Co-reconstitution of Phospholamban Mutants with the Ca-ATPase Reveals Dependence of Inhibitory Function on Phospholamban Structure

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Population

In vitro model using purified Ca-ATPase co-reconstituted with Phospholamban and its mutants

Comparison

PLB mutants (C41L-PLB and L37A-PLB) vs Wild type-PLB (wt-PLB)

Design

Preclinical

Authors

Discussion

Monomer potency of PLB may inform SERCA-targeted HF strategies; leaves open validation in human myocardium.

Population

In vitro model using purified Ca-ATPase co-reconstituted with Phospholamban (PLB) and its mutants (C41L-PLB and L37A-PLB)

Intervention

PLB mutants (C41L-PLB and L37A-PLB)

Comparator

Wild type-PLB (wt-PLB)

Outcome

Inhibitory activity on Ca-ATPasesurrogate

The inhibition of Ca-ATPase by Phospholamban depends on both its dissociation into monomers and the specific potency of the resulting monomer.

Reddy et al. (1999) studied this question.

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