Evidence map›Paper›PMID 12296769›Full record

ArticleThe Biochemical journal2003

Agonist-induced changes in the phosphorylation of the myosin- binding subunit of myosin light chain phosphatase and CPI17, two regulatory factors of myosin light chain phosphatase, in smooth muscle.

Naohisa Niiro, Yasuhiko Koga, Mitsuo Ikebe

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
6.4field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

42 citing papers in PubMed, 115 citations in OpenAlex.

  1. Regulation of myosin light-chain phosphorylation and its roles in cardiovascular physiology and pathophysiology.Hypertension research : official journal of the Japanese Society of Hypertension · 2022
    Review
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  15. Role of PKC and RhoA/ROCK pathways in the spontaneous phasic activity in the rectal smooth muscle.American journal of physiology. Gastrointestinal and liver physiology · 2013
    Article
  16. Article
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  18. Mechanisms underlying potentiation of endothelin-1-induced myofilament Ca(2+) sensitization after subarachnoid hemorrhage.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2012
    Article
  19. Article
  20. Hypoxic pulmonary vasoconstriction.Physiological reviews · 2012
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Naohisa NiiroDepartment of Physiology, University of Massachusetts Medical School, Worcester, MA 01655, USA.
Yasuhiko Koga
Mitsuo Ikebe
University of Massachusetts Chan Medical School · US

Funding

MOLECULAR REGULATION OF SMOOTH MUSCLE ACTOMYOSINR01AR041653 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 1992 to 2004
$1.8M
PROTEIN KINASES ON SMOOTH MUSCLE REGULATIONR01HL061426 · NHLBI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 1999 to 2002
$1.3M
NHLBI NIH HHS HL61426NIAMS NIH HHS AR41653PHS HHS 60831
6 · The paper itself

Abstract

The inhibition of myosin light chain phosphatase (MLCP) enhances smooth muscle contraction at a constant [Ca2+]. There are two components, myosin-binding subunit of MLCP (MBS) and CPI17, thought to be responsible for the inhibition of MLCP by external stimuli. The phosphorylation of MBS at Thr-641 and of CPI17 at Thr-38 inhibits the MLCP activity in vitro. Here we determined the changes in the phosphorylation of MBS and CPI17 after agonist stimulation in intact as well as permeabilized smooth muscle strips using phosphorylation-site-specific antibodies as probes. The CPI17 phosphorylation transiently increased after agonist stimulation in both alpha-toxin skinned and intact fibres. The time course of the increase in CPI17 phosphorylation after stimulation correlated with the increase in myosin regulatory light chain (MLC) phosphorylation. The increase in CPI17 phosphorylation was significantly diminished by Y27632, a Rho kinase inhibitor, and GF109203x, a protein kinase C inhibitor, suggesting that both the protein kinase C and Rho kinase pathways influence the change in CPI17 phosphorylation. On the other hand, a significant level of MBS phosphorylation at Thr-641, an inhibitory site, was observed in the resting state for both skinned and intact fibres and the agonist stimulation did not significantly alter the MBS phosphorylation level at Thr-641. While the removal of the agonist markedly decreased MLC phosphorylation and induced relaxation, the phosphorylation of MBS was unchanged, while CPI17 phosphorylation markedly diminished. These results strongly suggest that the phosphorylation of CPI17 plays a more significant role in the agonist-induced increase in myosin phosphorylation and contraction of smooth muscle than MBS phosphorylation in the Ca2+-independent activation mechanism of smooth muscle contraction.

Indexed as

Amino Acid SequenceAnimalsIn Vitro TechniquesMolecular Sequence DataMuscle ProteinsMuscle, SmoothMyosin-Light-Chain PhosphataseMyosinsPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationProtein BindingRabbitsRecombinant ProteinsCPI-17 protein, Oryctolagus cuniculusMuscle ProteinsMyosin-Light-Chain PhosphataseMyosinsPhosphoprotein PhosphatasesPhosphoproteinsRecombinant Proteins

Identifiers

PMID12296769
PMCPMC1223061
OpenAlexW2071701870

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.