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Article ; Online: Attacking cancer's Achilles heel: antagonism of anti-apoptotic BCL-2 family members.

Opferman, Joseph T

2015 Volume 283, Issue 14, Page(s) 2661–2675

Abstract: Malignant cells routinely violate cellular checkpoints that should initiate cell death in normal cells by triggering pro-apoptotic members of the BCL-2 family of proteins. To escape such death inducing signals, cancer cells often select for upregulation ... ...

Abstract	Malignant cells routinely violate cellular checkpoints that should initiate cell death in normal cells by triggering pro-apoptotic members of the BCL-2 family of proteins. To escape such death inducing signals, cancer cells often select for upregulation of anti-apoptotic BCL-2 family members including BCL-2, BCL-XL , BFL-1, BCL-W and MCL-1. These family members prevent death by sequestering pro-apoptotic molecules. To counter this resistance mechanism, small molecule inhibitors of anti-apoptotic BCL-2 family members have been under development. These molecules have shown promise in pre-clinical and clinical testing to overcome apoptotic resistance, prompting cancer cells to undergo apoptosis. Alternatively, other strategies have taken advantage of the normal regulatory machinery controlling anti-apoptotic molecules and have used inhibitors of signaling pathways to down-modulate the expression of anti-apoptotic molecules, thus tilting the balance in cancer cells to cell death. This review explores recent developments and strategies aimed at antagonizing anti-apoptotic BCL-2 family member action to promote the induction of cell death in cancer therapy.
MeSH term(s)	Aniline Compounds/pharmacology ; Animals ; Antineoplastic Agents/pharmacology ; Apoptosis/drug effects ; Apoptosis/physiology ; Bridged Bicyclo Compounds, Heterocyclic/pharmacology ; Drug Design ; Humans ; Inhibitor of Apoptosis Proteins/antagonists & inhibitors ; Models, Biological ; Myeloid Cell Leukemia Sequence 1 Protein/antagonists & inhibitors ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Neoplasms/pathology ; Proto-Oncogene Proteins c-bcl-2/antagonists & inhibitors ; Signal Transduction ; Sulfonamides/pharmacology ; bcl-2-Associated X Protein/agonists
Chemical Substances	Aniline Compounds ; Antineoplastic Agents ; Bridged Bicyclo Compounds, Heterocyclic ; Inhibitor of Apoptosis Proteins ; MCL1 protein, human ; Myeloid Cell Leukemia Sequence 1 Protein ; Proto-Oncogene Proteins c-bcl-2 ; Sulfonamides ; bcl-2-Associated X Protein ; venetoclax (N54AIC43PW) ; navitoclax (XKJ5VVK2WD)
Language	English
Publishing date	2015-09-15
Publishing country	England
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.13472
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Correction: Mcl-1 confers protection of Her2-positive breast cancer cells to hypoxia: therapeutic implications.

Bashari, Muhammad Hasan / Fan, Fengjuan / Vallet, Sonia / Sattler, Martin / Arn, Melissa / Luckner-Minden, Claudia / Schulze-Bergkamen, Henning / Zörnig, Inka / Marme, Frederik / Schneeweiss, Andreas / Cardone, Michael H / Opferman, Joseph T / Jäger, Dirk / Podar, Klaus

Breast cancer research : BCR

2024 Volume 26, Issue 1, Page(s) 58

Language	English
Publishing date	2024-04-02
Publishing country	England
Document type	Published Erratum
ZDB-ID	2015059-3
ISSN	1465-542X ; 1465-5411
ISSN (online)	1465-542X
ISSN	1465-5411
DOI	10.1186/s13058-024-01811-y
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Zs.A 5494: Show issues

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Article ; Online: Genetic ablation of

Rockfield, Stephanie M / Turnis, Meghan E / Rodriguez-Enriquez, Ricardo / Bathina, Madhavi / Ng, Seng Kah / Kurtz, Nathan / Becerra Mora, Nathalie / Pelletier, Stephane / Robinson, Camenzind G / Vogel, Peter / Opferman, Joseph T

Life science alliance

2024 Volume 7, Issue 6

Abstract: The mitochondrial contact site and cristae organizing system (MICOS) is important for crista junction formation and for maintaining inner mitochondrial membrane architecture. A key component of the MICOS complex is MIC60, which has been well studied in ... ...

Abstract	The mitochondrial contact site and cristae organizing system (MICOS) is important for crista junction formation and for maintaining inner mitochondrial membrane architecture. A key component of the MICOS complex is MIC60, which has been well studied in yeast and cell culture models. However, only one recent study has demonstrated the embryonic lethality of losing
MeSH term(s)	Animals ; Mice ; Mitochondria Associated Membranes ; Mitochondrial Proteins/metabolism ; Mitochondrial Membranes/metabolism ; Mitochondria/metabolism ; Saccharomyces cerevisiae/metabolism
Chemical Substances	Mitochondrial Proteins
Language	English
Publishing date	2024-03-11
Publishing country	United States
Document type	Journal Article
ISSN	2575-1077
ISSN (online)	2575-1077
DOI	10.26508/lsa.202302329
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Article ; Online: Anti-apoptotic MCL-1 promotes long-chain fatty acid oxidation through interaction with ACSL1.

Wright, Tristen / Turnis, Meghan E / Grace, Christy R / Li, Xiao / Brakefield, Lauren A / Wang, Yong-Dong / Xu, Haiyan / Kaminska, Ewa / Climer, Leslie K / Mukiza, Tresor O / Chang, Chi-Lun / Moldoveanu, Tudor / Opferman, Joseph T

Molecular cell

2024 Volume 84, Issue 7, Page(s) 1338–1353.e8

Abstract: MCL-1 is essential for promoting the survival of many normal cell lineages and confers survival and chemoresistance in cancer. Beyond apoptosis regulation, MCL-1 has been linked to modulating mitochondrial metabolism, but the mechanism(s) by which it ... ...

Abstract	MCL-1 is essential for promoting the survival of many normal cell lineages and confers survival and chemoresistance in cancer. Beyond apoptosis regulation, MCL-1 has been linked to modulating mitochondrial metabolism, but the mechanism(s) by which it does so are unclear. Here, we show in tissues and cells that MCL-1 supports essential steps in long-chain (but not short-chain) fatty acid β-oxidation (FAO) through its binding to specific long-chain acyl-coenzyme A (CoA) synthetases of the ACSL family. ACSL1 binds to the BH3-binding hydrophobic groove of MCL-1 through a non-conventional BH3-domain. Perturbation of this interaction, via genetic loss of Mcl1, mutagenesis, or use of selective BH3-mimetic MCL-1 inhibitors, represses long-chain FAO in cells and in mouse livers and hearts. Our findings reveal how anti-apoptotic MCL-1 facilitates mitochondrial metabolism and indicate that disruption of this function may be associated with unanticipated cardiac toxicities of MCL-1 inhibitors in clinical trials.
MeSH term(s)	Animals ; Mice ; Apoptosis ; Coenzyme A Ligases/genetics ; Fatty Acids/metabolism ; Mitochondria/metabolism ; Myeloid Cell Leukemia Sequence 1 Protein/genetics ; Myeloid Cell Leukemia Sequence 1 Protein/metabolism ; Oxidation-Reduction
Chemical Substances	ACSL1 protein, mouse (EC 6.2.1.-) ; Coenzyme A Ligases (EC 6.2.1.-) ; Fatty Acids ; Myeloid Cell Leukemia Sequence 1 Protein
Language	English
Publishing date	2024-03-18
Publishing country	United States
Document type	Journal Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2024.02.035
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Zs.A 5055: Show issues

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Article ; Online: Anti-apoptotic BCL-2 family members in development.

Opferman, Joseph T / Kothari, Anisha

Cell death and differentiation

2017 Volume 25, Issue 1, Page(s) 37–45

Abstract: Almost 30 years ago it was first appreciated that anti-apoptotic B-cell lymphoma-2 (BCL-2) prevents the induction of apoptosis not only in malignant cells, but also in normal cellular lineages. This critical observation has rapidly evolved from merely ... ...

Abstract	Almost 30 years ago it was first appreciated that anti-apoptotic B-cell lymphoma-2 (BCL-2) prevents the induction of apoptosis not only in malignant cells, but also in normal cellular lineages. This critical observation has rapidly evolved from merely identifying new BCL-2 family members to understanding how their biochemical interactions trigger the cell death process, and, more recently, to pharmacological inhibition of anti-apoptotic BCL-2 function in disease. Indeed, the proper regulation of apoptosis is important in many aspects of life including development, homeostasis, and disease biology. To better understand these processes, scientists have used many tools to assess the contribution of individual anti-apoptotic BCL-2 family members. This review will focus on the prominent roles for BCL-2 and other pro-survival family members in promoting the development of mammals during early embryogenesis, neurogenesis, and hematopoiesis.
MeSH term(s)	Animals ; Apoptosis ; Apoptosis Regulatory Proteins/physiology ; Embryonic Development ; Hematopoiesis ; Mice ; Nervous System/embryology ; Proto-Oncogene Proteins c-bcl-2/physiology
Chemical Substances	Apoptosis Regulatory Proteins ; Proto-Oncogene Proteins c-bcl-2
Language	English
Publishing date	2017-11-03
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1225672-9
ISSN	1476-5403 ; 1350-9047
ISSN (online)	1476-5403
ISSN	1350-9047
DOI	10.1038/cdd.2017.170
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Zs.A 4230: 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)
Zs.MG 80: Show issues

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Article: Attacking cancer's Achilles heel: antagonism of antiâapoptotic BCLâ2 family members

Opferman, Joseph T

FEBS journal. 2016 July, v. 283, no. 14

2016

Abstract: Malignant cells routinely violate cellular checkpoints that should initiate cell death in normal cells by triggering proâapoptotic members of the BCLâ2 family of proteins. To escape such death inducing signals, cancer cells often select for ... ...

Abstract	Malignant cells routinely violate cellular checkpoints that should initiate cell death in normal cells by triggering proâapoptotic members of the BCLâ2 family of proteins. To escape such death inducing signals, cancer cells often select for upregulation of antiâapoptotic BCLâ2 family members including BCLâ2, BCLâXL, BFLâ1, BCLâW and MCLâ1. These family members prevent death by sequestering proâapoptotic molecules. To counter this resistance mechanism, small molecule inhibitors of antiâapoptotic BCLâ2 family members have been under development. These molecules have shown promise in preâclinical and clinical testing to overcome apoptotic resistance, prompting cancer cells to undergo apoptosis. Alternatively, other strategies have taken advantage of the normal regulatory machinery controlling antiâapoptotic molecules and have used inhibitors of signaling pathways to downâmodulate the expression of antiâapoptotic molecules, thus tilting the balance in cancer cells to cell death. This review explores recent developments and strategies aimed at antagonizing antiâapoptotic BCLâ2 family member action to promote the induction of cell death in cancer therapy.
Keywords	apoptosis ; death ; neoplasm cells ; neoplasms ; proteins ; signal transduction ; therapeutics
Language	English
Dates of publication	2016-07
Size	p. 2661-2675.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	REVIEW
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.13472
Database	NAL-Catalogue (AGRICOLA)

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Article: The Role of Mcl-1 in Embryonic Neural Precursor Cell Apoptosis.

Flemmer, Robert T / Connolly, Sarah P / Geizer, Brittany A / Opferman, Joseph T / Vanderluit, Jacqueline L

Frontiers in cell and developmental biology

2021 Volume 9, Page(s) 659531

Abstract: Myeloid cell leukemia-1 (Mcl-1), an anti-apoptotic Bcl-2 protein, regulates neural precursor cell (NPC) survival in both the developing and adult mammalian nervous system. It is unclear when during the neurogenic period Mcl-1 becomes necessary for NPC ... ...

Abstract	Myeloid cell leukemia-1 (Mcl-1), an anti-apoptotic Bcl-2 protein, regulates neural precursor cell (NPC) survival in both the developing and adult mammalian nervous system. It is unclear when during the neurogenic period Mcl-1 becomes necessary for NPC survival and whether Bax is the sole pro-apoptotic target of Mcl-1. To address these questions, we used the nervous system-specific Nestin-Cre Mcl-1 conditional knockout mouse line (Mcl-1 CKO) to assess the anti-apoptotic role of Mcl-1 in developmental neurogenesis. Loss of Mcl-1 resulted in a wave of apoptosis beginning in the brainstem and cervical spinal cord at embryonic day 9.5 (E9.5) and in the forebrain at E10.5. Apoptosis was first observed ventrally in each region and spread dorsally over time. Within the spinal cord, apoptosis also spread in a rostral to caudal direction following the path of differentiation. Breeding the Mcl-1 CKO mouse with the Bax null mouse rescued the majority of NPC from apoptosis except in the dorsomedial brainstem and ventral thoracic spinal cord where only 50% were rescued. This demonstrates that Mcl-1 promotes NPC survival primarily by inhibiting the activation of Bax, but that Bax is not the sole pro-apoptotic target of Mcl-1 during embryonic neurogenesis. Interestingly, although co-deletion of Bax rescued the majority of NPC apoptosis, it resulted in embryonic lethality at E13, whereas conditional deletion of both Mcl-1 and Bax rescued embryonic lethality. In summary, this study demonstrates the widespread dependency on Mcl-1 during nervous system development.
Language	English
Publishing date	2021-04-20
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2021.659531
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Article: Mitochondrial proteostasis mediated by CRL5

Campos, Yvan / Rodriguez-Enriquez, Ricardo / Palacios, Gustavo / Van de Vlekkert, Diantha / Qiu, Xiaohui / Weesner, Jayce / Gomero, Elida / Demmers, Jeroen / Bertorini, Tulio / Opferman, Joseph T / Grosveld, Gerard C / d'Azzo, Alessandra

bioRxiv : the preprint server for biology

2023

Abstract: High energy-demanding tissues, such as skeletal muscle, require mitochondrial proteostasis to function properly. Two quality-control mechanisms, the ubiquitin proteasome system (UPS) and the release of mitochondria-derived vesicles, safeguard ... ...

Abstract	High energy-demanding tissues, such as skeletal muscle, require mitochondrial proteostasis to function properly. Two quality-control mechanisms, the ubiquitin proteasome system (UPS) and the release of mitochondria-derived vesicles, safeguard mitochondrial proteostasis. However, whether these processes interact is unknown. Here we show that the E3 ligase CRL5
Language	English
Publishing date	2023-07-11
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.07.11.548601
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Targeting MCL-1 triggers DNA damage and an anti-proliferative response independent from apoptosis induction.

Adhikary, Utsarga / Paulo, Joao A / Godes, Marina / Roychoudhury, Shrabasti / Prew, Michelle S / Ben-Nun, Yael / Yu, Ellen W / Budhraja, Amit / Opferman, Joseph T / Chowdhury, Dipanjan / Gygi, Steven P / Walensky, Loren D

Cell reports

2023 Volume 42, Issue 10, Page(s) 113176

Abstract: MCL-1 is a high-priority target due to its dominant role in the pathogenesis and chemoresistance of cancer, yet clinical trials of MCL-1 inhibitors are revealing toxic side effects. MCL-1 biology is complex, extending beyond apoptotic regulation and ... ...

Abstract	MCL-1 is a high-priority target due to its dominant role in the pathogenesis and chemoresistance of cancer, yet clinical trials of MCL-1 inhibitors are revealing toxic side effects. MCL-1 biology is complex, extending beyond apoptotic regulation and confounded by its multiple isoforms, its domains of unresolved structure and function, and challenges in distinguishing noncanonical activities from the apoptotic response. We find that, in the presence or absence of an intact mitochondrial apoptotic pathway, genetic deletion or pharmacologic targeting of MCL-1 induces DNA damage and retards cell proliferation. Indeed, the cancer cell susceptibility profile of MCL-1 inhibitors better matches that of anti-proliferative than pro-apoptotic drugs, expanding their potential therapeutic applications, including synergistic combinations, but heightening therapeutic window concerns. Proteomic profiling provides a resource for mechanistic dissection and reveals the minichromosome maintenance DNA helicase as an interacting nuclear protein complex that links MCL-1 to the regulation of DNA integrity and cell-cycle progression.
MeSH term(s)	Proto-Oncogene Proteins c-bcl-2/metabolism ; Myeloid Cell Leukemia Sequence 1 Protein/metabolism ; Apoptosis ; Proteomics ; Antineoplastic Agents/pharmacology ; DNA Damage ; Cell Line, Tumor
Chemical Substances	Proto-Oncogene Proteins c-bcl-2 ; Myeloid Cell Leukemia Sequence 1 Protein ; Antineoplastic Agents
Language	English
Publishing date	2023-09-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2023.113176
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Combination of MCL-1 and BCL-2 inhibitors is a promising approach for a host-directed therapy for tuberculosis.

Arnett, Eusondia / Pahari, Susanta / Leopold Wager, Chrissy M / Hernandez, Elizabeth / Bonifacio, Jordan R / Lumbreras, Miranda / Renshaw, Charles / Montoya, Maria J / Opferman, Joseph T / Schlesinger, Larry S

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie

2023 Volume 168, Page(s) 115738

Abstract: Tuberculosis (TB) accounts for 1.6 million deaths annually and over 25% of deaths due to antimicrobial resistance. Mycobacterium tuberculosis (M.tb) drives MCL-1 expression (family member of anti-apoptotic BCL-2 proteins) to limit apoptosis and grow ... ...

Abstract	Tuberculosis (TB) accounts for 1.6 million deaths annually and over 25% of deaths due to antimicrobial resistance. Mycobacterium tuberculosis (M.tb) drives MCL-1 expression (family member of anti-apoptotic BCL-2 proteins) to limit apoptosis and grow intracellularly in human macrophages. The feasibility of re-purposing specific MCL-1 and BCL-2 inhibitors to limit M.tb growth, using inhibitors that are in clinical trials and FDA-approved for cancer treatment has not be tested previously. We show that specifically inhibiting MCL-1 and BCL-2 induces apoptosis of M.tb-infected macrophages, and markedly reduces M.tb growth in human and murine macrophages, and in a pre-clinical model of human granulomas. MCL-1 and BCL-2 inhibitors limit growth of drug resistant and susceptible M.tb in macrophages and act in additive fashion with the antibiotics isoniazid and rifampicin. This exciting work uncovers targeting the intrinsic apoptosis pathway as a promising approach for TB host-directed therapy. Since safety and activity studies are underway in cancer clinics for MCL-1 and BCL-2 inhibitors, we expect that re-purposing them for TB treatment should translate more readily and rapidly to the clinic. Thus, the work supports further development of this host-directed therapy approach to augment current TB treatment.
MeSH term(s)	Animals ; Humans ; Mice ; Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Antitubercular Agents/pharmacology ; Antitubercular Agents/therapeutic use ; Antitubercular Agents/metabolism ; Macrophages/drug effects ; Mycobacterium tuberculosis/drug effects ; Myeloid Cell Leukemia Sequence 1 Protein/antagonists & inhibitors ; Myeloid Cell Leukemia Sequence 1 Protein/metabolism ; Proto-Oncogene Proteins c-bcl-2/antagonists & inhibitors ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Tuberculosis/drug therapy ; Tuberculosis/microbiology ; Drug Repositioning
Chemical Substances	Antineoplastic Agents ; Antitubercular Agents ; Myeloid Cell Leukemia Sequence 1 Protein ; Proto-Oncogene Proteins c-bcl-2
Language	English
Publishing date	2023-10-19
Publishing country	France
Document type	Journal Article
ZDB-ID	392415-4
ISSN	1950-6007 ; 0753-3322 ; 0300-0893
ISSN (online)	1950-6007
ISSN	0753-3322 ; 0300-0893
DOI	10.1016/j.biopha.2023.115738
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