Pyrroline-5-Carboxylate Reductase 1: a novel target for sensitizing multiple myeloma cells to bortezomib by inhibition of PRAS40-mediated protein synthesis.


Journal

Journal of experimental & clinical cancer research : CR
ISSN: 1756-9966
Titre abrégé: J Exp Clin Cancer Res
Pays: England
ID NLM: 8308647

Informations de publication

Date de publication:
01 Feb 2022
Historique:
received: 30 09 2021
accepted: 07 01 2022
entrez: 2 2 2022
pubmed: 3 2 2022
medline: 24 3 2022
Statut: epublish

Résumé

Multiple myeloma (MM) remains an incurable cancer despite advances in therapy. Therefore, the search for new targets is still essential to uncover potential treatment strategies. Metabolic changes, induced by the hypoxic bone marrow, contribute to both MM cell survival and drug resistance. Pyrroline-5-carboxylate reductase 1 and 2 (PYCR1 and PYCR2) are two mitochondrial enzymes that facilitate the last step in the glutamine-to-proline conversion. Overexpression of PYCR1 is involved in progression of several cancers, however, its' role in hematological cancers is unknown. In this study, we investigated whether PYCR affects MM viability, proliferation and response to bortezomib. Correlation of PYCR1/2 with overall survival was investigated in the MMRF CoMMpass trial (653 patients). OPM-2 and RPMI-8226 MM cell lines were used to perform in vitro experiments. RPMI-8226 cells were supplemented with We found that PYCR1 and PYCR2 mRNA expression correlated with an inferior overall survival. MM cells from relapsed/refractory patients express significantly higher levels of PYCR1 mRNA. In line with the strong expression of PYCR1, we performed a tracer study in RPMI-8226 cells, which revealed an increased conversion of This study identifies PYCR1 as a novel target in bortezomib-based combination therapies for MM.

Sections du résumé

BACKGROUND BACKGROUND
Multiple myeloma (MM) remains an incurable cancer despite advances in therapy. Therefore, the search for new targets is still essential to uncover potential treatment strategies. Metabolic changes, induced by the hypoxic bone marrow, contribute to both MM cell survival and drug resistance. Pyrroline-5-carboxylate reductase 1 and 2 (PYCR1 and PYCR2) are two mitochondrial enzymes that facilitate the last step in the glutamine-to-proline conversion. Overexpression of PYCR1 is involved in progression of several cancers, however, its' role in hematological cancers is unknown. In this study, we investigated whether PYCR affects MM viability, proliferation and response to bortezomib.
METHODS METHODS
Correlation of PYCR1/2 with overall survival was investigated in the MMRF CoMMpass trial (653 patients). OPM-2 and RPMI-8226 MM cell lines were used to perform in vitro experiments. RPMI-8226 cells were supplemented with
RESULTS RESULTS
We found that PYCR1 and PYCR2 mRNA expression correlated with an inferior overall survival. MM cells from relapsed/refractory patients express significantly higher levels of PYCR1 mRNA. In line with the strong expression of PYCR1, we performed a tracer study in RPMI-8226 cells, which revealed an increased conversion of
CONCLUSIONS CONCLUSIONS
This study identifies PYCR1 as a novel target in bortezomib-based combination therapies for MM.

Identifiants

pubmed: 35105345
doi: 10.1186/s13046-022-02250-3
pii: 10.1186/s13046-022-02250-3
pmc: PMC8805317
doi:

Substances chimiques

Antineoplastic Agents 0
Protein Synthesis Inhibitors 0
Bortezomib 69G8BD63PP
Pyrroline Carboxylate Reductases EC 1.5.1.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

45

Subventions

Organisme : Fonds Wetenschappelijk Onderzoek
ID : FWOAL806
Organisme : Vrije Universiteit Brussel
ID : SRP48

Informations de copyright

© 2022. The Author(s).

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Auteurs

Inge Oudaert (I)

Department of Hematology and Immunology-Myeloma Center Brussels, Vrije Universiteit Brussel, Laarbeeklaan 103, 1090, Jette, Brussels, Belgium.

Hatice Satilmis (H)

Department of Hematology and Immunology-Myeloma Center Brussels, Vrije Universiteit Brussel, Laarbeeklaan 103, 1090, Jette, Brussels, Belgium.

Philip Vlummens (P)

Department of Hematology and Immunology-Myeloma Center Brussels, Vrije Universiteit Brussel, Laarbeeklaan 103, 1090, Jette, Brussels, Belgium.
Department of Clinical Hematology, Ghent University Hospital, Gent, Belgium.

Wouter De Brouwer (W)

Department of Hematology, Vrije Universiteit Brussel, Universitair Ziekenhuis Brussel, Laarbeeklaan 101, 1090, Jette, Brussels, Belgium.

Anke Maes (A)

Department of Hematology and Immunology-Myeloma Center Brussels, Vrije Universiteit Brussel, Laarbeeklaan 103, 1090, Jette, Brussels, Belgium.

Dirk Hose (D)

Department of Hematology and Immunology-Myeloma Center Brussels, Vrije Universiteit Brussel, Laarbeeklaan 103, 1090, Jette, Brussels, Belgium.

Elke De Bruyne (E)

Department of Hematology and Immunology-Myeloma Center Brussels, Vrije Universiteit Brussel, Laarbeeklaan 103, 1090, Jette, Brussels, Belgium.

Bart Ghesquière (B)

Metabolomics Expertise Center, VIB Center for Cancer Biology (VIB-CCB) - Department of Oncology, KU Leuven, Leuven, Belgium.

Karin Vanderkerken (K)

Department of Hematology and Immunology-Myeloma Center Brussels, Vrije Universiteit Brussel, Laarbeeklaan 103, 1090, Jette, Brussels, Belgium.

Kim De Veirman (K)

Department of Hematology and Immunology-Myeloma Center Brussels, Vrije Universiteit Brussel, Laarbeeklaan 103, 1090, Jette, Brussels, Belgium.

Eline Menu (E)

Department of Hematology and Immunology-Myeloma Center Brussels, Vrije Universiteit Brussel, Laarbeeklaan 103, 1090, Jette, Brussels, Belgium. Eline.Menu@vub.be.

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