Basic FGF Enhances Calcium Permeable Channel Openings in Adult Rat Cardiac Myocytes: Implication in the bFGF-induced Increase of Free Ca2+Content

1997 ◽  
Vol 29 (10) ◽  
pp. 2687-2698 ◽  
Author(s):  
Pierre-Laurent Merle ◽  
Yves Usson ◽  
Michel Robert-Nicoud ◽  
Jean Verdetti
Keyword(s):  
Cardiac Myocytes ◽  
Basic Fgf ◽  
Permeable Channel ◽  
Adult Rat ◽  
Rat Cardiac Myocytes

scholarly journals Down-Regulation of Replication Factor C-40 (RFC40) Causes Chromosomal Missegregation in Neonatal and Hypertrophic Adult Rat Cardiac Myocytes

PLoS ONE ◽  
2012 ◽  
Vol 7 (6) ◽  
pp. e39009 ◽  
Author(s):  
Hirotaka Ata ◽  
Deepa Shrestha ◽  
Masahiko Oka ◽  
Rikuo Ochi ◽  
Chian Ju Jong ◽  
...  
Keyword(s):  
Cardiac Myocytes ◽  
Replication Factor C ◽  
Down Regulation ◽  
Replication Factor ◽  
Adult Rat ◽  
Factor C ◽  
Rat Cardiac Myocytes

Effect of Napip on K0 activation of the Na-K pump in adult rat cardiac myocytes

1994 ◽  
Vol 266 (1) ◽  
pp. C37-C41 ◽  
Author(s):  
T. A. Kinard ◽  
X. Y. Liu ◽  
S. Liu ◽  
J. R. Stimers
Keyword(s):  
Environmental Factors ◽  
Cardiac Myocytes ◽  
Pump Current ◽  
Apparent Affinity ◽  
Adult Rat ◽  
Cyclic Model ◽  
Pump Activity ◽  
Dose Dependent ◽  
Rat Cardiac Myocytes ◽  
External K

To determine if environmental factors influence the external K (K0) dependence of Na-K pump current (Ip), we systematically varied internal (pipette) Na (Napip) and Na-K pump activity while measuring the K0 dependence in adult rat cardiac myocytes. For each Napip, reactivation of Ip by K0 was dose dependent. The maximal Ip (Ipmax) and apparent affinity for K0 binding to the Na-K pump (K0.5) increased as Napip increased. The results of making an equimolar substitution of tetramethylammonium for K and Cs, and partial Ip inhibition with ouabain, also showed that Ipmax and K0.5 increased as Napip increased. We simulated pump activity as a function of intracellular Na (Nai) and K0 using a cyclic model of the Na-K pump and found that the model predicts K0.5 for K0 binding increases as Na increases, even when the conditions are adjusted by removing pipette K and partial pump inhibition with ouabain.

Effects of Saponin Monomer 13 of Dwarf Lilyturf Tuber on L-Type Calcium Currents in Adult Rat Ventricular Myocytes

2005 ◽  
Vol 33 (05) ◽  
pp. 797-806 ◽  
Author(s):  
Jin Tao ◽  
Hongyi Wang ◽  
Jiandong Chen ◽  
Huae Xu ◽  
Shengnan Li
Keyword(s):  
Cardiac Myocytes ◽  
Ventricular Myocytes ◽  
Calcium Currents ◽  
Inhibitory Effects ◽  
Patch Clamp Recording ◽  
Inactivation Curve ◽  
Control Value ◽  
Adult Rat ◽  
Cardioprotective Effects ◽  
Rat Cardiac Myocytes

The saponin monomer 13 of dwarf lilyturf tuber (DT-13), one of the saponin monomers of dwarf lilyturf tuber, has been found to have potent cardioprotective effects. In order to investigate the effect of DT-13 on L-type calcium currents ( I Ca,L ), exploring the mechanisms of DT-13's cardioprotective effects, we directly measured the I Ca,L in the adult rat cardiac myocytes exposed to DT-13 using standard whole-cell patch-clamp recording technique. Our results showed that DT-13 exerted inhibitory effects on the I Ca,L of the single adult rat cardiac myocytes. The current density was reduced by about 38% after exposure of the cells to DT-13 (0.1 μM) for 10 minutes, from the control value of 7.46 ± 1.31 pA/pF to 4.25 ± 0.35 pA/pF ( n = 6, p < 0.05). This I Ca,L -inhibiting action of DT-13 was concentration-dependent. DT-13 up-shifted the current-voltage (I-V) curve, but did not significantly affect the half activation potential (V0.5). V0.5 was from -11.8 ± 0.9 mV in the control to -12.6 ± 1.9 mV in the presence of DT-13 at 0.1 μmol/L. DT-13 at 0.1 μM did not markedly affect the activation of I Ca,L , but shifted the inactivation curve of I Ca,L to the left. In combination with previous reports, these results suggest that there might be a close relationship between the cardioprotective effects of dwarf lilyturf tuber and the inhibitory effects of DT-13 on L-type calcium currents.

Oxidation of myoglobin in isolated adult rat cardiac myocytes by 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid

FEBS Letters ◽  
1983 ◽  
Vol 163 (2) ◽  
pp. 292-296 ◽  
Author(s):  
Frederick P. Walters ◽  
Frances G. Kennedy ◽  
Dean P. Jones
Keyword(s):  
Cardiac Myocytes ◽  
Eicosatetraenoic Acid ◽  
Adult Rat ◽  
Rat Cardiac Myocytes

scholarly journals Phosphorylation and activation of mitogen- and stress-activated protein kinase-1 in adult rat cardiac myocytes by G-protein-coupled receptor agonists requires both extracellular-signal-regulated kinase and p38 mitogen-activated protein kinase

2002 ◽  
Vol 365 (3) ◽  
pp. 757-763 ◽  
Author(s):  
Thomais MARKOU ◽  
Antigone LAZOU
Keyword(s):  
Protein Kinase ◽  
G Protein ◽  
Cardiac Myocytes ◽  
P38 Mapk ◽  
Mitogen Activated Protein Kinase ◽  
G Protein Coupled Receptor ◽  
Receptor Agonists ◽  
Adult Rat ◽  
G Protein Coupled ◽  
Rat Cardiac Myocytes

G-protein-coupled receptor agonists are powerful stimulators of mitogen-activated protein kinase (MAPK) cascades in cardiac myocytes. However, little is known regarding the physiological activation of enzymes downstream of MAPKs. We examined the activation of mitogen- and stress-activated protein kinase-1 (MSK1), a downstream target of MAPKs, in adult rat cardiac myocytes by phenylephrine and endothelin-1. Both agonists induced the phosphorylation of MSK1 at Thr-581 and Ser-376 but not at Ser-360. Maximal phosphorylation was observed at 10–15min after stimulation and it correlated with increased activity. Maximal activation of MSK1 in adult cardiomyocytes temporally coincided with maximal p38 MAPK activation while activation of the extracellular-signal-regulated kinase (ERK) cascade was more rapid. Phosphorylation and activation of MSK1 was completely inhibited by either PD98059 (ERK1/2 pathway inhibitor) or SB203580 (p38 MAPK inhibitor) alone. These data demonstrate that MSK1 activation in adult rat cardiac myocytes by G-protein-coupled receptor agonists requires the simultaneous activation of both the ERK and p38 MAPK pathways. However, the lack of phosphorylation at Ser-360, an identified phosphorylation site targeted by MAPKs, may indicate that MSK1 is not a direct substrate of ERK1/2 and p38 MAPK in adult rat cardiomyocytes.

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