What does this research mean for the field?

Thiophosphorylation of the 130-kDa subunit of myosin light chain phosphatase decreases the enzyme's activity, suggesting that phosphorylation of this subunit plays a key role in regulating calcium sensitivity and force output in smooth muscle. Novelty: ClaimNovelty.INCREMENTAL. Consensus alignment: ConsensusAlignment.NEUTRAL.

What question did this study set out to answer?

This research aims to investigate the relationship between thiophosphorylation of the 130-kDa subunit and myosin light chain phosphatase activity.

August 1, 1995Journal of Biological ChemistryOpen Access

Thiophosphorylation of the 130-kDa Subunit Is Associated with a Decreased Activity of Myosin Light Chain Phosphatase in α-Toxin-permeabilized Smooth Muscle

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Population

α-toxin-permeabilized smooth muscle

Design

Preclinical

Authors

LTLaura Trinkle‐MulcahyUniversity of Ottawa KIKazuhito IchikawaNoda Institute for Scientific Research DHDavid J. HartshorneRutgers, The State University of New Jersey

Discussion

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Implication

No direct clinical implications from this animal study; leaves open regulatory role of subunit phosphorylation in contraction.

Key Points

This research aims to investigate the relationship between thiophosphorylation of the 130-kDa subunit and myosin light chain phosphatase activity.
Utilized ATPγS to pretreat α-toxin-permeabilized smooth muscle.
Assessed calcium sensitivity of force output and myosin light chain phosphorylation.
Measured changes in myosin light chain phosphatase activity.
Calcium sensitivity increased alongside myosin light chain phosphorylation after pretreatment.
Myosin light chain phosphatase activity decreased by 5-fold.
Thiophosphorylation of the 130-kDa subunit was noted, leading to diminished phosphatase activity.

Structured PICO

Population

α-toxin-permeabilized smooth muscle

Intervention

Pretreatment with ATPγS (adenosine 5ʹ-O-(thiotriphosphate))

Outcome

Myosin light chain phosphatase activity and calcium sensitivity of force outputsurrogate

Thiophosphorylation of the 130-kDa subunit of myosin light chain phosphatase decreases its activity, suggesting a regulatory role for phosphorylation of this subunit in smooth muscle contraction.

Cite This Study

Trinkle‐Mulcahy et al. (1995) studied this question.

synapsesocial.com/papers/6a1e40bf7f6e8bbb2368afee https://doi.org/10.1074/jbc.270.31.18191

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Thiophosphorylation of the 130-kDa Subunit Is Associated with a Decreased Activity of Myosin Light Chain Phosphatase in α-Toxin-permeabilized Smooth Muscle

Discussion

Member takes

Implication

Key Points

Structured PICO

Cite This Study

Thiophosphorylation of the 130-kDa Subunit Is Associated with a Decreased Activity of Myosin Light Chain Phosphatase in α-Toxin-permeabilized Smooth Muscle

Discussion

Member takes

Implication

Key Points

Structured PICO

Cite This Study

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