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Biomedical subjects

C Muscari

Publications and source records attributed to C Muscari.

57 records · Page 4Linked to original sources

Inhibitory action of opioid peptides on ouabain-sensitive Na+-K+ and Ca2+-dependent ATPase activities in bovine cardiac sarcolemma.

The present study demonstrates that morphine (10(-6) and 10(-5) M), methionine-enkephalin or leucine-enkephalin (10(-10), 10(-8), and 10(-6) M) were able to inhibit significantly, in a dose-dependent manner, both the sarcolemmal Ca2+-dependent ATPase and the ouabain-sensitive Na+-K+ ATPase activities. The inhibitory action of these opioids on the two ATPases was not antagonized by preincubation with naloxone (10(-6) M). Naloxone alone (10(-8), 10(-6) and 10(-5) M) did not affect both the sarcolemmal Ca2+-dependent ATPase and the ouabain-sensitive Na+-K+ ATPase activities. Heat-denatured methionine-enkephalin (10(-6) M) or leucine-enkephalin (10(-6) M) also unaffected both the ATPases. The possibility is also discussed that opioid peptides may regulate myocardial contractility by modulating the movement of ions across the heart sarcolemma.

Animals↗

Effect of catecholamines on ornithine decarboxylase activity monitored in the perfused rat heart.

The activity of ornithine decarboxylase was monitored in situ by perfusing rat heart with (1-14COOH)-ornithine. Infusion of isoproterenol or noradrenaline caused after 15-20 min an activation of the ornithine decarboxylation 5 fold above control hearts; less evident was the effect of adrenaline. Isoproterenol induced ornithine decarboxylation was prevented by difluoromethyl-ornithine. Also propranolol produced a significative reduction of the flux of 14CO2 collected from the perfusate. The measurement of the ornithine decarboxylase activity in heart homogenates by confirming the above results, indicated that the in situ monitor of ornithine decarboxylation can represent an accurate method which reveals rapid activation of the enzyme.

Animals↗

Inhibitory effect of oxidized glutathione on heart ornithine decarboxylase activity.

Cardiac ODC was prepared from rats after the injection of isoproterenol and was partially purified by thiol-affinity chromatography. This enzymatic preparation incubated with GSSG was inactivated in a concentration dependent process. The inactivated enzyme could be reactivated by the addition of various reducing compounds, including GSH. Kinetic studies on GSSG-inactivated ODC revealed that the enzyme was inhibited by a partially-non competitive mechanism.

Animals↗