Evidence map›Paper›PMID 37507081›Full record

ArticleAnalytical biochemistry2023

Differential Detection of O-GlcNAcylated proteins in the heart using antibodies.

Bhargavi Narayanan, Fiddia Zahra, Russell A Reeves, Akanksha Aggarwal, Robert N O'Meally, Roger K Henry, Megan Craven, Avital Jacobson, Robert N Cole, Mark J Kohr and 2 more

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

Article in Analytical biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

8 citing papers in PubMed, 8 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

12 authors at 2 institutions in 1 country.

Bhargavi NarayananThe Department of Biological Chemistry at the Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Fiddia ZahraThe Department of Biological Chemistry at the Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Russell A ReevesThe Department of Biological Chemistry at the Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA; Department of Radiology, David Geffen School of Medicine at UCLA, Los Angeles, CA, 90095, USA.
Akanksha AggarwalThe Department of Biological Chemistry at the Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Robert N O'MeallyThe Mass Spectrometry and Proteomics Facility, The Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Roger K HenryThe Department of Biological Chemistry at the Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA; Department of Ophthalmology and Visual Sciences at the Rutgers University New Jersey Medical School Newark, NJ, 07103, USA.
Megan CravenThe Department of Biological Chemistry at the Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Avital JacobsonThe Department of Biological Chemistry at the Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Robert N ColeThe Department of Biological Chemistry at the Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA; The Mass Spectrometry and Proteomics Facility, The Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Mark J KohrThe Department of Environmental Health and Engineering, The Johns Hopkins Bloomberg School of Public Health, Baltimore, MD, 21205, USA.
Priya UmapathiThe Department Medicine at the Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Natasha E ZacharaThe Department of Biological Chemistry at the Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA; The Department of Oncology at the Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA. Electronic address: nzachara@jhmi.edu.
Johns Hopkins University · USRutgers, The State University of New Jersey · US

Funding

Translational Research Central ServicesP30CA006973 · NCI · JOHNS HOPKINS UNIVERSITY · PI Rosalie Wollett · 1985 to 2026
$208.6M
QAQC Johns Hopkins Institute for Clinical and Translational ResearchUL1TR003098 · NCATS · JOHNS HOPKINS UNIVERSITY · PI FORD, DANIEL ERNEST · 2019 to 2023
$57.7M
Immersive Training in GlycosciencesK12HL141952 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI HASCALL, VINCENT CHARLES, SCHNAAR, RONALD L · 2018 to 2022
$4.8M
Regulation of O-GlcNAcylation During InjuryR01HL139640 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI ZACHARA, NATASHA ELIZABETH · 2018 to 2021
$1.6M
Tuning and Tagging the O-GlcNAc ModificationU01CA230978 · NCI · JOHNS HOPKINS UNIVERSITY · PI ZACHARA, NATASHA ELIZABETH · 2018 to 2020
$1.3M
NCATS NIH HHS UL1 TR003098NCI NIH HHS P30 CA006973NCI NIH HHS U01 CA230978NHLBI NIH HHS K12 HL141952NHLBI NIH HHS R01 HL139640
6 · The paper itself

Abstract

Thousands of mammalian intracellular proteins are dynamically modified by O-linked β-N-acetylglucosamine (O-GlcNAc). Global changes in O-GlcNAcylation have been associated with the development of cardiomyopathy, heart failure, hypertension, and neurodegenerative disease. Levels of O-GlcNAc in cells and tissues can be detected using numerous approaches; however, immunoblotting using GlcNAc-specific antibodies and lectins is commonplace. The goal of this study was to optimize the detection of O-GlcNAc in heart lysates by immunoblotting. Using a combination of tissue fractionation, immunoblotting, and galactosyltransferase labeling, as well as hearts from wild-type and O-GlcNAc transferase transgenic mice, we demonstrate that contractile proteins in the heart are differentially detected by two commercially available antibodies (CTD110.6 and RL2). As CTD110.6 displays poor reactivity toward contractile proteins, and as these proteins represent a major fraction of the heart proteome, a better assessment of cardiac O-GlcNAcylation is obtained in total tissue lysates with RL2. The data presented highlight tissue lysis approaches that should aid the assessment of the cardiac O-GlcNAcylation by immunoblotting.

Indexed as

Neurodegenerative DiseasesAcetylglucosamineAnimalsAntibodiesContractile ProteinsHeartMammalsMiceProtein Processing, Post-TranslationalProteomeAcetylglucosamineAntibodiesContractile ProteinsProteomeAntibodiesClick chemistryGlycosylationHeartO-GlcNAc

Identifiers

PMID37507081
PMCPMC10523836
OpenAlexW4385365748

What OpenQuestion holds

Textmetadata
LicenceTDM
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.