Chemotherapy selection pressure alters sphingolipid composition and mitochondrial bioenergetics in resistant HL-60 cells.


Journal

Journal of lipid research
ISSN: 1539-7262
Titre abrégé: J Lipid Res
Pays: United States
ID NLM: 0376606

Informations de publication

Date de publication:
09 2019
Historique:
received: 08 07 2019
revised: 27 07 2019
pubmed: 1 8 2019
medline: 21 7 2020
entrez: 1 8 2019
Statut: ppublish

Résumé

The combination of daunorubicin (dnr) and cytarabine (Ara-C) is a cornerstone of treatment for acute myelogenous leukemia (AML); resistance to these drugs is a major cause of treatment failure. Ceramide, a sphingolipid (SL), plays a critical role in cancer cell apoptosis in response to chemotherapy. Here, we investigated the effects of chemotherapy selection pressure with Ara-C and dnr on SL composition and enzyme activity in the AML cell line HL-60. Resistant cells, those selected for growth in Ara-C- and dnr-containing medium (HL-60/Ara-C and HL-60/dnr, respectively), demonstrated upregulated expression and activity of glucosylceramide synthase, acid ceramidase (AC), and sphingosine kinase 1 (SPHK1); were more resistant to ceramide than parental cells; and displayed sensitivity to inhibitors of SL metabolism. Lipidomic analysis revealed a general ceramide deficit and a profound upswing in levels of sphingosine 1-phosphate (S1P) and ceramide 1-phosphate (C1P) in HL-60/dnr cells versus parental and HL-60/Ara-C cells. Both chemotherapy-selected cells also exhibited comprehensive upregulations in mitochondrial biogenesis consistent with heightened reliance on oxidative phosphorylation, a property that was partially reversed by exposure to AC and SPHK1 inhibitors and that supports a role for the phosphorylation system in resistance. In summary, dnr and Ara-C selection pressure induces acute reductions in ceramide levels and large increases in S1P and C1P, concomitant with cell resilience bolstered by enhanced mitochondrial remodeling. Thus, strategic control of ceramide metabolism and further research to define mitochondrial perturbations that accompany the drug-resistant phenotype offer new opportunities for developing therapies that regulate cancer growth.

Identifiants

pubmed: 31363040
pii: S0022-2275(20)32320-8
doi: 10.1194/jlr.RA119000251
pmc: PMC6718434
pii:
doi:

Substances chimiques

(2R,3Z)-N-(1-hydroxyoctadec-3-en-2-yl)pivalamide 0
Amides 0
Ceramides 0
Fatty Acids, Unsaturated 0
Lysophospholipids 0
Sphingolipids 0
ceramide 1-phosphate 0
sphingosine 1-phosphate 26993-30-6
Glucosyltransferases EC 2.4.1.-
ceramide glucosyltransferase EC 2.4.1.80
Ceramidases EC 3.5.1.23
Sphingosine NGZ37HRE42

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1590-1602

Subventions

Organisme : NCI NIH HHS
ID : P01 CA171983
Pays : United States

Informations de copyright

Copyright © 2019 Kao et al.

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Auteurs

Li-Pin Kao (LP)

Department of Biochemistry and Molecular Biology Brody School of Medicine, East Carolina University, and the East Carolina Diabetes and Obesity Institute, Greenville, NC.

Samy A F Morad (SAF)

Department of Biochemistry and Molecular Biology Brody School of Medicine, East Carolina University, and the East Carolina Diabetes and Obesity Institute, Greenville, NC; Department of Pharmacology, Faculty of Veterinary Medicine, South Valley University, Qena, Egypt.

Traci S Davis (TS)

Department of Biochemistry and Molecular Biology Brody School of Medicine, East Carolina University, and the East Carolina Diabetes and Obesity Institute, Greenville, NC.

Matthew R MacDougall (MR)

Department of Biochemistry and Molecular Biology Brody School of Medicine, East Carolina University, and the East Carolina Diabetes and Obesity Institute, Greenville, NC.

Miki Kassai (M)

Department of Biochemistry and Molecular Biology Brody School of Medicine, East Carolina University, and the East Carolina Diabetes and Obesity Institute, Greenville, NC.

Noha Abdelmageed (N)

Department of Pharmacology, Faculty of Veterinary Medicine, Sohag University, Sohag, Egypt.

Todd E Fox (TE)

Department of Pharmacology, University of Virginia School of Medicine, Charlottesville, VA.

Mark Kester (M)

University of Virginia Cancer Center Charlottesville, VA.

Thomas P Loughran (TP)

University of Virginia Cancer Center Charlottesville, VA; Department of Medicine, Hematology/Oncology, University of Virginia, Charlottesville, VA.

Jose' L Abad (JL)

Instituto de Quimica Avanzada de Cataluña, Barcelona, Spain.

Gemma Fabrias (G)

Instituto de Quimica Avanzada de Cataluña, Barcelona, Spain.

Su-Fern Tan (SF)

Department of Medicine, Hematology/Oncology, University of Virginia, Charlottesville, VA.

David J Feith (DJ)

University of Virginia Cancer Center Charlottesville, VA; Department of Medicine, Hematology/Oncology, University of Virginia, Charlottesville, VA.

David F Claxton (DF)

Penn State Hershey Cancer Institute, Hershey, PA.

Sarah Spiegel (S)

Department of Biochemistry and Molecular Biology and the Massey Cancer Center, Virginia Commonwealth University School of Medicine, Richmond, VA.

Kelsey H Fisher-Wellman (KH)

Department of Physiology, Brody School of Medicine, East Carolina University, and the East Carolina Diabetes and Obesity Institute, Greenville, NC. Electronic address: fisherwellmank17@ecu.edu.

Myles C Cabot (MC)

Department of Biochemistry and Molecular Biology Brody School of Medicine, East Carolina University, and the East Carolina Diabetes and Obesity Institute, Greenville, NC. Electronic address: cabotm@ecu.edu.

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