High impact information on PLB

• We studied the developmental and tissue-specific expression of phospholamban mRNA using nuclease mapping analysis [1].
• The phospholamban gene, which is present as a single copy in the chicken genome, is about 10 kilobase pairs long, with approximately 6.5 kilobase pairs representing the intron sequences [1].
• Phosphorylation of phospholamban by protein kinase C was additive with that catalyzed by membrane-bound or exogenous cyclic AMP-dependent protein kinase and with Ca2+-calmodulin-dependent protein kinase [2].
• The major substrates for protein kinase C in cardiac membranes were peptides of 88,000, 51,000, 42,000 daltons, and the peptide known as phospholamban (Mr = 27,000 or 11,000 depending on sample preparation) [2].
• The data indicate separate genetic control for synthesis of phospholamban and sarcoplasmic reticulum Ca2+-ATPase [3].

Anatomical context of PLB

• Both phospholamban and skeletal alpha-tropomyosin messages in the myocardium of the AV canal region showed significant decrease during this period of the development [4].

Associations of PLB with chemical compounds

• N6(L-phenylisopropyl)adenosine reversed the effect of the beta-receptor agonist isoproterenol on phospholamban phosphorylation in 32P-labelled slices of newborn chick hearts [5].

Other interactions of PLB

• Three examples, 15H16 (phospholamban), E13 (skeletal alpha-tropomyosin) and 21C (a novel gene), are discussed here [4].

References