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Phosphorylation of phospholamban by either a cAMP-dependent or a calmodulin-dependent kinase stimulates the Ca2+ transporting activity of cardiac sarcoplasmic reticulum membranes. It has now been found that phospholamban consists of 2 distinct proteins; one is the specific substrate for the cAMP-dependent phosphorylation, and the other for the calmodulin-dependent kinase. In spite of functional diversity, the 2 polypeptides share a number of properties. Among them, the proteolipid character, Mr, resistance to trypsinization, and subunit composition.

The activity of the Ca2+-pumping ATPase of cardiac sarcoplasmic reticulum is controlled by the phosphorylation level of the intrinsic membrane protein phospholamban. Phospholamban monomers contain two distinct phosphorylation sites for either the cAMP-dependent or the calmodulin-dependent kinase. The two kinases, however, preferentially phosphorylate different populations of phospholamban molecules and double phosphorylation of the same subunit by their concerted action is a phenomenon that occurs only under particular experimental conditions. This study investigates the phosphorylation pattern of phospholamban in various subfractions derived from dog cardiac sarcoplasmic reticulum. The results show that the endogenous calmodulin-dependent kinase preferentially phosphorylates the phospholamban population found in association with the cisternal compartments of the reticulum. The differential phosphorylation occurs despite the presence of sufficient amounts of the kinase in all sarcoplasmic reticulum subfractions. On the other hand, phospholamban molecules localized on the longitudinal system are preferential substrates for the cAMP-dependent kinase. Possibly, the different lipid and/or protein microenvironment of phospholamban in the various sarcoplasmic reticulum domains is responsible for the apparent heterogeneity of phosphorylation. The present findings are compatible with the concept of additive and independent action of the cAMP-dependent and calmodulin-dependent kinases on cardiac sarcoplasmic reticulum. The imply, however, that different regions of the sarcoplasmic reticulum network are controlled by the two regulatory mechanisms.

A series of 30 carotid-ophthalmic aneurysms, some of them bilateral, is reported. All of them were treated by a direct surgical approach. There were 25 patients in this series, 23 female and two male. In some cases there were associated pituitary adenomas and other aneurysms. The anatomy, clinical manifestations, and surgical treatment are discussed. There were no deaths among these 25 patients. Twenty-two of these patients recovered completely.

The experience of the senior author was 16 anterior choroidal artery aneurysms is reviewed. The anatomic variations of the origin of the anterior choroidal artery are discussed, and the danger of sacrificing the artery in aneurysm surgery is stressed. The surgical procedure upon these aneurysms has frequently been difficult, requiring careful microdissection. This was due to variations of the origin of the aneurysm in respect to the artery and their frequent contiguity.