Determination of calcium transport and phosphoprotein phosphatase activity in microsomes from respiratory and vascular smooth muscle.
1. Calcium transport into microsomal vesicles of respiratory (tracheal) smooth muscle was characterized. This calcium transport was ATP dependent and stimulated by the presence of the oxalate ion. The magnitude of transport was similar to that reported for microsomes from other types of smooth muscle. 2. Bovine and rabbit, heavy and light microsomes were isolated from respiratory (tracheal) and vascular (aortic) smooth muscle. Preincubation of these vesicles with cyclic AMP and protein kinase did not alter the transport of calcium into the vesicles. There uas no evidence of phosphate incorporation into microsomal membrane proteins. Similar results were obtained if phosphorylase b kinase replaced the combination of cyclic AMP and protein kinase during the preincubation. 3. The phosphoprotein phosphatase activity of cardiac sarcoplasmic reticulum and smooth muscle microsomes was determined. The activity of this enzyme was found to be several-fold less in the cardiac sarcoplasmic reticulum than in various smooth muscle microsome preparations.
D000818:Animals; D001011:Aorta; D001692:Biological Transport; D002118:Calcium / Q000378:metabolism*; D002417:Cattle; D000242:Cyclic AMP / Q000494:pharmacology*; D008297:Male; D008861:Microsomes / Q000378:metabolism; D009130:Muscle, Smooth / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010764:Phosphorylase Kinase / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000378:metabolism; D014132:Trachea
D000242:Cyclic AMP; D011494:Protein Kinases; D010764:Phosphorylase Kinase; D010749:Phosphoprotein Phosphatases; D002118:Calcium