August 11, 2000Biochemistry

Synthetic Null-Cysteine Phospholamban Analogue and the Corresponding Transmembrane Domain Inhibit the Ca-ATPase

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Population

In vitro model using synthetic null-cysteine phospholamban analogue and its transmembrane domain…

Comparison

Synthetic null-cysteine PLB analogue and… vs Full-length parent PLB molecule

Design

Preclinical

Authors

CKChristine B. KarimUniversity of Minnesota CMChristopher G. MarquardtUniversity of Minnesota JSJohn D. StammUniversity of Iowa

Discussion

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Implication

TM domain suffices for phospholamban-SERCA inhibition in animal models; extends mechanistic data but leaves clinical translation open.

Structured PICO

Population

In vitro model using synthetic null-cysteine phospholamban (PLB) analogue and its transmembrane (TM) domain reconstituted into liposomes containing Ca-ATPase from cardiac sarcoplasmic reticulum

Intervention

Synthetic null-cysteine PLB analogue and synthetic null-cysteine TM domain (residues 26-52)

Comparator

Full-length parent PLB molecule

Outcome

Inhibitory function on Ca-ATPase and oligomeric stabilitysurrogate

The transmembrane domain of phospholamban is sufficient for inhibiting the cardiac sarcoplasmic reticulum calcium pump, independent of its oligomeric stability or cysteine residues.

Cite This Study

Karim et al. (2000) studied this question.

synapsesocial.com/papers/6a8a4f7a186271ac99335d10 https://doi.org/10.1021/bi0003543

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Synthetic Null-Cysteine Phospholamban Analogue and the Corresponding Transmembrane Domain Inhibit the Ca-ATPase

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Synthetic Null-Cysteine Phospholamban Analogue and the Corresponding Transmembrane Domain Inhibit the Ca-ATPase

Discussion

Member takes

Implication

Structured PICO

Cite This Study

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Also Consider