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Article ; Online: Multiple myeloma metabolism - a treasure trove of therapeutic targets?

Roman-Trufero, Monica / Auner, Holger W / Edwards, Claire M

2022 Volume 13, Page(s) 897862

Abstract: Multiple myeloma is an incurable cancer of plasma cells that is predominantly located in the bone marrow. Multiple myeloma cells are characterized by distinctive biological features that are intricately linked to their core function, the assembly and ... ...

Abstract	Multiple myeloma is an incurable cancer of plasma cells that is predominantly located in the bone marrow. Multiple myeloma cells are characterized by distinctive biological features that are intricately linked to their core function, the assembly and secretion of large amounts of antibodies, and their diverse interactions with the bone marrow microenvironment. Here, we provide a concise and introductory discussion of major metabolic hallmarks of plasma cells and myeloma cells, their roles in myeloma development and progression, and how they could be exploited for therapeutic purposes. We review the role of glucose consumption and catabolism, assess the dependency on glutamine to support key metabolic processes, and consider metabolic adaptations in drug-resistant myeloma cells. Finally, we examine the complex metabolic effects of proteasome inhibitors on myeloma cells and the extracellular matrix, and we explore the complex relationship between myeloma cells and bone marrow adipocytes.
MeSH term(s)	Bone Marrow/metabolism ; Humans ; Multiple Myeloma ; Proteasome Inhibitors/pharmacology ; Proteasome Inhibitors/therapeutic use ; Tumor Microenvironment
Chemical Substances	Proteasome Inhibitors
Language	English
Publishing date	2022-08-22
Publishing country	Switzerland
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2022.897862
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Article ; Online: Label-free nanoscale mapping of intracellular organelle chemistry.

Greaves, George E / Kiryushko, Darya / Auner, Holger W / Porter, Alexandra E / Phillips, Chris C

Communications biology

2023 Volume 6, Issue 1, Page(s) 583

Abstract: The ability to image cell chemistry at the nanoscale is key for understanding cell biology, but many optical microscopies are restricted by the ~(200-250)nm diffraction limit. Electron microscopy and super-resolution fluorescence techniques beat this ... ...

Abstract	The ability to image cell chemistry at the nanoscale is key for understanding cell biology, but many optical microscopies are restricted by the ~(200-250)nm diffraction limit. Electron microscopy and super-resolution fluorescence techniques beat this limit, but rely on staining and specialised labelling to generate image contrast. It is challenging, therefore, to obtain information about the functional chemistry of intracellular components. Here we demonstrate a technique for intracellular label-free chemical mapping with nanoscale (~30 nm) resolution. We use a probe-based optical microscope illuminated with a mid-infrared laser whose wavelengths excite vibrational modes of functional groups occurring within biological molecules. As a demonstration, we chemically map intracellular structures in human multiple myeloma cells and compare the morphologies with electron micrographs of the same cell line. We also demonstrate label-free mapping at wavelengths chosen to target the chemical signatures of proteins and nucleic acids, in a way that can be used to identify biochemical markers in the study of disease and pharmacology.
MeSH term(s)	Humans ; Microscopy/methods ; Light ; Proteins ; Organelles
Chemical Substances	Proteins
Language	English
Publishing date	2023-05-31
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-023-04943-7
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Article ; Online: More convenient proteasome inhibition for improved outcomes.

Auner, Holger W / Yong, Kwee L

The Lancet. Oncology

2018 Volume 19, Issue 7, Page(s) 856–858

MeSH term(s)	Humans ; Multiple Myeloma ; Oligopeptides ; Proteasome Endopeptidase Complex ; Proteasome Inhibitors
Chemical Substances	Oligopeptides ; Proteasome Inhibitors ; carfilzomib (72X6E3J5AR) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2018-06-01
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	2049730-1
ISSN	1474-5488 ; 1470-2045
ISSN (online)	1474-5488
ISSN	1470-2045
DOI	10.1016/S1470-2045(18)30411-X
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Zs.A 5696: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Proteasome inhibition in multiple myeloma: lessons for other cancers.

Saavedra-García, Paula / Martini, Francesca / Auner, Holger W

American journal of physiology. Cell physiology

2019 Volume 318, Issue 3, Page(s) C451–C462

Abstract: Cellular protein homeostasis (proteostasis) depends on the controlled degradation of proteins that are damaged or no longer required by the ubiquitin-proteasome system (UPS). The 26S proteasome is the principal executer of substrate-specific proteolysis ... ...

Abstract	Cellular protein homeostasis (proteostasis) depends on the controlled degradation of proteins that are damaged or no longer required by the ubiquitin-proteasome system (UPS). The 26S proteasome is the principal executer of substrate-specific proteolysis in eukaryotic cells and regulates a myriad of cellular functions. Proteasome inhibitors were initially developed as chemical tools to study proteasomal function but rapidly became widely used anticancer drugs that are now used at all stages of treatment for the bone marrow cancer multiple myeloma (MM). Here, we review the mechanisms of action of proteasome inhibitors that underlie their preferential toxicity to MM cells, focusing on endoplasmic reticulum stress, depletion of amino acids, and effects on glucose and lipid metabolism. We also discuss mechanisms of resistance to proteasome inhibition such as autophagy and metabolic rewiring and what lessons we may learn from the success and failure of proteasome inhibition in MM for treating other cancers with proteostasis-targeting drugs.
MeSH term(s)	Animals ; Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Autophagy/drug effects ; Autophagy/physiology ; Endoplasmic Reticulum Stress/drug effects ; Endoplasmic Reticulum Stress/physiology ; Humans ; Multiple Myeloma/drug therapy ; Multiple Myeloma/metabolism ; Proteasome Inhibitors/pharmacology ; Proteasome Inhibitors/therapeutic use
Chemical Substances	Antineoplastic Agents ; Proteasome Inhibitors
Language	English
Publishing date	2019-12-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	392098-7
ISSN	1522-1563 ; 0363-6143
ISSN (online)	1522-1563
ISSN	0363-6143
DOI	10.1152/ajpcell.00286.2019
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Article: Macrophage migration inhibitory factor blockade reprograms macrophages and disrupts prosurvival signaling in acute myeloid leukemia.

Spertini, Caroline / Bénéchet, Alexandre P / Birch, Flora / Bellotti, Axel / Román-Trufero, Mónica / Arber, Caroline / Auner, Holger W / Mitchell, Robert A / Spertini, Olivier / Smirnova, Tatiana

Cell death discovery

2024 Volume 10, Issue 1, Page(s) 157

Abstract: The malignant microenvironment plays a major role in the development of resistance to therapies and the occurrence of relapses in acute myeloid leukemia (AML). We previously showed that interactions of AML blasts with bone marrow macrophages (MΦ) shift ... ...

Abstract	The malignant microenvironment plays a major role in the development of resistance to therapies and the occurrence of relapses in acute myeloid leukemia (AML). We previously showed that interactions of AML blasts with bone marrow macrophages (MΦ) shift their polarization towards a protumoral (M2-like) phenotype, promoting drug resistance; we demonstrated that inhibiting the colony-stimulating factor-1 receptor (CSF1R) repolarizes MΦ towards an antitumoral (M1-like) phenotype and that other factors may be involved. We investigated here macrophage migration inhibitory factor (MIF) as a target in AML blast survival and protumoral interactions with MΦ. We show that pharmacologically inhibiting MIF secreted by AML blasts results in their apoptosis. However, this effect is abrogated when blasts are co-cultured in close contact with M2-like MΦ. We next demonstrate that pharmacological inhibition of MIF secreted by MΦ, in the presence of granulocyte macrophage-colony stimulating factor (GM-CSF), efficiently reprograms MΦ to an M1-like phenotype that triggers apoptosis of interacting blasts. Furthermore, contact with reprogrammed MΦ relieves blast resistance to venetoclax and midostaurin acquired in contact with CD163
Language	English
Publishing date	2024-03-28
Publishing country	United States
Document type	Journal Article
ISSN	2058-7716
ISSN	2058-7716
DOI	10.1038/s41420-024-01924-5
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Article ; Online: MUKtwelve protocol: a phase II randomised, controlled, open, parallel group, multicentre trial of selinexor, cyclophosphamide and prednisolone (SCP) versus cyclophosphamide and prednisolone (CP) in patients with relapsed or refractory multiple myeloma.

Kendall, Jessica / Hall, Andrew / Roberts, Sadie / Brown, Sarah / Boyd, Kevin / Auner, Holger W / Garg, Mamta / Kaiser, Martin

BMJ open

2022 Volume 12, Issue 10, Page(s) e062504

Abstract: Introduction: Multiple myeloma is a malignancy of plasma cells with around 6000 new cases per year in the UK. Cyclophosphamide plus prednisolone is considered a standard of care for disease and symptom control in the advanced relapsed or refractory ... ...

Abstract	Introduction: Multiple myeloma is a malignancy of plasma cells with around 6000 new cases per year in the UK. Cyclophosphamide plus prednisolone is considered a standard of care for disease and symptom control in the advanced relapsed or refractory myeloma setting within the UK NHS. The selective nuclear export inhibitor, selinexor, has been relatively well tolerated in previous clinical trials and offers promise when used in combination with a wide range of other anti-cancer treatments. Here, we investigate if the addition of selinexor can improve responses to cyclophosphamide plus prednisolone without adding prohibitive toxicity. Methods and analysis: MUKtwelve is a UK-based, randomised, controlled, open, parallel group, multicentre phase II trial designed to evaluate clinical efficacy of selinexor in combination with cyclophosphamide and prednisolone (SCP) in patients with relapsed or refractory multiple myeloma. A calibration arm will receive cyclophosphamide and prednisolone alone (CP). Participants who experience disease progression on the CP arm may, if eligible, receive SCP.The MUK Ethics and dissemination: Ethics approval is obtained. Results will be submitted for publication in a peer-reviewed journal. Trial registration number: ISRCTN15028850.
MeSH term(s)	Humans ; Antineoplastic Combined Chemotherapy Protocols/therapeutic use ; Clinical Trials, Phase II as Topic ; Cyclophosphamide/therapeutic use ; Dexamethasone/therapeutic use ; Multicenter Studies as Topic ; Multiple Myeloma/drug therapy ; Neoplasm Recurrence, Local/drug therapy ; Prednisolone/therapeutic use ; Randomized Controlled Trials as Topic
Chemical Substances	Cyclophosphamide (8N3DW7272P) ; Dexamethasone (7S5I7G3JQL) ; Prednisolone (9PHQ9Y1OLM) ; selinexor (31TZ62FO8F)
Language	English
Publishing date	2022-10-26
Publishing country	England
Document type	Clinical Trial Protocol ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2599832-8
ISSN	2044-6055 ; 2044-6055
ISSN (online)	2044-6055
ISSN	2044-6055
DOI	10.1136/bmjopen-2022-062504
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Article ; Online: Repeatability and test-retest reproducibility of mean apparent diffusion coefficient measurements of focal and diffuse disease in relapsed multiple myeloma at 3T whole body diffusion-weighted MRI (WB-DW-MRI).

ElGendy, Khalil / Barwick, Tara D / Auner, Holger W / Chaidos, Aristeidis / Wallitt, Kathryn / Sergot, Antoni / Rockall, Andrea

The British journal of radiology

2022 Volume 95, Issue 1138, Page(s) 20220418

Abstract: Objective: To assess the test-retest reproducibility and intra/interobserver agreement of apparent diffusion coefficient (ADC) measurements of myeloma lesions using whole body diffusion-weighted MRI (WB-DW-MRI) at 3T MRI.: Methods: Following ethical ... ...

Abstract	Objective: To assess the test-retest reproducibility and intra/interobserver agreement of apparent diffusion coefficient (ADC) measurements of myeloma lesions using whole body diffusion-weighted MRI (WB-DW-MRI) at 3T MRI. Methods: Following ethical approval, 11 consenting patients with relapsed multiple myeloma were prospectively recruited and underwent baseline WB-DW-MRI. For a single bed position, axial DWI was repeated after a short interval to permit test-retest measurements.Mean ADC measurement was performed by two experienced observers. Intra- and interobserver agreement and test-retest reproducibility were assessed, using coefficient of variation (CV) and interclass correlation coefficient (ICC) measures, for diffuse and focal lesions (small ≤10 mm and large >10 mm). Results: 47 sites of disease were outlined (23 focal, 24 diffuse) in different bed positions (pelvis = 22, thorax = 20, head and neck = 5). For all lesions, there was excellent intraobserver agreement with ICC of 0.99 (0.98-0.99) and COV of 5%. For interobserver agreement, ICC was 0.89 (0.8-0.934) and COV was 17%. There was poor interobserver agreement for diffuse disease (ICC = 0.46) and small lesions (ICC = 0.54).For test-retest reproducibility, excellent ICC (0.916) and COV (14.5%) values for mean ADC measurements were observed. ICCs of test-retest were similar between focal lesions (0.83) and diffuse infiltration (0.80), while ICCs were higher in pelvic (0.95) compared to thoracic (0.81) region and in small (0.96) compared to large (0.8) lesions. Conclusion: ADC measurements of focal lesions in multiple myeloma are repeatable and reproducible, while there is more variation in ADC measurements of diffuse disease in patients with multiple myeloma. Advances in knowledge: Mean ADC measurements are repeatable and reproducible in focal lesions in multiple myeloma, while the ADC measurements of diffuse disease in multiple myeloma are more subject to variation. The evidence supports the future potential role of ADC measurements as predictive quantitative biomarker in multiple myeloma.
MeSH term(s)	Biomarkers ; Diffusion Magnetic Resonance Imaging ; Humans ; Magnetic Resonance Imaging ; Multiple Myeloma/diagnostic imaging ; Observer Variation ; Prospective Studies ; Reproducibility of Results
Chemical Substances	Biomarkers
Language	English
Publishing date	2022-07-28
Publishing country	England
Document type	Journal Article
ZDB-ID	2982-8
ISSN	1748-880X ; 0007-1285
ISSN (online)	1748-880X
ISSN	0007-1285
DOI	10.1259/bjr.20220418
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Article ; Online: High patient satisfaction and increased physical activity following a remote multidisciplinary team multiple myeloma clinic.

Lecat, Catherine S Y / Fisher, Abigail / Atta, Maria / Camilleri, Marquita / McCourt, Orla / Land, Joanne / Worthington, Sarah / Hart, Alyse / Daniel, Angela / Uddin, Inayah / Roche, Charlotte / Auner, Holger W / Yong, Kwee

Supportive care in cancer : official journal of the Multinational Association of Supportive Care in Cancer

2023 Volume 31, Issue 2, Page(s) 127

Abstract: Purpose: Patients with multiple myeloma suffer from disease-related complications such as bone destruction, toxicities from repeated therapies and age-related co-morbidities. With improved treatment options, patients are living longer and have specific ... ...

Abstract	Purpose: Patients with multiple myeloma suffer from disease-related complications such as bone destruction, toxicities from repeated therapies and age-related co-morbidities. With improved treatment options, patients are living longer and have specific survivorship needs such as low exercise levels that need to be addressed. In this study, we designed, implemented and evaluated a multidisciplinary team (MDT) myeloma clinic that provided participants with tailored exercise and lifestyle advice. Methods: The Promoting Individualised Self-Management and Survivorship (PrISMS) clinic was set up in two UK myeloma centres. This remote MDT clinic comprised of a doctor, a nurse specialist and a physiotherapist. Patients were required to complete blood tests and a questionnaire about their symptoms and concerns before each consultation. Patient-reported outcome measures were captured using validated questionnaires. Patient feedback was collected using a specially designed survey and structured telephone interviews. Results: Sixty-one patients were enrolled in the pilot clinic with 210 consultations held during the study period. Nine patients had disease progression and were referred safely back to face-to-face clinics. There was a significant improvement in patients' exercise score (p = 0.02) after PrISMS clinic. Patient satisfaction was high, with 83% feeling more confident in self-managing myeloma after PrISMS clinic. Conclusion: PrISMS clinic is safe and feasible, with high patient compliant and acceptability. It empowers patients to self-manage their condition and encourages physical activity, which is associated with improved quality of life and fatigue level. Future randomised controlled trials will help to confirm its benefits on patient clinical outcomes and cost-effectiveness.
MeSH term(s)	Humans ; Patient Satisfaction ; Multiple Myeloma/therapy ; Quality of Life ; Exercise ; Patient Care Team
Language	English
Publishing date	2023-01-21
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1134446-5
ISSN	1433-7339 ; 0941-4355
ISSN (online)	1433-7339
ISSN	0941-4355
DOI	10.1007/s00520-023-07587-9
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Article ; Online: Recent advances and future directions in targeting the secretory apparatus in multiple myeloma.

Auner, Holger W / Cenci, Simone

British journal of haematology

2014 Volume 168, Issue 1, Page(s) 14–25

Abstract: Multiple myeloma is a genetically heterogeneous tumour of transformed plasma cells, terminally differentiated effectors of the B cell lineage specialized in producing large amounts of immunoglobulins. The uniquely well-developed secretory apparatus that ... ...

Abstract	Multiple myeloma is a genetically heterogeneous tumour of transformed plasma cells, terminally differentiated effectors of the B cell lineage specialized in producing large amounts of immunoglobulins. The uniquely well-developed secretory apparatus that equips normal and transformed plasma cells with the capacity for high-level protein secretion constitutes a distinctive therapeutic target. In this review we discuss how fundamental cellular processes, such as the unfolded protein response (UPR), endoplasmic reticulum (ER)-associated degradation and autophagy, maintain intracellular protein homeostasis (proteostasis) and regulate plasma cell ontogeny and malignancy. We summarize our current understanding of the cellular effects of proteasome inhibitors and the molecular bases of resistance to them. Furthermore, we discuss how improvements in our understanding of the secretory apparatus and of the complex interactions between intracellular protein synthesis and degradation pathways can disclose novel drug targets for multiple myeloma, defining a paradigm of general interest for cancer biology and disorders of altered proteostasis.
MeSH term(s)	Animals ; Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Autophagy ; Drug Resistance, Neoplasm ; Endoplasmic Reticulum-Associated Degradation ; Homeostasis/drug effects ; Humans ; Molecular Targeted Therapy ; Multiple Myeloma/drug therapy ; Plasma Cells/drug effects ; Plasma Cells/metabolism ; Proteasome Inhibitors/pharmacology ; Proteasome Inhibitors/therapeutic use ; Proteolysis ; Secretory Pathway/drug effects ; Unfolded Protein Response
Chemical Substances	Antineoplastic Agents ; Proteasome Inhibitors
Language	English
Publishing date	2014-10-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80077-6
ISSN	1365-2141 ; 0007-1048
ISSN (online)	1365-2141
ISSN	0007-1048
DOI	10.1111/bjh.13172
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Article ; Online: GLI1, a novel target of the ER stress regulator p97/VCP, promotes ATF6f-mediated activation of XBP1.

Almada, Luciana L / Barroso, Kim / Sen, Sandhya / Toruner, Murat / Sigafoos, Ashley N / Raja Arul, Glancis L / Pease, David R / Vera, Renzo E / Olson, Rachel L O / Auner, Holger W / Pedeux, Rémy / Iovanna, Juan L / Chevet, Eric / Fernandez-Zapico, Martin E

Biochimica et biophysica acta. Gene regulatory mechanisms

2023 Volume 1866, Issue 2, Page(s) 194924

Abstract: Upon accumulation of improperly folded proteins in the Endoplasmic Reticulum (ER), the Unfolded Protein Response (UPR) is triggered to restore ER homeostasis. The induction of stress genes is a sine qua non condition for effective adaptive UPR. Although ... ...

Abstract	Upon accumulation of improperly folded proteins in the Endoplasmic Reticulum (ER), the Unfolded Protein Response (UPR) is triggered to restore ER homeostasis. The induction of stress genes is a sine qua non condition for effective adaptive UPR. Although this requirement has been extensively described, the mechanisms underlying this process remain in part uncharacterized. Here, we show that p97/VCP, an AAA+ ATPase known to contribute to ER stress-induced gene expression, regulates the transcription factor GLI1, a primary effector of Hedgehog (Hh) signaling. Under basal (non-ER stress) conditions, GLI1 is repressed by a p97/VCP-HDAC1 complex while upon ER stress GLI1 is induced through a mechanism requiring both USF2 binding and increase histone acetylation at its promoter. Interestingly, the induction of GLI1 was independent of ligand-regulated Hh signaling. Further analysis showed that GLI1 cooperates with ATF6f to induce promoter activity and expression of XBP1, a key transcription factor driving UPR. Overall, our work demonstrates a novel role for GLI1 in the regulation of ER stress gene expression and defines the interplay between p97/VCP, HDAC1 and USF2 as essential players in this process.
MeSH term(s)	Zinc Finger Protein GLI1/genetics ; Zinc Finger Protein GLI1/metabolism ; Valosin Containing Protein/genetics ; Valosin Containing Protein/metabolism ; Hedgehog Proteins/genetics ; Hedgehog Proteins/metabolism ; Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	Zinc Finger Protein GLI1 ; Valosin Containing Protein (EC 3.6.4.6) ; Hedgehog Proteins ; Adenosine Triphosphatases (EC 3.6.1.-) ; Transcription Factors
Language	English
Publishing date	2023-02-25
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2918786-2
ISSN	1876-4320 ; 1874-9399
ISSN (online)	1876-4320
ISSN	1874-9399
DOI	10.1016/j.bbagrm.2023.194924
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