October 1, 2001Journal of Biological ChemistryOpen Access

Defining the Structural Determinants and a Potential Mechanism for Inhibition of Myosin Phosphatase by the Protein Kinase C-potentiated Inhibitor Protein of 17 kDa

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Population

In vitro biochemical assays and fibroblast cell models

Comparison

CPI-17 deletion mutants and point mutants vs Wild-type CPI-17

Design

Preclinical

Authors

YHYuichiro HayashiNagoya University SSShingo SenbaHokkaido University MYMichio YazawaHokkaido University of Science

Discussion

Member takes

Implication

Clarifies CPI-17 domain for MLCP inhibition; extends molecular basis of vascular tone but leaves open in vivo validation.

Structured PICO

Population

In vitro biochemical assays and fibroblast cell models

Intervention

CPI-17 deletion mutants and point mutants (e.g., Y41A)

Comparator

Wild-type CPI-17

Outcome

Inhibitory potency (IC50) toward myosin light chain phosphatase (MLCP)surrogate

Identifies the structural domain (residues 35-120) and key residue (Tyr41) of CPI-17 required for inhibiting myosin light chain phosphatase, a key mechanism in vascular smooth muscle contraction.

Cite This Study

Hayashi et al. (2001) studied this question.

synapsesocial.com/papers/6a7cadd4273accedbda8aff1 https://doi.org/10.1074/jbc.m107302200

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Defining the Structural Determinants and a Potential Mechanism for Inhibition of Myosin Phosphatase by the Protein Kinase C-potentiated Inhibitor Protein of 17 kDa

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Defining the Structural Determinants and a Potential Mechanism for Inhibition of Myosin Phosphatase by the Protein Kinase C-potentiated Inhibitor Protein of 17 kDa

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider