TY - JOUR
T1 - Determination of calcium transport and phosphoprotein phosphatase activity in microsomes from respiratory and vascular smooth muscle
AU - Sands, Howard
AU - Mascali, James
AU - Paietta, Elisabeth
N1 - Funding Information:
This work was supported by research grant HL-14964 from the National Institutes of Health, United States Public Health Service.
PY - 1977/12/22
Y1 - 1977/12/22
N2 - 1. 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. 2. Bovine and rabbit, heavy and light microsomes were isolated from respiratory (tracheal) and vascualar (aortic) smooth muscle. Preincubation of these vesicles with cyclic AMP and protein kinase did not alter the transport of calcium into the vesicles. There was no evidence of phosphate incorporatio 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. 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.
AB - 1. 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. 2. Bovine and rabbit, heavy and light microsomes were isolated from respiratory (tracheal) and vascualar (aortic) smooth muscle. Preincubation of these vesicles with cyclic AMP and protein kinase did not alter the transport of calcium into the vesicles. There was no evidence of phosphate incorporatio 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. 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.
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U2 - 10.1016/0304-4165(77)90015-0
DO - 10.1016/0304-4165(77)90015-0
M3 - Article
C2 - 201293
AN - SCOPUS:0017668918
SN - 0304-4165
VL - 500
SP - 223
EP - 234
JO - BBA - General Subjects
JF - BBA - General Subjects
IS - 2
ER -