in Heart Failure
- Julie Bossuyt, K. Helmstadter, +6 authors D. Bers
- Biology, MedicineCirculation research
- 28 March 2008
Chronic upregulation and activation of inositol trisphosphate receptors, CaMKII, and PKD in HF shifts HDAC5 out of the nucleus, derepressing transcription of hypertrophic genes, which may directly contribute to the development and/or maintenance of HF.
Protein kinase d in the cardiovascular system: emerging roles in health and disease.
A primer on PKD signaling is provided, using information gained from studies in multiple cell types, and recent data that suggest novel functions for PKD-mediated pathways in the heart and the circulation are discussed.
Protein Kinase D Selectively Targets Cardiac Troponin I and Regulates Myofilament Ca2+ Sensitivity in Ventricular Myocytes
- F. Cuello, Sonya C. Bardswell, +6 authors M. Avkiran
- Biology, MedicineCirculation research
- 30 March 2007
It is concluded that increased myocardial PKD activity induces cardiac troponin I phosphorylation at Ser22/Ser23 and reduces myofilament Ca2+ sensitivity, suggesting that altered PKDActivity in disease may impact on contractile function.
Activation of p38 mitogen-activated protein kinase contributes to the early cardiodepressant action of tumor necrosis factor.
- M. Bellahcene, S. Jacquet, +10 authors M. Marber
- MedicineJournal of the American College of Cardiology
- 1 August 2006
Tumor necrosis factor activates p38-MAPK in the intact heart and in isolated cardiac myocytes through MKK3, and this activation likely contributes to the early cardiodepressant action of TNFalpha.
The ERK pathway regulates Na(+)-HCO(3)(-) cotransport activity in adult rat cardiomyocytes.
- D. Baetz, R. Haworth, M. Avkiran, D. Feuvray
- Chemistry, MedicineAmerican journal of physiology. Heart and…
- 1 November 2002
The MAPK(ERK)-dependent pathway facilitates the rate of pH(i) recovery from acid load through NBC activity and is involved in the AT(1) receptor-mediated stimulation of such activity by ANG II.
Effects of bisindolylmaleimide PKC inhibitors on p90RSK activity in vitro and in adult ventricular myocytes
These data show that GF109203X and Ro31‐8220 inhibit various isoforms of PKC and p90RSK in vitro and in intact ARVM, with the former agent exhibiting relatively greater selectivity for PKC.
Protein Kinase D Is a Novel Mediator of Cardiac Troponin I Phosphorylation and Regulates Myofilament Function
- R. Haworth, F. Cuello, +4 authors M. Avkiran
- Chemistry, MedicineCirculation research
- 26 November 2004
The data suggest that PKD is a novel mediator of cTnI phosphorylation at the PKA sites and may contribute to the regulation of myofilament function.
Inhibition of protein kinase D by resveratrol.
It is confirmed that the activity of PKD is indeed inhibited in vitro by resveratrol, and its value as a selective tool to investigate the cellular function(s) ofPKD is questionable.