September 1, 1986Journal of Biological ChemistryOpen Access

Involvement of 60-kilodalton phosphoprotein in the regulation of calcium release from skeletal muscle sarcoplasmic reticulum.

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Population

"Heavy" sarcoplasmic reticulum vesicles from skeletal muscle

Comparison

Phosphorylation by addition of MgATP in the… vs Unphosphorylated state / absence of added…

Design

Preclinical

Authors

DKD H KimUniversity of Tsukuba NINoriaki IkemotoDenso (Japan)

Discussion

Member takes

Implication

Does not support clinical translation; leaves open the role of calmodulin-dependent 60-kDa phosphorylation in skeletal muscle Ca2+ regulation.

Structured PICO

Population

"Heavy" sarcoplasmic reticulum vesicles from skeletal muscle

Intervention

Phosphorylation by addition of MgATP in the presence or absence of calmodulin

Comparator

Unphosphorylated state / absence of added calmodulin

Outcome

Initial rate of Ca2+ release and phosphorylation level of the 60-kDa proteinsurrogate

Calmodulin-dependent phosphorylation of a 60-kDa protein plays an important role in regulating calcium release from skeletal muscle sarcoplasmic reticulum.

Cite This Study

Kim et al. (1986) studied this question.

synapsesocial.com/papers/6a83d2478df3fed3c85bd770 https://doi.org/10.1016/s0021-9258(18)67296-5

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Implication

Does not support clinical translation; leaves open the role of calmodulin-dependent 60-kDa phosphorylation in skeletal muscle Ca2+ regulation.

Involvement of 60-kilodalton phosphoprotein in the regulation of calcium release from skeletal muscle sarcoplasmic reticulum.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Involvement of 60-kilodalton phosphoprotein in the regulation of calcium release from skeletal muscle sarcoplasmic reticulum.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider