Evidence map›Paper›PMID 27758871›Full record

ArticleThe Journal of biological chemistry2016

Novel Molecular Interactions of Acylcarnitines and Fatty Acids with Myoglobin.

Sree V Chintapalli, Srinivas Jayanthi, Prema L Mallipeddi, Ravikumar Gundampati, Thallapuranam Krishnaswamy Suresh Kumar, Damian B van Rossum, Andriy Anishkin, Sean H Adams

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Metabolic physiology and skeletal muscle phenotypes in male and female myoglobin knockout mice.American journal of physiology. Endocrinology and metabolism · 2021
    Article
  18. Article
  19. Article
  20. 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

8 authors.

Sree V ChintapalliFrom the Arkansas Children's Nutrition Center and Department of Pediatrics, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72202, svchintapalli@uams.edu.
Srinivas Jayanthithe Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas 72701.
Prema L Mallipeddithe Department of Biology and Biochemistry, University of Houston, Houston, Texas 77204.
Ravikumar Gundampatithe Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas 72701.
Thallapuranam Krishnaswamy Suresh Kumarthe Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas 72701.
Damian B van Rossumthe Center for Computational Proteomics and.
Andriy Anishkinthe Department of Biology, University of Maryland, College Park, Maryland 20742.
Sean H AdamsFrom the Arkansas Children's Nutrition Center and Department of Pediatrics, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72202, shadams@uams.edu.

Funding

Identification of Muscle-Specific Biomarkers of Fatty Acid beta-OxidationR01DK078328 · NIDDK · U.S. AGRICULTURAL RESEARCH SERVICE · PI ADAMS, SEAN HARRISON · 2008 to 2012
$1.8M
Biopolymer-based strategies for local delivery of cytokine therapeuticsR01CA172631 · NCI · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI ZAHAROFF, DAVID · 2014 to 2018
$1.5M
NCI NIH HHS R01 CA172631NIDDK NIH HHS R01 DK078328
6 · The paper itself

Abstract

Previous research has indicated that long-chain fatty acids can bind myoglobin (Mb) in an oxygen-dependent manner. This suggests that oxy-Mb may play an important role in fuel delivery in Mb-rich muscle fibers (e.g. type I fibers and cardiomyocytes), and raises the possibility that Mb also serves as an acylcarnitine-binding protein. We report for the first time the putative interaction and affinity characteristics for different chain lengths of both fatty acids and acylcarnitines with oxy-Mb using molecular dynamic simulations and isothermal titration calorimetry experiments. We found that short- to medium-chain fatty acids or acylcarnitines (ranging from C2:0 to C10:0) fail to achieve a stable conformation with oxy-Mb. Furthermore, our results indicate that C12:0 is the minimum chain length essential for stable binding of either fatty acids or acylcarnitines with oxy-Mb. Importantly, the empirical lipid binding studies were consistent with structural modeling. These results reveal that: (i) the lipid binding affinity for oxy-Mb increases as the chain length increases (i.e. C12:0 to C18:1), (ii) the binding affinities of acylcarnitines are higher when compared with their respective fatty acid counterparts, and (iii) both fatty acids and acylcarnitines bind to oxy-Mb in 1:1 stoichiometry. Taken together, our results support a model in which oxy-Mb is a novel regulator of long-chain acylcarnitine and fatty acid pools in Mb-rich tissues. This has important implications for physiological fuel management during exercise, and relevance to pathophysiological conditions (e.g. fatty acid oxidation disorders and cardiac ischemia) where long-chain acylcarnitine accumulation is evident.

Indexed as

Models, ChemicalAnimalsCarnitineFatty AcidsHorsesMyoglobinacylcarnitineCarnitineFatty AcidsMyoglobinisothermal titration calorimetry (ITC)lipid binding proteinlipotoxicitymolecular dockingmolecular dynamicsmyoglobinpolyunsaturated fatty acid (PUFA)

Identifiers

PMID27758871
PMCPMC5122780

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.