Protein kinase C and cAMP‐dependent protein kinase induce opposite effects on actin polymerizability
Population
In vitro muscle and non-muscle monomeric and filamentous actin
Comparison
Phosphorylation by protein kinase C or… vs Unphosphorylated actin
Design
Preclinical
Authors
Discussion
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Member takes
Implication
Requires confirmation in intact cardiomyocytes; leaves open any role in cytoskeletal regulation of cardiac function.
Structured PICO
P
Population
In vitro muscle and non-muscle monomeric and filamentous actin
I
Intervention
Phosphorylation by protein kinase C or cAMP-dependent protein kinase
C
Comparator
Unphosphorylated actin
O
Outcome
Actin polymerizability (incorporation into F-actin)surrogate
Protein kinase C and cAMP-dependent protein kinase phosphorylate actin differently and induce opposite effects on its polymerizability in vitro.
Cite This Study
Ohta et al. (1987) studied this question.