Abstract
The Ca2+ uptake and the (Ca2+ + Mg2+)-dependent ATPase of the porcine coronary-artery smooth-muscle microsomal fraction ('microsomes') are only slightly stimulated by calmodulin. The Ca2+ uptake after 2 min in the absence of oxalate, corrected for the ATP-independent binding, increased by a factor of 1.44, whereas the (Ca2+ + Mg2+)-dependent ATPase is stimulated 1.39 times. These findings contrast with the effect observed in human erythrocyte 'inside-out' microsomes. In these vesicles calmodulin increases the Ca2+ uptake after 20 min in an oxalate-free medium and the (Ca2+ + Mg2+)-dependent ATPase respectively by a factor of 3.82 and 6.18. The magnitude of the calmodulin stimulation of the Ca2+ transport in coronary-artery microsomes is similar to that observed in heart microsomes.
MeSH Terms
Animals
Calcium/metabolism
Calcium-Binding Proteins/pharmacology
Calcium-Transporting ATPases/metabolism
Calmodulin/pharmacology
Dogs
Erythrocytes/drug effects,metabolism
Heart/drug effects
Humans
Microsomes/metabolism
Muscle, Smooth, Vascular/drug effects,metabolism
Myocardium/metabolism
Swine
Chemicals
Calcium-Binding Proteins
Calmodulin
Calcium-Transporting ATPases
Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Wuytack F
De Schutter G
Casteels R
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14 references, click to expand
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