Evidence map›Paper›PMID 39021187›Full record

ArticleProtein and peptide letters2024

A Functional Human Glycogen Debranching Enzyme Encoded by a Synthetic Gene: Its Implications for Glycogen Storage Disease Type III Management.

Doriana Triggiani, Olivia C Demurtas, Elena Illiano, Silvia Massa, Alessandra Pasquo, Carlo Dionisi-Vici, Carmela Marino, Giovanni Giuliano, Rosella Franconi

Abstract read
PubMed Publisher
In one paragraph

Article in Protein and peptide letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

9 authors.

Doriana TriggianiDepartment of Sustainability, ENEA, Italian National Agency for New Technologies, Energy and Sustainable Economic Development, Casaccia Research Center, Via Anguillarese 301, 00123, Rome, Italy.
Olivia C DemurtasDepartment of Sustainability, ENEA, Italian National Agency for New Technologies, Energy and Sustainable Economic Development, Casaccia Research Center, Via Anguillarese 301, 00123, Rome, Italy.
Elena IllianoDepartment of Sustainability, ENEA, Italian National Agency for New Technologies, Energy and Sustainable Economic Development, Casaccia Research Center, Via Anguillarese 301, 00123, Rome, Italy.
Silvia MassaDepartment of Sustainability, ENEA, Italian National Agency for New Technologies, Energy and Sustainable Economic Development, Casaccia Research Center, Via Anguillarese 301, 00123, Rome, Italy.
Alessandra PasquoDepartment of FSNTECFIS-DIM ENEA, Italian National Agency for New Technologies, Energy and Sustainable Economic Development, Frascati Research Center, Via Enrico Fermi 45, 00044, Frascati RM, Italy.
Carlo Dionisi-ViciDivision of Metabolic Diseases and Hepatology, Ospedale Pediatrico Bambino Gesù IRCCS, Piazza S. Onofrio 4, 00165, Rome, Italy.
Carmela MarinoDepartment of Sustainability, ENEA, Italian National Agency for New Technologies, Energy and Sustainable Economic Development, Casaccia Research Center, Via Anguillarese 301, 00123, Rome, Italy.
Giovanni GiulianoDepartment of Sustainability, ENEA, Italian National Agency for New Technologies, Energy and Sustainable Economic Development, Casaccia Research Center, Via Anguillarese 301, 00123, Rome, Italy.
Rosella FranconiDepartment of Sustainability, ENEA, Italian National Agency for New Technologies, Energy and Sustainable Economic Development, Casaccia Research Center, Via Anguillarese 301, 00123, Rome, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundGlycogen Storage Disease type III (GSD III) is a metabolic disorder resulting from a deficiency of the Glycogen Debranching Enzyme (GDE), a large monomeric protein (approximately 170 kDa) with cytoplasmic localization and two distinct enzymatic activities: 4-α-glucantransferase and amylo-α-1,6-glucosidase. Mutations in the Agl gene, with consequent deficiency in GDE, lead to the accumulation of abnormal/toxic glycogen with shorter chains (phosphorylase limit dextrin, PLD) in skeletal and/or heart muscle and/or in the liver. Currently, there is no targeted therapy, and available treatments are symptomatic, relying on specific diets.

methodsEnzyme Replacement Therapy (ERT) might represent a potential therapeutic strategy for GSD III. Moreover, the single-gene nature of GSD III, the subcellular localization of GDE, and the type of affected tissues represent ideal conditions for exploring gene therapy approaches. Toward this direction, we designed a synthetic, codon-optimized cDNA encoding the human GDE.

resultsThis gene yielded high amounts of soluble, enzymatically active protein in Escherichia coli. Moreover, when transfected in Human Embryonic Kidney cells (HEK-293), it successfully encoded a functional GDE.

conclusionThese results suggest that our gene or protein might complement the missing function in GSD III patients, opening the door to further exploration of therapeutic approaches for this disease.

Indexed as

Glycogen Debranching Enzyme SystemGlycogen Storage Disease Type IIIEnzyme Replacement TherapyEscherichia coliGenetic TherapyHEK293 CellsHumansRecombinant ProteinsGlycogen Debranching Enzyme SystemRecombinant Proteinsenzymegene therapy.Glycogen Debranching Enzyme (GDE)Glycogenosis type IIIGlycogen Storage Disease (GSD)rare disease

Identifiers

PMID39021187

What OpenQuestion holds

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Registered trials

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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.