October 1, 1992Journal of Biological ChemistryOpen Access

Inhibition of actin-tropomyosin activation of myosin MgATPase activity by the smooth muscle regulatory protein caldesmon.

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Population

In vitro model using sheep aorta actin-tropomyosin and skeletal muscle heavy meromyosin / subfragment 1

Design

Preclinical

Authors

SMSteven B. MarstonImperial College London CRCharles RedwoodHeart Failure / Cardiomyopathy

Discussion

Member takes

Implication

Does not alter clinical practice; leaves open caldesmon C-terminus validation in human vascular models.

Structured PICO

Population

In vitro model using sheep aorta actin-tropomyosin and skeletal muscle heavy meromyosin (HMM) / subfragment 1 (S1)

Intervention

Caldesmon and an expressed mutant comprising the C-terminal 99 amino acids

Outcome

Inhibition of actin-tropomyosin activation of myosin MgATPase activitysurrogate

The inhibitory function of caldesmon on actomyosin ATPase resides entirely in its extreme C-terminus and acts by slowing the rate-limiting step of the activation pathway.

Cite This Study

Marston et al. (1992) studied this question.

synapsesocial.com/papers/6a843ec77ae632e783bd837e https://doi.org/10.1016/s0021-9258(18)41852-2

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Inhibition of actin-tropomyosin activation of myosin MgATPase activity by the smooth muscle regulatory protein caldesmon.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Inhibition of actin-tropomyosin activation of myosin MgATPase activity by the smooth muscle regulatory protein caldesmon.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider