Evidence map›Paper›PMID 19349274›Full record

ArticleThe Journal of biological chemistry2009

Signaling processes for initiating smooth muscle contraction upon neural stimulation.

Hai-Lei Ding, Jeffrey W Ryder, James T Stull, Kristine E Kamm

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

43 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
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  3. Review
  4. Lead acetate versus cadmium sulfate in the modulation of main physiological pathways controlling detrusor muscle contractility in rat.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2022
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  12. Cardiac myosin light chain is phosphorylated by Ca2+/calmodulin-dependent and -independent kinase activities.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Article
  14. Control of urinary drainage and voiding.Clinical journal of the American Society of Nephrology : CJASN · 2015
    Review
  15. Article
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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

4 authors at 1 institution in 1 country.

Hai-Lei DingDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
Jeffrey W Ryder
James T Stull
Kristine E Kamm
The University of Texas Southwestern Medical Center · US

Funding

MYOSIN LIGHT CHAIN KINASE FUNCTION IN SMOOTH MUSCLER01HL026043 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI STULL, JAMES T · 1985 to 2009
$3.4M
BIOCHEMICAL MECHANISMS OF SMOOTH MUSCLE CONTRACTIONR37HL026043 · NHLBI · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI STULL, JAMES T · 1991 to 1999
–
NHLBI NIH HHS HL26043NHLBI NIH HHS R01 HL026043NHLBI NIH HHS R37 HL026043
6 · The paper itself

Abstract

Relationships among biochemical signaling processes involved in Ca2+/calmodulin (CaM)-dependent phosphorylation of smooth muscle myosin regulatory light chain (RLC) by myosin light chain kinase (MLCK) were determined. A genetically-encoded biosensor MLCK for measuring Ca(2+)-dependent CaM binding and activation was expressed in smooth muscles of transgenic mice. We performed real-time evaluations of the relationships among [Ca2+](i), MLCK activation, and contraction in urinary bladder smooth muscle strips neurally stimulated for 3 s. Latencies for the onset of [Ca2+](i) and kinase activation were 55 +/- 8 and 65 +/- 6 ms, respectively. Both increased with RLC phosphorylation at 100 ms, whereas force latency was 109 +/- 3 ms. [Ca2+](i), kinase activation, and RLC phosphorylation responses were maximal by 1.2 s, whereas force increased more slowly to a maximal value at 3 s. A delayed temporal response between RLC phosphorylation and force is probably due to mechanical effects associated with elastic elements in the tissue. MLCK activation partially declined at 3 s of stimulation with no change in [Ca2+](i) and also declined more rapidly than [Ca2+](i) during relaxation. The apparent desensitization of MLCK to Ca2+ activation appears to be due to phosphorylation in its calmodulin binding segment. Phosphorylation of two myosin light chain phosphatase regulatory proteins (MYPT1 and CPI-17) or a protein implicated in strengthening membrane adhesion complexes for force transmission (paxillin) did not change during force development. Thus, neural stimulation leads to rapid increases in [Ca2+](i), MLCK activation, and RLC phosphorylation in phasic smooth muscle, showing a tightly coupled Ca2+ signaling complex as an elementary mechanism initiating contraction.

Indexed as

AnimalsCalciumCalmodulinElectric StimulationIsometric ContractionKineticsMiceMice, TransgenicMuscle ContractionMuscle, SmoothMyosin-Light-Chain KinaseNeuronsSignal TransductionUrinary BladderCalciumCalmodulinMyosin-Light-Chain Kinase

Identifiers

PMID19349274
PMCPMC2708850
OpenAlexW2095949077

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.