March 15, 1985Biochemical JournalOpen Access

Cardiac sarcoplasmic-reticulum calmodulin-binding proteins. Modulation of calmodulin binding to phospholamban by phosphorylation

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Population

Canine cardiac sarcoplasmic reticulum

Comparison

Phosphorylation by catalytic subunit of cyclic… vs Unphosphorylated state (dephosphophospholamban)

Design

Preclinical

Authors

Discussion

Indicates potential SR Ca2+ regulation via phospholamban; leaves open physiological role in intact hearts.

Population

Canine cardiac sarcoplasmic reticulum

Intervention

Phosphorylation by catalytic subunit of cyclic AMP-dependent protein kinase or Ca2+/calmodulin-dependent phospholamban kinase

Comparator

Unphosphorylated state (dephosphophospholamban)

Outcome

Calmodulin bindingsurrogate

Phosphorylation of phospholamban inhibits its binding to calmodulin, suggesting a regulatory mechanism in cardiac sarcoplasmic reticulum function.

Molla et al. (1985) studied this question.

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