Human apolipoprotein L1 interferes with mitochondrial function in Saccharomyces cerevisiae.


Journal

Molecular medicine reports
ISSN: 1791-3004
Titre abrégé: Mol Med Rep
Pays: Greece
ID NLM: 101475259

Informations de publication

Date de publication:
09 2020
Historique:
received: 20 10 2019
accepted: 24 04 2020
pubmed: 26 6 2020
medline: 21 4 2021
entrez: 26 6 2020
Statut: ppublish

Résumé

To the best of our knowledge, the vertebrate apolipoprotein L (APOL) family has not previously been ascribed to any definite pathophysiological function, although the conserved BH3 protein domain suggests a role in programmed cell death or an interference with mitochondrial processes. In the present study, the human APOL1 was expressed in the yeast Saccharomyces cerevisiae in order to determine the molecular action of APOL1. APOL1 inhibited cell proliferation in a non‑fermentable carbon source, such as glycerol, while it had no effect on proliferation in fermentable carbon sources, such as galactose. APOL1, expressed in yeast, is localized in the mitochondrial fraction, as determined via western blotting. APOL1 induced a loss of mitochondrial function, demonstrated by a loss of respiratory index, and mitochondrial membrane potential. Green fluorescent protein tagging of mitochondrial protein revealed that APOL1 was associated with abnormal mitochondrial and lysosomal morphologies, observed by a loss of the normal mitochondrial tubular network. Thus, the results of the present study suggest that APOL1 could be a physiological regulator of mitochondrial function.

Identifiants

pubmed: 32583004
doi: 10.3892/mmr.2020.11271
pmc: PMC7411449
doi:

Substances chimiques

APOL1 protein, human 0
Apolipoprotein L1 0
Recombinant Proteins 0
Glycerol PDC6A3C0OX

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

1910-1920

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Auteurs

Mounia Chidiac (M)

Laboratory of Molecular Parasitology, Laboratory of Gene Molecular Biology, IBMM, Université Libre de Bruxelles, 6041 Gosselies, Belgium.

Jalil Daher (J)

Department of Biology, University of Balamand, P.O. Box 100, Tripoli, Lebanon.

Mélanie Boeckstaens (M)

Laboratory of Membrane Transport Biology, IBMM, Faculty of Sciences, Université Libre de Bruxelles, 6041 Gosselies, Belgium.

Philippe Poelvoorde (P)

Laboratory of Molecular Parasitology, Laboratory of Gene Molecular Biology, IBMM, Université Libre de Bruxelles, 6041 Gosselies, Belgium.

Bassam Badran (B)

Department of Biochemistry, Laboratory of Immunology, Lebanese University, Faculty of Sciences, P.O. Box 6573, Hadath‑Beirut, Lebanon.

Anna Maria Marini (AM)

Laboratory of Membrane Transport Biology, IBMM, Faculty of Sciences, Université Libre de Bruxelles, 6041 Gosselies, Belgium.

Roy Khalaf (R)

Department of Natural Sciences, Lebanese American University, P.O. Box 36, Byblos, Lebanon.

Luc Vanhamme (L)

Laboratory of Molecular Parasitology, Laboratory of Gene Molecular Biology, IBMM, Université Libre de Bruxelles, 6041 Gosselies, Belgium.

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