September 1, 1994Journal of Biological ChemistryOpen Access

Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban.

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Population

In vitro model coexpressing mutant SERCA2 or chimeric SERCA2/SERCA3 molecules with phospholamban

Comparison

Mutation of amino acids in the phosphorylation… vs Wild-type SERCA2, wild-type SERCA3, or other…

Design

Preclinical

Authors

TTToshihiko ToyofukuIhara Chemical Industry (Japan)KKKazimierz KurzydlowskiUniversity of Toronto MTMichihiko TadaUniversity of Vermont

Discussion

Member takes

Implication

No immediate clinical implications; leaves open targeted modulation of SERCA2-PLN interaction for future cardiac studies.

Structured PICO

Population

In vitro model coexpressing mutant SERCA2 or chimeric SERCA2/SERCA3 molecules with phospholamban

Intervention

Mutation of amino acids in the phosphorylation domain of SERCA2/SERCA3 (specifically Lys397 to Val402)

Comparator

Wild-type SERCA2, wild-type SERCA3, or other mutations

Outcome

Functional association with phospholambansurrogate

Amino acids Lys397-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum (SERCA2) are critical for its functional association with phospholamban.

Cite This Study

Toyofuku et al. (1994) studied this question.

synapsesocial.com/papers/6a730c0b91c366bb2031e70a https://doi.org/10.1016/s0021-9258(17)31597-1

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Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider