Evidence map›Paper›PMID 17182736›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

A quantitative study of bioenergetics in skeletal muscle lacking carbonic anhydrase III using 31P magnetic resonance spectroscopy.

M Liu, G A Walter, N C Pathare, R E Forster, K Vandenborne

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
9.3field-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

26 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Lactic acidosis: implications for human exercise performance.European journal of applied physiology · 2025
    Review
  3. Article
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  5. Mitochondria-localized AMPK responds to local energetics and contributes to exercise and energetic stress-induced mitophagy.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Review
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  18. Extramitochondrial domain rich in carbonic anhydrase activity improves myocardial energetics.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. 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

5 authors at 2 institutions in 1 country.

M LiuDepartment of Physical Therapy, University of Florida, Gainesville, FL 32610-0154, USA.
G A Walter
N C Pathare
R E Forster
K Vandenborne
University of Florida · USUniversity of Pennsylvania · US

Funding

METABOLIC AND TRANSPORT PATHWAYS IN SKELETAL MUSCLER01AR045394 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI FORSTER, ROBERT E · 2000 to 2004
$1.5M
NIAMS NIH HHS AR45394NIAMS NIH HHS R01 AR045394
6 · The paper itself

Abstract

Oxidative slow skeletal muscle contains carbonic anhydrase III in high concentration, but its primary function remains unknown. To determine whether its lack handicaps energy metabolism and/or acid elimination, we measured the intracellular pH and energy phosphates by (31)P magnetic resonance spectroscopy in hind limb muscles of wild-type and CA III knockout mice during and after ischemia and intense exercise (electrical stimulation). Thirty minutes of ischemia caused phosphocreatine (PCr) to fall and P(i) to rise while pH and ATP remained constant in both strains of mice. PCr and P(i) kinetics during ischemia and recovery were not significantly different between the two genotypes. From this we conclude that under neutral pH conditions resting muscle anaerobic metabolism, the rate of the creatine kinase reaction, intracellular buffering of protons, and phosphorylation of creatine by mitochondrial oxygen metabolism are not influenced by the lack of CA III. Two minutes of intense stimulation of the mouse gastrocnemius caused PCr, ATP, and pH to fall and ADP and P(i) to rise, and these changes, with the exception of ATP, were all significantly larger in the CA III knockouts. The rate of return of pH and ADP to control values was the same in wild-type and mutant mice, but in the mutants PCr and P(i) recovery were delayed in the first minute after stimulation. Because the tension decrease during fatigue is known to be the same in the two genotypes, we conclude that a lack of CA III impairs mitochondrial ATP synthesis.

Indexed as

Energy MetabolismAdenosine TriphosphateAnimalsCarbonic Anhydrase IIIFemaleHydrogen-Ion ConcentrationMagnetic Resonance SpectroscopyMaleMiceMice, KnockoutMuscle, SkeletalAdenosine TriphosphateCarbonic Anhydrase III

Identifiers

PMID17182736
PMCPMC1765468
OpenAlexW2049338248

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.