April 1, 1998Biochemical JournalOpen Access

Anti-phospholamban and protein kinase A alter the Ca2+ sensitivity and maximum velocity of Ca2+ uptake by the cardiac sarcoplasmic reticulum

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Population

Native cardiac sarcoplasmic reticulum (SR) vesicles

Comparison

Constitutively active subunit of PKA or… vs Denatured cPKA or denatured A1

Design

Preclinical

Authors

MKMargaret E. KargacinUniversity of Calgary ZAZenobia AliUniversity of Calgary GKGary J. KargacinUniversity of Calgary

Discussion

Member takes

Implication

Supports phospholamban phosphorylation effects on SR Ca2+ handling in animals; leaves open translation to in vivo function or human therapy.

Structured PICO

Population

Native cardiac sarcoplasmic reticulum (SR) vesicles

Intervention

Constitutively active subunit of PKA (cPKA) or monoclonal antibody (A1) against phospholamban

Comparator

Denatured cPKA or denatured A1

Outcome

Net Ca2+ uptake (Ca2+ sensitivity and maximum velocity) measured by fluorescencesurrogate

Phosphorylation of phospholamban increases both the calcium sensitivity and the maximum velocity of calcium uptake into the cardiac sarcoplasmic reticulum.

Cite This Study

Kargacin et al. (1998) studied this question.

synapsesocial.com/papers/6a75a3f6ef3d015f2ddd7f71 https://doi.org/10.1042/bj3310245

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Implication

Supports phospholamban phosphorylation effects on SR Ca2+ handling in animals; leaves open translation to in vivo function or human therapy.

Anti-phospholamban and protein kinase A alter the Ca2+ sensitivity and maximum velocity of Ca2+ uptake by the cardiac sarcoplasmic reticulum

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Anti-phospholamban and protein kinase A alter the Ca2+ sensitivity and maximum velocity of Ca2+ uptake by the cardiac sarcoplasmic reticulum

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider