August 1, 1985Journal of Biological ChemistryOpen Access

Dephosphorylation of myosin by the catalytic subunit of a type-2 phosphatase produces relaxation of chemically skinned uterine smooth muscle.

View Full Paper

Ask AI

Bookmark

Population

Glycerinated uterine smooth muscle preparation

Design

Preclinical

Authors

JHJoe R. HaeberleUniversity of Vermont DHDavid R. HathawayNational Heart Lung and Blood Institute ADAnna Depaoli-RoachIndiana University School of Medicine

Discussion

Member takes

Implication

Supports myosin dephosphorylation as a relaxation mechanism in uterine smooth muscle; leaves open in vivo relevance and therapeutic targeting.

Structured PICO

Population

Glycerinated uterine smooth muscle preparation

Intervention

Addition of highly purified catalytic subunit of a type-2, skeletal muscle phosphoprotein phosphatase (protein phosphatase 2A) (0.28 microM)

Outcome

Muscle relaxation and myosin light chain phosphorylation levelssurrogate

Dephosphorylation of the 20,000-dalton myosin light chain by protein phosphatase 2A is sufficient to induce relaxation in contracted uterine smooth muscle.

Cite This Study

Haeberle et al. (1985) studied this question.

synapsesocial.com/papers/6a7027f653da1ffdb5079d80 https://doi.org/10.1016/s0021-9258(17)39195-0

View Full Paper

Ask AI

Bookmark

Implication

Supports myosin dephosphorylation as a relaxation mechanism in uterine smooth muscle; leaves open in vivo relevance and therapeutic targeting.

Dephosphorylation of myosin by the catalytic subunit of a type-2 phosphatase produces relaxation of chemically skinned uterine smooth muscle.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Dephosphorylation of myosin by the catalytic subunit of a type-2 phosphatase produces relaxation of chemically skinned uterine smooth muscle.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider