Evidence map›Paper›PMID 34735873›Full record

ArticleBiochemical and biophysical research communications2021

Cardiomyocyte protein O-GlcNAcylation is regulated by GFAT1 not GFAT2.

Adam A Nabeebaccus, Sharwari Verma, Anna Zoccarato, Giulia Emanuelli, Celio Xc Santos, Katrin Streckfuss-Bömeke, Ajay M Shah

Open access · hybridAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2021. 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
2.7field-weighted citation impact, top 9% 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, 17 citations in OpenAlex.

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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

7 authors at 2 institutions in 2 countries.

Adam A NabeebaccusBHF Centre of Excellence King's College London, The James Black Centre, 125 Coldharbour Lane, London, SE5 9NU, UK. Electronic address: adam.a.nabeebaccus@kcl.ac.uk.
Sharwari VermaBHF Centre of Excellence King's College London, The James Black Centre, 125 Coldharbour Lane, London, SE5 9NU, UK.
Anna ZoccaratoBHF Centre of Excellence King's College London, The James Black Centre, 125 Coldharbour Lane, London, SE5 9NU, UK.
Giulia EmanuelliBHF Centre of Excellence King's College London, The James Black Centre, 125 Coldharbour Lane, London, SE5 9NU, UK.
Celio Xc SantosBHF Centre of Excellence King's College London, The James Black Centre, 125 Coldharbour Lane, London, SE5 9NU, UK.
Katrin Streckfuss-BömekeGerman Centre for Cardiovascular Research, 10785 Berlin, partnersite Göttingen, Germany; Institute of Pharmacology and Toxicology, University of Würzburg, 97078 Würzburg, Germany.
Ajay M ShahBHF Centre of Excellence King's College London, The James Black Centre, 125 Coldharbour Lane, London, SE5 9NU, UK.
King's College London · GBUniversity of Würzburg · DE

Funding

British Heart Foundation RG/13/11/30384British Heart Foundation RG/20/3/34823
6 · The paper itself

Abstract

In response to cardiac injury, increased activity of the hexosamine biosynthesis pathway (HBP) is linked with cytoprotective as well as adverse effects depending on the type and duration of injury. Glutamine-fructose amidotransferase (GFAT; gene name gfpt) is the rate-limiting enzyme that controls flux through HBP. Two protein isoforms exist in the heart called GFAT1 and GFAT2. There are conflicting data on the relative importance of GFAT1 and GFAT2 during stress-induced HBP responses in the heart. Using neonatal rat cardiac cell preparations, targeted knockdown of GFPT1 and GFPT2 were performed and HBP activity measured. Immunostaining with specific GFAT1 and GFAT2 antibodies was undertaken in neonatal rat cardiac preparations and murine cardiac tissues to characterise cell-specific expression. Publicly available human heart single cell sequencing data was interrogated to determine cell-type expression. Western blots for GFAT isoform protein expression were performed in human cardiomyocytes derived from induced pluripotent stem cells (iPSCs). GFPT1 but not GFPT2 knockdown resulted in a loss of stress-induced protein O-GlcNAcylation in neonatal cardiac cell preparations indicating reduced HBP activity. In rodent cells and tissue, immunostaining for GFAT1 identified expression in both cardiac myocytes and fibroblasts whereas immunostaining for GFAT2 was only identified in fibroblasts. Further corroboration of findings in human heart cells identified an enrichment of GFPT2 gene expression in cardiac fibroblasts but not ventricular myocytes whereas GFPT1 was expressed in both myocytes and fibroblasts. In human iPSC-derived cardiomyocytes, only GFAT1 protein was expressed with an absence of GFAT2. In conclusion, these results indicate that GFAT1 is the primary cardiomyocyte isoform and GFAT2 is only present in cardiac fibroblasts. Cell-specific isoform expression may have differing effects on cell function and should be considered when studying HBP and GFAT functions in the heart.

Indexed as

AnimalsFibroblastsGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)HexosaminesInduced Pluripotent Stem CellsMiceMyocardiumMyocytes, CardiacProtein IsoformsRatsRats, Sprague-DawleyGFPT1 protein, humanGFPT2 protein, humanGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)HexosaminesProtein IsoformsGFAT1GFAT2GFPT1GFPT2Hexosamine biosynthesis pathwayO-GlcNAc

Identifiers

PMID34735873
PMCPMC8606754
OpenAlexW3210186904

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.