Evidence map›Paper›PMID 9518739›Full record

ArticleThe Journal of physiology1998

Possible involvement of the novel CPI-17 protein in protein kinase C signal transduction of rabbit arterial smooth muscle.

L Li, M Eto, M R Lee, F Morita, M Yazawa, T Kitazawa

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

46 citing papers in PubMed, 171 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
  2. Review
  3. Article
  4. Review
  5. Article
  6. Smooth muscle-protein translocation and tissue function.Anatomical record (Hoboken, N.J. : 2007) · 2014
    Review
  7. Article
  8. Article
  9. Smooth muscle-selective CPI-17 expression increases vascular smooth muscle contraction and blood pressure.American journal of physiology. Heart and circulatory physiology · 2013
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
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  19. Maturation and the role of PKC-mediated contractility in ovine cerebral arteries.American journal of physiology. Heart and circulatory physiology · 2009
    Article
  20. The actin cytoskeleton in cancer cell motility.Clinical & experimental metastasis · 2009
    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

6 authors at 2 institutions in 2 countries.

L LiDepartment of Physiology and Biophysics, Georgetown University School of Medicine, Washington, DC 20007, USA.
M Eto
M R Lee
F Morita
M Yazawa
T Kitazawa
Hokkaido University · JPGeorgetown University · US

Funding

G PROTEIN-MEDIATED CA++ SENSITIZATION IN SMOOTH MUSCLER01HL051824 · NHLBI · GEORGETOWN UNIVERSITY · PI KITAZAWA, TOSHIO · 1993 to 2002
$952k
NHLBI NIH HHS HL51824
6 · The paper itself

Abstract

1. CPI-17 has recently been identified as a novel protein in vascular smooth muscle. In vitro , its phosphorylation and thiophosphorylation by protein kinase C (PKC) specifically inhibits the type 1 class of protein phosphatases, including myosin light chain (MLC) phosphatase. 2. Both of the phosphorylated CPI-17 states dose-dependently potentiated submaximal contractions at constant [Ca2+] in beta-escin-permeabilized and Triton X-100-demembranated arterial smooth muscle, but produced no effect in intact and less intensely permeabilized (alpha-toxin) tissue. Thiophosphorylated CPI-17 (tp-CPI) induced large contractions even under Ca2+-free conditions and decreased Ca2+ EC50 by more than an order of magnitude. Unphosphorylated CPI-17 produced minimal but significant effects. 3. tp-CPI substantially increased the steady-state MLC phosphorylation to Ca2+ ratios in beta-escin preparations. 4. tp-CPI affected the kinetics of contraction and relaxation and of MLC phosphorylation and dephosphorylation in such a manner that indicates its major physiological effect is to inhibit MLC phosphatase. 5. Results from use of specific inhibitors in concurrence with tp-CPI repudiate the involvement of general G proteins, rho A or PKC itself in the Ca2+ sensitization by tp-CPI. 6. Our results indicate that phosphorylation of CPI-17 by PKC stimulates binding of CPI-17 to and subsequent inhibition of MLC phosphatase. This implies that CPI-17 accounts largely for the heretofore unknown signalling pathway between PKC and inhibited MLC phosphatase.

Indexed as

AnimalsAortaCalciumDose-Response Relationship, DrugEnzyme InhibitorsFemoral ArteryGuanosine DiphosphateMaleMuscle ContractionMuscle, Smooth, VascularMyosin-Light-Chain PhosphatasePeptide FragmentsPhosphoprotein PhosphatasesPhosphorylationProtein Kinase CProtein Phosphatase 2CalciumEnzyme Inhibitorsguanosine 5'-O-(2-thiodiphosphate)Guanosine DiphosphateMyosin-Light-Chain PhosphatasePeptide Fragmentsphosphoprotein phosphatase inhibitor 1Phosphoprotein PhosphatasesProtein Kinase Cprotein kinase C (19-31)Protein Phosphatase 2ProteinsRecombinant ProteinsSulfur CompoundsThionucleotides

Identifiers

PMID9518739
PMCPMC2230912
OpenAlexW2157631270

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.