Drugs online research references
J Pharmacol Exp Ther. 1980 Nov;215(2):455-60.
A comparative study of the pharmacological properties of the positive potential recorded from the superior cervical ganglia of several species.
Dun NJ, Karczmar AG.
Sucrose gap recording technique was employed to record surface potentials from superior cervical ganglia (SCGs) of several species. Repetitive preganglionic stimulation (30 Hz, 1-2 sec) elicited in curarized rabbit, rat and cat SCGs, a biphasic response as the initial slow positive (P) potential, was followed by a late negative (LN) potential. In curarized guinea-pig SCG, a LN response with no detectable P potential was observed. Neostigmine (0.5-1 microM) increased the amplitude and duration of the P and LN responses in the majority of the rabbit, rat and cat SCGs. LN response of guinea-pig SCG was first enhanced by neostigmine; subsequently, it was converted into a hyperpolarizing potential. Alpha receptor antagonists, phenoxybenzamine, phentolamine and dihydroergotamine, and a beta receptor antagonist, propranolol, did not appreciably alter the P and LN responses of the rabbit, cat and rat SCG or neostigmine-induced hyperpolarization of the guinea-pig SCG. Dopaminergic receptor antagonists, haloperidol, chlorpromazine and metoclopramide, caused no significant depression of the P and LN responses in the rabbit SCG. Atropine (1 microM) consistently abolished the P and/or LN of all these ganglia, as well as the neostigmine-induced hyperpolarization of the guinea-pig SCG. These results demonstrate that muscarinic receptors are involved in the generation of P and LN potentials of mammalian sympathetic ganglia, while the adrenergic and disynaptic nature of P response remains to be clarified. Furthermore, there appears to be no correlation between the generation of P potential and elevation of cyclic AMP in the SCG.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=6108360&dopt=Abstract
Acta Physiol Scand Suppl. 1983;518:1-68.
The regulation of glycogen phosphorylase and glycogen breakdown in human skeletal muscle.
Chasiotis D.
The regulation of glycogen phosphorylase and glycogen breakdown in human skeletal muscle has been investigated using the needle biopsy technique. Preliminary studies showed that the activity of phosphorylase in vitro was dependent upon the concentration of inorganic phosphate (Pi) used in the assay system. The Km of phosphorylase a for Pi was found to be 26.2 mmol/l, and that of (a+b) (assayed in the presence of saturating AMP) was 6.8 mmol/l. Because of the difference in Km the apparent percentage of a to (a+b) activity varies with the Pi concentration used in the assay system. Phosphorylase a and (a+b) activities were therefore adjusted to saturating Pi concentrations. The ratio of the activities in this case is independent of the Pi concentration and constitutes a minimal estimate of the fraction of phosphorylase molecules in the a form. The fraction of phosphorylase in the a form in resting muscle was as a mean 22%. Despite nearly a quarter of the phosphorylase being in the a form glycogenolytic activity is extremely low. It is proposed that the concentration of Pi at the active site of the enzyme is low compared to the Km for this of either form of the enzyme, and is limiting to activity. A Pi concentration in resting muscle of 1-3 mmol/l was calculated. During epinephrine infusion at rest 90% of the phosphorylase was transformed to the a form but only a moderate increase in the glycogenolytic rate occurred. This rate approximated to 5-10% of the maximum rate of the enzyme (Vmaxa). During prolonged epinephrine infusion the glycogenolytic rate decreased despite the continuance of 90% or more of the phosphorylase in the a form. In contrast to epinephrine infusion prolonged ischemia resulted in a decrease in the mole fraction of phosphorylase a and simultaneously in an increase of the glycogenolytic rate. During isometric and dynamic exercise there was a rapid transformation of phosphorylase b to a paralleled by pronounced increase in the rate of glycogen breakdown. The increased rate of glycogenolysis during isometric exercise was close to the Vmax of phosphorylase a in vivo. When either form of exercise was continued to fatigue/exhaustion, a re-transformation of phosphorylase a to b was observed. During dynamic exercise cAMP in the muscle increased two fold. This increase was blocked by the prior administration of propranolol.+
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=6139934&dopt=Abstract
Biochem J. 1983 Dec 15;216(3):675-80.
Beta-adrenergic control of phosphatidylcholine synthesis by transmethylation in hepatocytes from juvenile, adult and adrenalectomized rats.
Marin-Cao D, Alvarez Chiva V, Mato JM.
Changes in isoprenaline-sensitive phospholipid methyltransferase were studied in hepatocytes isolated from juvenile, mature and adrenalectomized rats. Isoprenaline produced greater stimulation of cyclic AMP accumulation in juvenile and mature adrenalectomized rats than in mature animals. Similarly, isoprenaline stimulated phospholipid methyltransferase in juvenile and mature adrenalectomized rats but had no effect in mature animals. Isoprenaline-mediated activation of phospholipid methyltransferase in adrenalectomized rats was time- and dose-dependent. In hepatocytes isolated from adrenalectomized rats incubated with [Me-3H]methionine or [3H]-ethanolamine the addition of isoprenaline increased the amount of radioactivity incorporated into phosphatidylcholine. The activation by isoprenaline of phospholipid methyltransferase was abolished by the beta-blocker propranolol and by insulin. These results indicate that rat liver the occupation of functional beta-receptors causes a stimulation of phospholipid methylation. It is suggested that, as reported previously, cyclic AMP activates phospholipid methyltransferase.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=6320796&dopt=Abstract
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