Evidence map›Paper›PMID 12154187›Full record

ArticleThe Journal of physiology2002

An asymmetry in the phosphate dependence of tension transients induced by length perturbation in mammalian (rabbit psoas) muscle fibres.

K W Ranatunga, Moira E Coupland, G Mutungi

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

34 citing papers in PubMed, 52 citations in OpenAlex.

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  7. Myosin Cross-Bridge Behaviour in Contracting Muscle-The TInternational journal of molecular sciences · 2019
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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

3 authors at 1 institution in 1 country.

K W RanatungaDepartment of Physiology, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, UK. k.w.ranatunga@bristol.ac.uk
Moira E Coupland
G Mutungi
University of Bristol · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The effects of inorganic phosphate (P(i), a product released during ATP hydrolysis in active muscle) on tension transients induced by length perturbation (approximately 0.3 ms) were examined in chemically skinned (0.5 % Brij), maximally Ca(2+)-activated rabbit psoas muscle fibres at 10 degrees C (ionic strength 200 mM, pH 7.1). In one type of experiment, the tension transients induced by length release and stretch of a standard amplitude (0.4-0.5 % of L(o), muscle fibre length) were examined at a range of added [P(i)] (range 3-25 mM). The steady active tension was depressed approximately 45 % with 25 mM added P(i). The initial tension recovery (from T(1), extreme tension reached after length step, to T(2), tension after quick recovery) was analysed by half-time measurement and also by exponential curve fitting - extracting a fast (phase 2a) and a slow (phase 2b) component. The tension decay after a stretch became faster with increased [P(i)], whereas the quick tension rise induced by a length release was insensitive to added P(i). Consequently, the asymmetry in the speed of tension recovery from stretch and release was reduced at high [P(i)]. A plot of the phase 2b rate (or 1/half-time) of tension decay after stretch versus [P(i)] was approximately hyperbolic and showed saturation at higher [P(i)] levels. In a second type of experiment, the tension transients induced by length steps of different amplitudes were examined in control (no added P(i)) and in the presence of 25 mM added P(i). Over a range of length step amplitudes (up to 1 % L(0)), the tension decay after stretch was consistently faster in the presence of P(i) than in the control; this was particularly pronounced in phase 2b. The rate of tension rise after length release remained high but similar in the presence and absence of added P(i). These observations indicate that a stretch and release perturb different molecular steps in the crossbridge cycle. The P(i) sensitivity of tension decay (phase 2b) after stretch is similar to that seen using other perturbations (e.g. [P(i)] jumps, hydrostatic pressure jumps and temperature jumps and sinusoidal length oscillations). The results indicate that the P(i)-sensitive force generation identified in previous studies is strain sensitive (as expected), but it is seen only with respect to positive strain (stretches).

Indexed as

AnimalsIn Vitro TechniquesMaleMuscle ContractionMuscle Fibers, SkeletalPhosphatesPsoas MusclesRabbitsStress, MechanicalPhosphates

Identifiers

PMID12154187
PMCPMC2290445
OpenAlexW2030967378

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.