Evidence map›Paper›PMID 36056254›Full record

ReviewJournal of molecular medicine (Berlin, Germany)2022

Polypeptide N-acetylgalactosamine transferase 3: a post-translational writer on human health.

Yohana Camila Garay, Romina Beatriz Cejas, Virginia Lorenz, Natacha Zlocowski, Pedro Parodi, Franco Alejandro Ferrero, Genaro Angeloni, Valentina Alfonso García, Victor German Sendra, Ricardo Dante Lardone and 1 more

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of molecular medicine (Berlin, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.3field-weighted citation impact, top 48% 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

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

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

11 authors at 3 institutions in 2 countries.

Yohana Camila Garay *Centro de Investigaciones en Química Biológica de Córdoba, CIQUIBIC, CONICET and Departamento de Química Biológica Ranwel Caputto, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ciudad Universitaria, X5000HUA, Córdoba, Argentina.
Romina Beatriz Cejas *Department of Pharmacology, Northwestern University Feinberg School of Medicine, Chicago, IL, 60611, USA.
Virginia Lorenz *Facultad de Bioquímica Y Ciencias Biológicas, Instituto de Salud Y Ambiente del Litoral (ISAL), Universidad Nacional del Litoral (UNL) - Consejo Nacional de Investigaciones Científicas Y Técnicas (CONICET), Santa Fe, Argentina.
Natacha ZlocowskiCentro de Microscopía Electrónica, Facultad de Ciencias Médicas, Instituto de Investigaciones en Ciencias de La Salud (INICSA-CONICET), Universidad Nacional de Córdoba, Córdoba, Argentina.
Pedro ParodiCentro de Investigaciones en Química Biológica de Córdoba, CIQUIBIC, CONICET and Departamento de Química Biológica Ranwel Caputto, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ciudad Universitaria, X5000HUA, Córdoba, Argentina.
Franco Alejandro FerreroCentro de Investigaciones en Química Biológica de Córdoba, CIQUIBIC, CONICET and Departamento de Química Biológica Ranwel Caputto, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ciudad Universitaria, X5000HUA, Córdoba, Argentina.
Genaro AngeloniCentro de Investigaciones en Química Biológica de Córdoba, CIQUIBIC, CONICET and Departamento de Química Biológica Ranwel Caputto, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ciudad Universitaria, X5000HUA, Córdoba, Argentina.
Valentina Alfonso GarcíaCentro de Investigaciones en Química Biológica de Córdoba, CIQUIBIC, CONICET and Departamento de Química Biológica Ranwel Caputto, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ciudad Universitaria, X5000HUA, Córdoba, Argentina.
Victor German SendraCenter for Translational Ocular Immunology, Department of Ophthalmology, Tufts Medical Center, Tufts University School of Medicine, Boston, MA, USA.
Ricardo Dante LardoneCentro de Investigaciones en Química Biológica de Córdoba, CIQUIBIC, CONICET and Departamento de Química Biológica Ranwel Caputto, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ciudad Universitaria, X5000HUA, Córdoba, Argentina.
Fernando José IrazoquiCentro de Investigaciones en Química Biológica de Córdoba, CIQUIBIC, CONICET and Departamento de Química Biológica Ranwel Caputto, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ciudad Universitaria, X5000HUA, Córdoba, Argentina. fernando.irazoqui@unc.edu.ar.ORCID 0000-0002-5874-8391
Consejo Nacional de Investigaciones Científicas y Técnicas · ARNorthwestern University · USTufts University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polypeptide N-acetylgalactosamine transferase 3 (ppGalNAc-T3) is an enzyme involved in the initiation of O-GalNAc glycan biosynthesis. Acting as a writer of frequent post-translational modification (PTM) on human proteins, ppGalNAc-T3 has key functions in the homeostasis of human cells and tissues. We review the relevant roles of this molecule in the biosynthesis of O-GalNAc glycans, as well as in biological functions related to human physiological and pathological conditions. With main emphasis in ppGalNAc-T3, we draw attention to the different ways involved in the modulation of ppGalNAc-Ts enzymatic activity. In addition, we take notice on recent reports of ppGalNAc-T3 having different subcellular localizations, highlight critical intrinsic and extrinsic functions in cellular physiology that are exerted by ppGalNAc-T3-synthesized PTMs, and provide an update on several human pathologies associated with dysfunctional ppGalNAc-T3. Finally, we propose biotechnological tools as new therapeutic options for the treatment of pathologies related to altered ppGalNAc-T3. KEY MESSAGES: ppGalNAc-T3 is a key enzyme in the human O-GalNAc glycans biosynthesis. enzyme activity is regulated by PTMs, lectin domain and protein-protein interactions. ppGalNAc-T3 is located in human Golgi apparatus and cell nucleus. ppGalNAc-T3 has a central role in cell physiology as well as in several pathologies. Biotechnological tools for pathological management are proposed.

Indexed as

Protein Processing, Post-TranslationalCell Physiological PhenomenaHumansN-AcetylgalactosaminyltransferasesPeptidesPolypeptide N-acetylgalactosaminyltransferasePolysaccharidesTransferasesN-AcetylgalactosaminyltransferasesPeptidesPolypeptide N-acetylgalactosaminyltransferasePolysaccharidesTransferasesGlycobiologyGlycosyltransferasesO-GlycansPost-translational modificationsPotential therapies

Identifiers

PMID36056254
OpenAlexW4294543920

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.