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Article: Induced pluripotent stem cell-derived hepatocytes reveal TCA cycle disruption and the potential basis for triheptanoin treatment for malate dehydrogenase 2 deficiency.

Mathis, Déborah / Koch, Jasmine / Koller, Sophie / Sauter, Kay / Flück, Christa / Uldry, Anne-Christine / Forny, Patrick / Froese, D Sean / Laemmle, Alexander

Molecular genetics and metabolism reports

2024 Volume 39, Page(s) 101066

Abstract: Mitochondrial malate dehydrogenase 2 (MDH2) is crucial to cellular energy generation through direct participation in the tricarboxylic acid (TCA) cycle and the malate aspartate shuttle (MAS). Inherited MDH2 deficiency is an ultra-rare metabolic disease ... ...

Abstract	Mitochondrial malate dehydrogenase 2 (MDH2) is crucial to cellular energy generation through direct participation in the tricarboxylic acid (TCA) cycle and the malate aspartate shuttle (MAS). Inherited MDH2 deficiency is an ultra-rare metabolic disease caused by bi-allelic pathogenic variants in the Synopsis: This study reveals altered expression of mitochondrial pathways including the tricarboxylic acid cycle and changes in metabolite profiles in malate dehydrogenase 2 deficiency and provides the molecular basis for triheptanoin treatment in this ultra-rare disease.
Language	English
Publishing date	2024-02-23
Publishing country	United States
Document type	Journal Article
ZDB-ID	2821908-9
ISSN	2214-4269
ISSN	2214-4269
DOI	10.1016/j.ymgmr.2024.101066
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Article ; Online: The complex machinery of human cobalamin metabolism.

McCorvie, Thomas J / Ferreira, Douglas / Yue, Wyatt W / Froese, D Sean

Journal of inherited metabolic disease

2023 Volume 46, Issue 3, Page(s) 406–420

Abstract: ... Vitamin ... ...

Abstract	Vitamin B
MeSH term(s)	Humans ; Vitamin B 12/metabolism ; Methylmalonyl-CoA Mutase/metabolism ; Biological Transport ; Molecular Chaperones ; ATP-Binding Cassette Transporters/metabolism ; Oxidoreductases/metabolism
Chemical Substances	Vitamin B 12 (P6YC3EG204) ; Methylmalonyl-CoA Mutase (EC 5.4.99.2) ; Molecular Chaperones ; ABCD4 protein, human ; ATP-Binding Cassette Transporters ; MMACHC protein, human (EC 1.-) ; Oxidoreductases (EC 1.-)
Language	English
Publishing date	2023-02-08
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	438341-2
ISSN	1573-2665 ; 0141-8955
ISSN (online)	1573-2665
ISSN	0141-8955
DOI	10.1002/jimd.12593
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Article ; Online: Dynamic inter-domain transformations mediate the allosteric regulation of human 5, 10-methylenetetrahydrofolate reductase.

Blomgren, Linnea K M / Huber, Melanie / Mackinnon, Sabrina R / Bürer, Céline / Baslé, Arnaud / Yue, Wyatt W / Froese, D Sean / McCorvie, Thomas J

Nature communications

2024 Volume 15, Issue 1, Page(s) 3248

Abstract: 5,10-methylenetetrahydrofolate reductase (MTHFR) commits folate-derived one-carbon units to generate the methyl-donor S-adenosyl-L-methionine (SAM). Eukaryotic MTHFR appends to the well-conserved catalytic domain (CD) a unique regulatory domain (RD) that ...

Abstract	5,10-methylenetetrahydrofolate reductase (MTHFR) commits folate-derived one-carbon units to generate the methyl-donor S-adenosyl-L-methionine (SAM). Eukaryotic MTHFR appends to the well-conserved catalytic domain (CD) a unique regulatory domain (RD) that confers feedback inhibition by SAM. Here we determine the cryo-electron microscopy structures of human MTHFR bound to SAM and its demethylated product S-adenosyl-L-homocysteine (SAH). In the active state, with the RD bound to a single SAH, the CD is flexible and exposes its active site for catalysis. However, in the inhibited state the RD pocket is remodelled, exposing a second SAM-binding site that was previously occluded. Dual-SAM bound MTHFR demonstrates a substantially rearranged inter-domain linker that reorients the CD, inserts a loop into the active site, positions Tyr404 to bind the cofactor FAD, and blocks substrate access. Our data therefore explain the long-distance regulatory mechanism of MTHFR inhibition, underpinned by the transition between dual-SAM and single-SAH binding in response to cellular methylation status.
MeSH term(s)	Humans ; Allosteric Regulation ; Methylenetetrahydrofolate Reductase (NADPH2)/chemistry ; Cryoelectron Microscopy ; S-Adenosylmethionine/metabolism ; Methylation
Chemical Substances	Methylenetetrahydrofolate Reductase (NADPH2) (EC 1.5.1.20) ; S-Adenosylmethionine (7LP2MPO46S)
Language	English
Publishing date	2024-04-15
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-024-47174-y
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Article ; Online: Cellular and computational models reveal environmental and metabolic interactions in MMUT-type methylmalonic aciduria.

Ramon, Charlotte / Traversi, Florian / Bürer, Céline / Froese, D Sean / Stelling, Jörg

Journal of inherited metabolic disease

2022 Volume 46, Issue 3, Page(s) 421–435

Abstract: Methylmalonyl-coenzyme A (CoA) mutase (MMUT)-type methylmalonic aciduria is a rare inherited metabolic disease caused by the loss of function of the MMUT enzyme. Patients develop symptoms resembling those of primary mitochondrial disorders, but the ... ...

Abstract	Methylmalonyl-coenzyme A (CoA) mutase (MMUT)-type methylmalonic aciduria is a rare inherited metabolic disease caused by the loss of function of the MMUT enzyme. Patients develop symptoms resembling those of primary mitochondrial disorders, but the underlying causes of mitochondrial dysfunction remain unclear. Here, we examined environmental and genetic interactions in MMUT deficiency using a combination of computational modeling and cellular models to decipher pathways interacting with MMUT. Immortalized fibroblast (hTERT BJ5ta) MMUT-KO (MUTKO) clones displayed a mild mitochondrial impairment in standard glucose-based medium, but they did not to show increased reliance on respiratory metabolism nor reduced growth or viability. Consistently, our modeling predicted MUTKO specific growth phenotypes only for lower extracellular glutamine concentrations. Indeed, two of three MMUT-deficient BJ5ta cell lines showed a reduced viability in glutamine-free medium. Further, growth on 183 different carbon and nitrogen substrates identified increased NADH (nicotinamide adenine dinucleotide) metabolism of BJ5ta and HEK293 MUTKO cells compared with controls on purine- and glutamine-based substrates. With this knowledge, our modeling predicted 13 reactions interacting with MMUT that potentiate an effect on growth, primarily those of secondary oxidation of propionyl-CoA, oxidative phosphorylation and oxygen diffusion. Of these, we validated 3-hydroxyisobutytyl-CoA hydrolase (HIBCH) in the secondary propionyl-CoA oxidation pathway. Altogether, these results suggest compensation for the loss of MMUT function by increasing anaplerosis through glutamine or by diverting flux away from MMUT through the secondary propionyl-CoA oxidation pathway, which may have therapeutic relevance.
MeSH term(s)	Humans ; HEK293 Cells ; Amino Acid Metabolism, Inborn Errors/diagnosis ; Mitochondrial Diseases/metabolism ; Methylmalonyl-CoA Mutase ; Methylmalonic Acid/metabolism
Chemical Substances	Methylmalonyl-CoA Mutase (EC 5.4.99.2) ; Methylmalonic Acid (8LL8S712J7)
Language	English
Publishing date	2022-11-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	438341-2
ISSN	1573-2665 ; 0141-8955
ISSN (online)	1573-2665
ISSN	0141-8955
DOI	10.1002/jimd.12575
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Article ; Online: Vitamin B

Froese, D Sean / Fowler, Brian / Baumgartner, Matthias R

Journal of inherited metabolic disease

2019 Volume 42, Issue 4, Page(s) 673–685

Abstract: ... Vitamin ... ...

Abstract	Vitamin B
MeSH term(s)	5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/metabolism ; Animals ; Folic Acid/pharmacology ; Folic Acid Deficiency/metabolism ; Humans ; Methylmalonyl-CoA Mutase/metabolism ; Vitamin B 12/pharmacology ; Vitamin B 12 Deficiency/metabolism
Chemical Substances	Folic Acid (935E97BOY8) ; 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase (EC 2.1.1.13) ; Methylmalonyl-CoA Mutase (EC 5.4.99.2) ; Vitamin B 12 (P6YC3EG204)
Language	English
Publishing date	2019-01-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	438341-2
ISSN	1573-2665 ; 0141-8955
ISSN (online)	1573-2665
ISSN	0141-8955
DOI	10.1002/jimd.12009
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Article ; Online: Mitochondrial disease, mitophagy, and cellular distress in methylmalonic acidemia.

Luciani, Alessandro / Denley, Matthew C S / Govers, Larissa P / Sorrentino, Vincenzo / Froese, D Sean

Cellular and molecular life sciences : CMLS

2021 Volume 78, Issue 21-22, Page(s) 6851–6867

Abstract: Mitochondria-the intracellular powerhouse in which nutrients are converted into energy in the form of ATP or heat-are highly dynamic, double-membraned organelles that harness a plethora of cellular functions that sustain energy metabolism and homeostasis. ...

Abstract	Mitochondria-the intracellular powerhouse in which nutrients are converted into energy in the form of ATP or heat-are highly dynamic, double-membraned organelles that harness a plethora of cellular functions that sustain energy metabolism and homeostasis. Exciting new discoveries now indicate that the maintenance of this ever changing and functionally pleiotropic organelle is particularly relevant in terminally differentiated cells that are highly dependent on aerobic metabolism. Given the central role in maintaining metabolic and physiological homeostasis, dysregulation of the mitochondrial network might therefore confer a potentially devastating vulnerability to high-energy requiring cell types, contributing to a broad variety of hereditary and acquired diseases. In this Review, we highlight the biological functions of mitochondria-localized enzymes from the perspective of understanding-and potentially reversing-the pathophysiology of inherited disorders affecting the homeostasis of the mitochondrial network and cellular metabolism. Using methylmalonic acidemia as a paradigm of complex mitochondrial dysfunction, we discuss how mitochondrial directed-signaling circuitries govern the homeostasis and physiology of specialized cell types and how these may be disturbed in disease. This Review also provides a critical analysis of affected tissues, potential molecular mechanisms, and novel cellular and animal models of methylmalonic acidemia which are being used to develop new therapeutic options for this disease. These insights might ultimately lead to new therapeutics, not only for methylmalonic acidemia, but also for other currently intractable mitochondrial diseases, potentially transforming our ability to regulate homeostasis and health.
MeSH term(s)	Amino Acid Metabolism, Inborn Errors/metabolism ; Animals ; Energy Metabolism/physiology ; Homeostasis/physiology ; Humans ; Mitochondria/metabolism ; Mitochondrial Diseases/metabolism ; Mitophagy/physiology ; Organelles/metabolism ; Signal Transduction/physiology
Language	English
Publishing date	2021-09-15
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-021-03934-3
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Article ; Online: HIF1 and DROSHA are involved in MMACHC repression in hypoxia.

Kiessling, Eva / Peters, Florian / Ebner, Lynn J A / Merolla, Luca / Samardzija, Marijana / Baumgartner, Matthias R / Grimm, Christian / Froese, D Sean

Biochimica et biophysica acta. General subjects

2022 Volume 1866, Issue 9, Page(s) 130175

Abstract: The MMACHC gene encodes for an enzyme involved in intracellular vitamin ... ...

Abstract	The MMACHC gene encodes for an enzyme involved in intracellular vitamin B
MeSH term(s)	Animals ; HeLa Cells ; Humans ; Hypoxia ; Hypoxia-Inducible Factor 1/metabolism ; Mice ; MicroRNAs ; Oxidoreductases ; Repressor Proteins/genetics ; Ribonuclease III/genetics ; Trans-Activators ; Transcription Factors ; Vitamin B 12/genetics ; Vitamin B 12/metabolism ; Vitamins
Chemical Substances	Hypoxia-Inducible Factor 1 ; MicroRNAs ; Repressor Proteins ; THAP11 protein, human ; Thap11 protein, mouse ; Trans-Activators ; Transcription Factors ; Vitamins ; ZNF143 protein, human ; MMACHC protein, human (EC 1.-) ; Oxidoreductases (EC 1.-) ; DROSHA protein, human (EC 3.1.26.3) ; Ribonuclease III (EC 3.1.26.3) ; Vitamin B 12 (P6YC3EG204)
Language	English
Publishing date	2022-05-28
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagen.2022.130175
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Article ; Online: Spectrum and characterization of bi-allelic variants in MMAB causing cblB-type methylmalonic aciduria.

Forny, Patrick / Plessl, Tanja / Frei, Caroline / Bürer, Celine / Froese, D Sean / Baumgartner, Matthias R

Human genetics

2021 Volume 141, Issue 7, Page(s) 1253–1267

Abstract: Pathogenic variants in MMAB cause cblB-type methylmalonic aciduria, an autosomal-recessive disorder of propionate metabolism. MMAB encodes ATP:cobalamin adenosyltransferase, using ATP and cob(I)alamin to create 5'-deoxyadenosylcobalamin (AdoCbl), the ... ...

Abstract	Pathogenic variants in MMAB cause cblB-type methylmalonic aciduria, an autosomal-recessive disorder of propionate metabolism. MMAB encodes ATP:cobalamin adenosyltransferase, using ATP and cob(I)alamin to create 5'-deoxyadenosylcobalamin (AdoCbl), the cofactor of methylmalonyl-CoA mutase (MMUT). We identified bi-allelic disease-causing variants in MMAB in 97 individuals with cblB-type methylmalonic aciduria, including 33 different and 16 novel variants. Missense changes accounted for the most frequent pathogenic alleles (p.(Arg186Trp), N = 57; p.(Arg191Trp), N = 19); while c.700C > T (p.(Arg234)) was the most frequently identified truncating variant (N = 14). In fibroblasts from 76 affected individuals, the ratio of propionate incorporation in the presence and absence of hydroxocobalamin (PI ratio) was associated to clinical cobalamin responsiveness and later disease onset. We found p.(Arg234) to be associated with cobalamin responsiveness in vitro, and clinically with later onset; p.(Arg186Trp) and p.(Arg191Trp) showed no clear cobalamin responsiveness and early onset. Mapping these and novel variants onto the MMAB structure revealed their potential to affect ATP and AdoCbl binding. Follow-up biochemical characterization of recombinant MMAB identified its three active sites to be equivalent for ATP binding, determined by fluorescence spectroscopy (K
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Adenosine Triphosphate/chemistry ; Adenosine Triphosphate/metabolism ; Alkyl and Aryl Transferases/metabolism ; Alleles ; Amino Acid Metabolism, Inborn Errors/genetics ; Amino Acid Metabolism, Inborn Errors/pathology ; Humans ; Mutation ; Propionates ; Proto-Oncogene Proteins c-cbl/metabolism ; Vitamin B 12/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Propionates ; Adenosine Triphosphate (8L70Q75FXE) ; CBLB protein, human (EC 2.3.2.27) ; Proto-Oncogene Proteins c-cbl (EC 2.3.2.27) ; Alkyl and Aryl Transferases (EC 2.5.-) ; Vitamin B 12 (P6YC3EG204)
Language	English
Publishing date	2021-11-18
Publishing country	Germany
Document type	Journal Article
ZDB-ID	223009-4
ISSN	1432-1203 ; 0340-6717
ISSN (online)	1432-1203
ISSN	0340-6717
DOI	10.1007/s00439-021-02398-6
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Article: Decrease of disease-related metabolites upon fasting in a hemizygous knock-in mouse model (

Lucienne, Marie / Mathis, Déborah / Perkins, Nathan / Fingerhut, Ralph / Baumgartner, Matthias R / Froese, D Sean

JIMD reports

2020 Volume 58, Issue 1, Page(s) 44–51

Abstract: Methylmalonyl-CoA mutase (MMUT) is part of the propionyl-CoA catabolic pathway, responsible for the breakdown of branched-chain amino acids, odd-chain fatty acids and the side-chain of cholesterol. Patients with deficient activity of MMUT suffer from ... ...

Abstract	Methylmalonyl-CoA mutase (MMUT) is part of the propionyl-CoA catabolic pathway, responsible for the breakdown of branched-chain amino acids, odd-chain fatty acids and the side-chain of cholesterol. Patients with deficient activity of MMUT suffer from isolated methylmalonic aciduria (MMAuria), frequently presenting in the newborn period with failure to thrive and metabolic crisis. Even well managed patients remain at risk for metabolic crises, of which one known trigger is acute illness, which may lead to poor feeding and vomiting, putting the patient in a catabolic state. This situation is believed to result in increased breakdown of propionyl-CoA catabolic pathway precursors, producing massively elevated levels of disease related metabolites, including methylmalonic acid and propionylcarnitine. Here, we used fasting of a hemizygous mouse model (
Language	English
Publishing date	2020-11-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	2672872-2
ISSN	2192-8312 ; 2192-8304
ISSN (online)	2192-8312
ISSN	2192-8304
DOI	10.1002/jmd2.12182
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Article: Mitochondrial disease, mitophagy, and cellular distress in methylmalonic acidemia

Luciani, Alessandro / Denley, Matthew C. S. / Govers, Larissa P. / Sorrentino, Vincenzo / Froese, D. Sean

Cellular and molecular life sciences. 2021 Nov., v. 78, no. 21-22

2021

Abstract: Mitochondria—the intracellular powerhouse in which nutrients are converted into energy in the form of ATP or heat—are highly dynamic, double-membraned organelles that harness a plethora of cellular functions that sustain energy metabolism and homeostasis. ...

Abstract	Mitochondria—the intracellular powerhouse in which nutrients are converted into energy in the form of ATP or heat—are highly dynamic, double-membraned organelles that harness a plethora of cellular functions that sustain energy metabolism and homeostasis. Exciting new discoveries now indicate that the maintenance of this ever changing and functionally pleiotropic organelle is particularly relevant in terminally differentiated cells that are highly dependent on aerobic metabolism. Given the central role in maintaining metabolic and physiological homeostasis, dysregulation of the mitochondrial network might therefore confer a potentially devastating vulnerability to high-energy requiring cell types, contributing to a broad variety of hereditary and acquired diseases. In this Review, we highlight the biological functions of mitochondria-localized enzymes from the perspective of understanding—and potentially reversing—the pathophysiology of inherited disorders affecting the homeostasis of the mitochondrial network and cellular metabolism. Using methylmalonic acidemia as a paradigm of complex mitochondrial dysfunction, we discuss how mitochondrial directed-signaling circuitries govern the homeostasis and physiology of specialized cell types and how these may be disturbed in disease. This Review also provides a critical analysis of affected tissues, potential molecular mechanisms, and novel cellular and animal models of methylmalonic acidemia which are being used to develop new therapeutic options for this disease. These insights might ultimately lead to new therapeutics, not only for methylmalonic acidemia, but also for other currently intractable mitochondrial diseases, potentially transforming our ability to regulate homeostasis and health.
Keywords	animals ; distress ; energy ; energy metabolism ; homeostasis ; mitochondria ; mitophagy ; pathophysiology ; therapeutics
Language	English
Dates of publication	2021-11
Size	p. 6851-6867.
Publishing place	Springer International Publishing
Document type	Article
Note	Review
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-021-03934-3
Database	NAL-Catalogue (AGRICOLA)

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