Ontogenetic differences in energy metabolism and inhibition of protein synthesis in hippocampal slices during in vitro ischemia and 24 h of recovery

1996 ◽  
Vol 91 (2) ◽  
pp. 281-291 ◽  
Author(s):  
Richard Berger ◽  
Bogdan Djuricic ◽  
Arne Jensen ◽  
Konstantin Alexander Hossmann ◽  
Wulf Paschen
Keyword(s):  
Protein Synthesis ◽  
Energy Metabolism ◽  
Hippocampal Slices ◽  
In Vitro Ischemia ◽  
Inhibition Of Protein Synthesis

scholarly journals Inhibition of protein synthesis in vitro by procollagen-derived fragments is associated with changes in protein phosphorylation.

1982 ◽  
Vol 257 (15) ◽  
pp. 8557-8560 ◽  
Author(s):  
J M McPherson ◽  
D Hörlein ◽  
D Abbott-Brown ◽  
P Bornstein
Keyword(s):  
Protein Synthesis ◽  
Protein Phosphorylation ◽  
Inhibition Of Protein Synthesis

The Effects of Juvenile Hormone on Imaginal Discs of Drosophila In Vitro: The Role of the Inhibition of Protein Synthesis

1976 ◽  
pp. 432-448 ◽  
Author(s):  
J. W. Fristrom ◽  
C. J. Chihara ◽  
L. Kelly ◽  
J. T. Nishiura
Keyword(s):  
Protein Synthesis ◽  
Juvenile Hormone ◽  
Imaginal Discs ◽  
Inhibition Of Protein Synthesis

Extrusion of Intracellular Calcium Ion After In Vitro Ischemia in the Rat Hippocampal CA1 Region

2002 ◽  
Vol 88 (2) ◽  
pp. 879-887 ◽  
Author(s):  
E. Tanaka ◽  
H. Uchikado ◽  
S. Niiyama ◽  
K. Uematsu ◽  
H. Higashi
Keyword(s):  
Glial Cells ◽  
Hippocampal Slices ◽  
Negative Potential ◽  
Acetoxymethyl Ester ◽  
Rapid Reduction ◽  
In Vitro Ischemia ◽  
Ca1 Region ◽  
Dc Potential ◽  
Slow Negative Potential

Simultaneous recordings of intracellular Ca2+([Ca2+]i) signal and extracellular DC potential were obtained from the CA1 region in 1-[6-amino-2-(5-carboxy-2-oxazolyl)-5-benzofuranyloxy]-2-(2-amino-5-methylphenoxy)-ethane- N, N, N′, N′-tetraacetic acid penta-acetoxymethyl ester (Fura-2/AM)-loaded rat hippocampal slices. Superfusion with oxygen- and glucose-deprived medium (in vitro ischemia) for 5–6 min produced a rapid rise of the [Ca2+]i level in the stratum radiatum (rising phase of the [Ca2+]i signal), which occurred simultaneously with a rapid negative DC potential (rapid negative potential). When oxygen and glucose were reintroduced, the increased [Ca2+]i signal diminished rapidly (falling phase of the [Ca2+]i signal) during the generation of a slow negative DC potential (slow negative potential), which occurred within 1 min from the onset of the reintroduction. Thereafter, the [Ca2+]i signal partially and the slow negative potential completely returned to the preexposure level approximately 6 min after the reintroduction. The changes in [Ca2+]i signal during and after in vitro ischemia were very similar to the changes in the membrane potential of glial cells. The rising and falling phases of [Ca2+]i signal corresponded to the rapid depolarization and a depolarizing hump, respectively, in the repolarizing phase of glial cells. A prolonged application of in vitro ischemia or a reintroduction of either glucose or oxygen suppressed the falling phase after ischemic exposure. The application of ouabain (30 μM) generated both a rapid negative potential and a rapid elevation of [Ca2+]i, but no slow negative potential or rapid reduction in [Ca2+]i were observed. When oxygen and glucose were reintroduced to slices in the Na+-free or ouabain- or Ni2+-containing medium, the falling phase was suppressed. The falling phase was significantly accelerated in Ca2+- and Mg2+-free with EGTA-containing medium. In contrast, the falling phase was significantly slower in the Ca2+-free with high Mg2+- and EGTA-containing medium. The falling phase of the [Ca2+]isignal after ischemic exposure is thus considered to be primarily dependent on the reactivation of Na+, K+-ATPases, while the extrusion of cytosolic Ca2+ via the forward-mode operation of Na+/Ca2+ exchangers in glial cells is thought to be directly involved in the rapid reduction of [Ca2+]i after ischemic exposure.

scholarly journals Glucocorticoid inhibition of protein synthesis in vivo and in vitro.

1975 ◽  
Vol 250 (6) ◽  
pp. 2293-2298
Author(s):  
YS Kim ◽  
Y Kim
Keyword(s):  
Protein Synthesis ◽  
Inhibition Of Protein Synthesis

Origin of intracellular Ca2+ elevation induced by in vitro ischemia-like condition in hippocampal slices

1993 ◽  
Vol 601 (1-2) ◽  
pp. 103-110 ◽  
Author(s):  
Akira Mitani ◽  
Hisato Yanase ◽  
Kimiko Sakai ◽  
Youseke Wake ◽  
Kiyoshi Kataoka
Keyword(s):  
Hippocampal Slices ◽  
In Vitro Ischemia

scholarly journals Studies on valinomycin inhibition of synaptosome-fraction protein synthesis

1981 ◽  
Vol 196 (1) ◽  
pp. 25-32 ◽  
Author(s):  
M A Verity ◽  
M K Cheung ◽  
W J Brown
Keyword(s):  
Protein Synthesis ◽  
Respiratory Control ◽  
Microsomal Protein ◽  
Mitochondrial Oxidative Phosphorylation ◽  
Subsequent Decrease ◽  
High K ◽  
Rapid Fall ◽  
Inhibition Of Protein Synthesis ◽  
External K

The ionophore valinomycin inhibited adult and neonatal synaptosome fraction protein synthesis with half-maximal inhibition at approximately 10nM. Valinomycin had no effect on [3H]leucine uptake into synaptosomes at high or low external [K+]. Synaptosome-fraction protein synthesis was dependent on [K+]e reaching a maximum at 25mM-K+. Valinomycin inhibition of protein synthesis was not reversed at high [K+]e. Valinomycin failed to influence the intrasynaptosomal [K+] even at zero [K+]e. A significant increase in State-4 respiration of synaptosomal fractions was found at 5nM-valinomycin with a decrease in the respiratory control index. At these concentrations of valinomycin there was no inhibition of the ADP-stimulated (State 3) respiration rate. Valinomycin had no effect on cerebral microsomal protein synthesis in vitro, which was inhibited by puromycin (100 micrograms/ml) or the absence of ATP. Valinomycin, 2,4-dinitrophenol and KCN inhibition of protein synthesis was not reversed by added ATP, suggesting impermeability of the membrane to ATP. Valinomycin induced a rapid fall in synaptosome ATP content not observed with atractylate or ouabain. Valinomycin inhibition of protein synthesis under these conditions is secondary to uncoupling of mitochondrial oxidative phosphorylation with a subsequent decrease in intraterminal ATP necessary for translation.

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