Enhanced Eryptosis in Glucose-6-Phosphate Dehydrogenase Deficiency.


Journal

Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology
ISSN: 1421-9778
Titre abrégé: Cell Physiol Biochem
Pays: Germany
ID NLM: 9113221

Informations de publication

Date de publication:
11 Dec 2021
Historique:
accepted: 15 01 2021
entrez: 11 12 2021
pubmed: 12 12 2021
medline: 8 2 2022
Statut: ppublish

Résumé

Defects in the Glucose-6-Phosphate Dehydrogenase (G6PD) enzyme enhance cellular oxidative damage, thus impairing erythrocytes and radically shortening their lifespan. We aimed to study programmed erythrocyte cell death in G6PD-deficient patients, describe the molecular genetics basis of G6PD and investigate phenotype-genotype correlations. We explored eryptosis using the annexin V-binding assay, taken as an indicator of PS exposure at the erythrocyte surface. We assessed reactive oxygen species (ROS) production, intracellular calcium concentrations and ceramide formation at the cell surface. Prior to and following treatments, cells were analyzed by flow cytometry. Finally, we explored G6PD gene mutations through PCR-Sanger sequencing. Before stimulation, PS-exposing erythrocytes were significantly higher in G6PD-deficient patients than in healthy volunteers. This was paralleled by a significant increase in reactive oxygen species production, suggesting that oxidative stress is the main trigger of PS exposure in G6PD-deficient erythrocytes. Five previously described mutations were detected in our patients. Two genotypes correlated with a significantly higher percentage of PS-exposing cells. Our study uncovers a novel effect detected in G6PD-deficient erythrocytes which is cell membrane scrambling with PS translocation to the erythrocyte surface. Our findings shed a light on the mechanisms of premature erythrocyte clearance in G6PD deficiency.

Sections du résumé

BACKGROUND/AIMS OBJECTIVE
Defects in the Glucose-6-Phosphate Dehydrogenase (G6PD) enzyme enhance cellular oxidative damage, thus impairing erythrocytes and radically shortening their lifespan. We aimed to study programmed erythrocyte cell death in G6PD-deficient patients, describe the molecular genetics basis of G6PD and investigate phenotype-genotype correlations.
METHODS METHODS
We explored eryptosis using the annexin V-binding assay, taken as an indicator of PS exposure at the erythrocyte surface. We assessed reactive oxygen species (ROS) production, intracellular calcium concentrations and ceramide formation at the cell surface. Prior to and following treatments, cells were analyzed by flow cytometry. Finally, we explored G6PD gene mutations through PCR-Sanger sequencing.
RESULTS RESULTS
Before stimulation, PS-exposing erythrocytes were significantly higher in G6PD-deficient patients than in healthy volunteers. This was paralleled by a significant increase in reactive oxygen species production, suggesting that oxidative stress is the main trigger of PS exposure in G6PD-deficient erythrocytes. Five previously described mutations were detected in our patients. Two genotypes correlated with a significantly higher percentage of PS-exposing cells.
CONCLUSION CONCLUSIONS
Our study uncovers a novel effect detected in G6PD-deficient erythrocytes which is cell membrane scrambling with PS translocation to the erythrocyte surface. Our findings shed a light on the mechanisms of premature erythrocyte clearance in G6PD deficiency.

Identifiants

pubmed: 34894207
doi: 10.33594/000000474
doi:

Substances chimiques

Annexin A5 0
Reactive Oxygen Species 0

Types de publication

Clinical Trial Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

761-772

Informations de copyright

© Copyright by the Author(s). Published by Cell Physiol Biochem Press.

Déclaration de conflit d'intérêts

The authors declare that no conflicts of interest exist.

Auteurs

Ghada Bouguerra (G)

Université de Tunis El Manar, Faculté de Médecine de Tunis, Tunis, Tunisie, ghada.bouguerra@yahoo.fr.
Université de Tunis El Manar, Laboratoire d'Hématologie Moléculaire et Cellulaire, Institut Pasteur de Tunis, Tunis, Tunisie.

Khaoula Talbi (K)

Université de Tunis El Manar, Laboratoire d'Hématologie Moléculaire et Cellulaire, Institut Pasteur de Tunis, Tunis, Tunisie.
Université de Tunis El Manar, Faculté des Sciences de Tunis, Tunis, Tunisie.

Nawel Trabelsi (N)

Université de Tunis El Manar, Laboratoire d'Hématologie Moléculaire et Cellulaire, Institut Pasteur de Tunis, Tunis, Tunisie.
Université de Tunis El Manar, Faculté des Sciences de Tunis, Tunis, Tunisie.

Dorra Chaouachi (D)

Université de Tunis El Manar, Laboratoire d'Hématologie Moléculaire et Cellulaire, Institut Pasteur de Tunis, Tunis, Tunisie.

Imen Boudriga (I)

Université de Tunis El Manar, Laboratoire d'Hématologie Moléculaire et Cellulaire, Institut Pasteur de Tunis, Tunis, Tunisie.

Salem Abbès (S)

Université de Tunis El Manar, Faculté de Médecine de Tunis, Tunis, Tunisie.
Université de Tunis El Manar, Laboratoire d'Hématologie Moléculaire et Cellulaire, Institut Pasteur de Tunis, Tunis, Tunisie.

Samia Menif (S)

Université de Tunis El Manar, Faculté de Médecine de Tunis, Tunis, Tunisie.
Université de Tunis El Manar, Laboratoire d'Hématologie Moléculaire et Cellulaire, Institut Pasteur de Tunis, Tunis, Tunisie.

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Classifications MeSH