Evidence map›Paper›PMID 23638346›Full record

ArticlePeerJ2013

Novel control of lactate dehydrogenase from the freeze tolerant wood frog: role of posttranslational modifications.

Jean Abboud, Kenneth B Storey

Open access · goldAbstract read
In one paragraph

Article in PeerJ, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

13 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Purification and characterization of a urea sensitive lactate dehydrogenase from skeletal muscle of the African clawed frog, Xenopus laevis.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2019
    Article
  5. Comparative Proteomic Analysis ofMolecules (Basel, Switzerland) · 2018
    Article
  6. Article
  7. Histone methylation in the freeze-tolerant wood frog (Rana sylvatica).Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2018
    Article
  8. Article
  9. Review
  10. Review
  11. Purification and characterization of a urea sensitive lactate dehydrogenase from the liver of the African clawed frog, Xenopus laevis.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2014
    Article
  12. Article
  13. Article
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

2 authors at 1 institution in 1 country.

Jean AbboudInstitute of Biochemistry, Department of Biology and Department of Chemistry , Carleton University , Canada.
Kenneth B Storey
Carleton University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lactate dehydrogenase (LDH), the terminal enzyme of anaerobic glycolysis, plays a crucial role both in sustaining glycolytic ATP production under oxygen-limiting conditions and in facilitating the catabolism of accumulated lactate when stress conditions are relieved. In this study, the effects on LDH of in vivo freezing and dehydration stresses (both of which impose hypoxia/anoxia stress on tissues) were examined in skeletal muscle of the freeze-tolerant wood frog, Rana sylvatica. LDH from muscle of control, frozen and dehydrated wood frogs was purified to homogeneity in a two-step process. The kinetic properties and stability of purified LDH were analyzed, revealing no significant differences in V max, K m and I 50 values between control and frozen LDH. However, control and dehydrated LDH differed significantly in K m values for pyruvate, lactate, and NAD, I 50 urea, and in temperature, glucose, and urea effects on these parameters. The possibility that posttranslational modification of LDH was responsible for the stable differences in enzyme behavior between control and dehydrated states was assessed using ProQ diamond staining to detect phosphorylation and immunoblotting to detect acetylation, methylation, ubiquitination, SUMOylation and nitrosylation of the enzyme. LDH from muscle of dehydrated wood frogs showed significantly lower levels of acetylation, providing one of the first demonstrations of a potential role for protein acetylation in the stress-responsive control of a metabolic enzyme.

Indexed as

CryobiologyDehydrationEnzyme regulationFreeze toleranceMuscle glycolysisPosttranslational modificationRana sylvatica

Identifiers

PMID23638346
PMCPMC3628601
OpenAlexW2019695389

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.