Evidence map›Paper›PMID 25608649›Full record

ArticleInternational journal of molecular sciences2015

Mechanisms of hyperhomocysteinemia induced skeletal muscle myopathy after ischemia in the CBS-/+ mouse model.

Sudhakar Veeranki, Suresh C Tyagi

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. HHandbook of experimental pharmacology · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. The Role of HAdvances in experimental medicine and biology · 2021
    Article
  8. Review
  9. Development of AD-Like Pathology in Skeletal Muscle.Journal of Parkinson's disease and Alzheimer's disease · 2019
    Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Hyperhomocysteinemia inhibits satellite cell regenerative capacity through p38 alpha/beta MAPK signaling.American journal of physiology. Heart and circulatory physiology · 2015
    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.

Sudhakar VeerankiDepartment of Physiology & Biophysics, University of Louisville, Louisville, KY 40202, USA. s0veer02@louisville.edu.
Suresh C TyagiDepartment of Physiology & Biophysics, University of Louisville, Louisville, KY 40202, USA. s0tyag01@exchange.louisville.edu.
University of Louisville · US

Funding

Reversing diabetic muscle myopathy by exercise and exosomesR01HL074185 · NHLBI · UNIVERSITY OF LOUISVILLE · PI TYAGI, SURESH C. · 2003 to 2018
$5.7M
Mechanisms of Homocysteine-Induced Fibrinogen-Amyloid Plaque FormationR01NS084823 · NINDS · UNIVERSITY OF LOUISVILLE · PI LOMINADZE, DAVID, TYAGI, SURESH C. · 2013 to 2017
$2.7M
Mitophagic and anti-angiogenic mechanism of heart failureR01HL108621 · NHLBI · UNIVERSITY OF LOUISVILLE · PI TYAGI, SURESH C. · 2011 to 2015
$1.8M
NHLBI NIH HHS HL-108621NHLBI NIH HHS HL-74185NHLBI NIH HHS R01 HL074185NHLBI NIH HHS R01 HL108621NINDS NIH HHS NS-84823NINDS NIH HHS R01 NS084823
6 · The paper itself

Abstract

Although hyperhomocysteinemia (HHcy) elicits lower than normal body weights and skeletal muscle weakness, the mechanisms remain unclear. Despite the fact that HHcy-mediated enhancement in ROS and consequent damage to regulators of different cellular processes is relatively well established in other organs, the nature of such events is unknown in skeletal muscles. Previously, we reported that HHcy attenuation of PGC-1α and HIF-1α levels enhanced the likelihood of muscle atrophy and declined function after ischemia. In the current study, we examined muscle levels of homocysteine (Hcy) metabolizing enzymes, anti-oxidant capacity and focused on protein modifications that might compromise PGC-1α function during ischemic angiogenesis. Although skeletal muscles express the key enzyme (MTHFR) that participates in re-methylation of Hcy into methionine, lack of trans-sulfuration enzymes (CBS and CSE) make skeletal muscles more susceptible to the HHcy-induced myopathy. Our study indicates that elevated Hcy levels in the CBS-/+ mouse skeletal muscles caused diminished anti-oxidant capacity and contributed to enhanced total protein as well as PGC-1α specific nitrotyrosylation after ischemia. Furthermore, in the presence of NO donor SNP, either homocysteine (Hcy) or its cyclized version, Hcy thiolactone, not only increased PGC-1α specific protein nitrotyrosylation but also reduced its association with PPARγ in C2C12 cells. Altogether these results suggest that HHcy exerts its myopathic effects via reduction of the PGC-1/PPARγ axis after ischemia.

Indexed as

AnimalsAntioxidantsBlotting, WesternCystathionine beta-SynthaseDisease Models, AnimalHomocysteineHyperhomocysteinemiaIschemiaMice, Inbred C57BLModels, BiologicalMuscle, SkeletalMuscular DiseasesNitric Oxide DonorsPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaPPAR gammaProtein Binding3-nitrotyrosineAntioxidantsCystathionine beta-SynthaseHomocysteineNitric Oxide DonorsPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaPPAR gammaPpargc1a protein, mouseTranscription FactorsTyrosine

Identifiers

PMID25608649
PMCPMC4307302
OpenAlexW2079617651

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.