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Article ; Online: Characterization of an

De Vitto, Humberto / Belfon, Kafi K J / Sharma, Nandini / Toay, Sarah / Abendroth, Jan / Dranow, David M / Lukacs, Christine M / Choi, Ryan / Udell, Hannah S / Willis, Sydney / Barrera, George / Beyer, Olive / Li, Teng Da / Hicks, Katherine A / Torelli, Andrew T / French, Jarrod B

Biochemistry

2024

Abstract: Thiamin and its phosphate derivatives are ubiquitous molecules involved as essential cofactors in many cellular processes. ... ...

Abstract	Thiamin and its phosphate derivatives are ubiquitous molecules involved as essential cofactors in many cellular processes. The
Language	English
Publishing date	2024-02-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.3c00640
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Article ; Online: Long-term efficacy and safety of mRNA therapy in two murine models of methylmalonic acidemia.

An, Ding / Frassetto, Andrea / Jacquinet, Eric / Eybye, Marianne / Milano, Joseph / DeAntonis, Christine / Nguyen, Vi / Laureano, Rodrigo / Milton, Jaclyn / Sabnis, Staci / Lukacs, Christine M / Guey, Lin T

EBioMedicine

2019 Volume 45, Page(s) 519–528

Abstract: Background: Isolated methylmalonic acidemia/aciduria (MMA) is an ultra-rare, serious, inherited metabolic disorder with significant morbidity and mortality. Exogenously delivered mRNA encoding human methylmalonyl-CoA mutase (hMUT), the enzyme most ... ...

Abstract	Background: Isolated methylmalonic acidemia/aciduria (MMA) is an ultra-rare, serious, inherited metabolic disorder with significant morbidity and mortality. Exogenously delivered mRNA encoding human methylmalonyl-CoA mutase (hMUT), the enzyme most frequently mutated in MMA, is a potential therapy to produce functional MUT enzyme in liver. Methods: Two 12-week repeat-dose studies were conducted to evaluate the efficacy and safety of intravenously-administered hMUT mRNA encapsulated in lipid nanoparticles in two murine models of MMA. Findings: In MMA hypomorphic mice, hMUT mRNA treatment resulted in dose-dependent and reproducible biomarker responses after each dose. Enzymatically-active MUT protein was produced in liver in a dose-dependent manner. hMUT mRNA was well-tolerated with no adverse effects, as indicated by the lack of clinical observations, minimal changes in clinical chemistry parameters, and histopathology examination across all tissues. In severe MMA mice, hMUT mRNA led to substantially improved survival and growth and ameliorated biochemical abnormalities, all of which are cardinal clinical manifestations in severely affected patients. Interpretation: These data demonstrate durable functional benefit of hMUT mRNA and support development of this new class of therapy for a devastating, pediatric disorder. FUND: This work was funded by Moderna, Inc.
MeSH term(s)	Amino Acid Metabolism, Inborn Errors/genetics ; Amino Acid Metabolism, Inborn Errors/pathology ; Amino Acid Metabolism, Inborn Errors/therapy ; Animals ; Child ; Disease Models, Animal ; Humans ; Lipids/genetics ; Liver/drug effects ; Liver/metabolism ; Liver/pathology ; Methylmalonyl-CoA Mutase/genetics ; Methylmalonyl-CoA Mutase/pharmacology ; Mice ; RNA, Messenger/genetics ; RNA, Messenger/pharmacology
Chemical Substances	Lipids ; RNA, Messenger ; Methylmalonyl-CoA Mutase (EC 5.4.99.2)
Language	English
Publishing date	2019-07-12
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2851331-9
ISSN	2352-3964
ISSN (online)	2352-3964
DOI	10.1016/j.ebiom.2019.07.003
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Zs.A 7090: Show issues

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Article ; Online: Optimization of ether and aniline based inhibitors of lactate dehydrogenase.

Bioorganic & medicinal chemistry letters

2021 Volume 41, Page(s) 127974

Abstract: Lactate dehydrogenase (LDH) is a critical enzyme in the glycolytic metabolism pathway that is used by many tumor cells. Inhibitors of LDH may be expected to inhibit the metabolic processes in cancer cells and thus selectively delay or inhibit growth in ... ...

Abstract	Lactate dehydrogenase (LDH) is a critical enzyme in the glycolytic metabolism pathway that is used by many tumor cells. Inhibitors of LDH may be expected to inhibit the metabolic processes in cancer cells and thus selectively delay or inhibit growth in transformed versus normal cells. We have previously disclosed a pyrazole-based series of potent LDH inhibitors with long residence times on the enzyme. Here, we report the elaboration of a new subseries of LDH inhibitors based on those leads. These new compounds potently inhibit both LDHA and LDHB enzymes, and inhibit lactate production in cancer cell lines.
MeSH term(s)	Aniline Compounds/chemistry ; Aniline Compounds/pharmacology ; Antineoplastic Agents/chemistry ; Antineoplastic Agents/pharmacology ; Cell Line, Tumor ; Drug Design ; Ethers/chemistry ; Ethers/pharmacology ; Humans ; L-Lactate Dehydrogenase/antagonists & inhibitors ; L-Lactate Dehydrogenase/chemistry ; L-Lactate Dehydrogenase/metabolism
Chemical Substances	Aniline Compounds ; Antineoplastic Agents ; Ethers ; L-Lactate Dehydrogenase (EC 1.1.1.27)
Language	English
Publishing date	2021-03-24
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1063195-1
ISSN	1464-3405 ; 0960-894X
ISSN (online)	1464-3405
ISSN	0960-894X
DOI	10.1016/j.bmcl.2021.127974
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Article ; Online: Dual mRNA therapy restores metabolic function in long-term studies in mice with propionic acidemia.

Nature communications

2020 Volume 11, Issue 1, Page(s) 5339

Abstract: Propionic acidemia/aciduria (PA) is an ultra-rare, life-threatening, inherited metabolic disorder caused by deficiency of the mitochondrial enzyme, propionyl-CoA carboxylase (PCC) composed of six alpha (PCCA) and six beta (PCCB) subunits. We herein ... ...

Abstract	Propionic acidemia/aciduria (PA) is an ultra-rare, life-threatening, inherited metabolic disorder caused by deficiency of the mitochondrial enzyme, propionyl-CoA carboxylase (PCC) composed of six alpha (PCCA) and six beta (PCCB) subunits. We herein report an enzyme replacement approach to treat PA using a combination of two messenger RNAs (mRNAs) (dual mRNAs) encoding both human PCCA (hPCCA) and PCCB (hPCCB) encapsulated in biodegradable lipid nanoparticles (LNPs) to produce functional PCC enzyme in liver. In patient fibroblasts, dual mRNAs encoded proteins localize in mitochondria and produce higher PCC enzyme activity vs. single (PCCA or PCCB) mRNA alone. In a hypomorphic murine model of PA, dual mRNAs normalize ammonia similarly to carglumic acid, a drug approved in Europe for the treatment of hyperammonemia due to PA. Dual mRNAs additionally restore functional PCC enzyme in liver and thus reduce primary disease-associated toxins in a dose-dependent manner in long-term 3- and 6-month repeat-dose studies in PA mice. Dual mRNAs are well-tolerated in these studies with no adverse findings. These studies demonstrate the potential of mRNA technology to chronically administer multiple mRNAs to produce large complex enzymes, with applicability to other genetic disorders.
MeSH term(s)	Animals ; Disease Models, Animal ; Enzyme Replacement Therapy/methods ; Glutamates/therapeutic use ; Humans ; Kinetics ; Lipids/chemistry ; Liver/enzymology ; Methylmalonyl-CoA Decarboxylase/chemistry ; Methylmalonyl-CoA Decarboxylase/genetics ; Methylmalonyl-CoA Decarboxylase/metabolism ; Mice ; Mice, Knockout ; Mice, Transgenic ; Mitochondria/enzymology ; Nanoparticles/administration & dosage ; Nanoparticles/chemistry ; Propionic Acidemia/genetics ; Propionic Acidemia/metabolism ; Propionic Acidemia/therapy ; Protein Subunits/chemistry ; Protein Subunits/genetics ; RNA, Messenger/administration & dosage ; RNA, Messenger/genetics ; RNA, Messenger/therapeutic use
Chemical Substances	Glutamates ; Lipids ; Protein Subunits ; RNA, Messenger ; carglumic acid (5L0HB4V1EW) ; Methylmalonyl-CoA Decarboxylase (EC 7.2.4.3)
Language	English
Publishing date	2020-10-21
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/s41467-020-19156-3
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Article ; Online: Systemic mRNA Therapy for the Treatment of Fabry Disease: Preclinical Studies in Wild-Type Mice, Fabry Mouse Model, and Wild-Type Non-human Primates.

American journal of human genetics

2019 Volume 104, Issue 4, Page(s) 625–637

Abstract: Fabry disease is an X-linked lysosomal storage disease caused by loss of alpha galactosidase A (α-Gal A) activity and is characterized by progressive accumulation of globotriaosylceramide and its analogs in all cells and tissues. Although enzyme ... ...

Abstract	Fabry disease is an X-linked lysosomal storage disease caused by loss of alpha galactosidase A (α-Gal A) activity and is characterized by progressive accumulation of globotriaosylceramide and its analogs in all cells and tissues. Although enzyme replacement therapy (ERT) is considered standard of care, the long-term effects of ERT on renal and cardiac manifestations remain uncertain and thus novel therapies are desirable. We herein report preclinical studies evaluating systemic messenger RNA (mRNA) encoding human α-Gal A in wild-type (WT) mice, α-Gal A-deficient mice, and WT non-human primates (NHPs). The pharmacokinetics and distribution of h-α-Gal A mRNA encoded protein in WT mice demonstrated prolonged half-lives of α-Gal A in tissues and plasma. Single intravenous administration of h-α-Gal A mRNA to Gla-deficient mice showed dose-dependent protein activity and substrate reduction. Moreover, long duration (up to 6 weeks) of substrate reductions in tissues and plasma were observed after a single injection. Furthermore, repeat i.v. administration of h-α-Gal A mRNA showed a sustained pharmacodynamic response and efficacy in Fabry mice model. Lastly, multiple administrations to non-human primates confirmed safety and translatability. Taken together, these studies across species demonstrate preclinical proof-of-concept of systemic mRNA therapy for the treatment of Fabry disease and this approach may be useful for other lysosomal storage disorders.
MeSH term(s)	Animals ; Disease Models, Animal ; Endocytosis ; Enzyme Replacement Therapy ; Fabry Disease/genetics ; Fabry Disease/therapy ; Genetic Therapy ; Humans ; Lipids/chemistry ; Lysosomes/metabolism ; Macaca fascicularis ; Male ; Mice ; Mice, Knockout ; RNA, Messenger/pharmacokinetics ; RNA, Messenger/therapeutic use ; Tissue Distribution ; Trihexosylceramides/metabolism ; alpha-Galactosidase/genetics
Chemical Substances	Lipids ; RNA, Messenger ; Trihexosylceramides ; globotriaosylceramide (71965-57-6) ; alpha-Galactosidase (EC 3.2.1.22)
Language	English
Publishing date	2019-03-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	219384-x
ISSN	1537-6605 ; 0002-9297
ISSN (online)	1537-6605
ISSN	0002-9297
DOI	10.1016/j.ajhg.2019.02.003
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Zs.A 107: Show issues

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Article ; Online: Structures of aspartate aminotransferases from Trypanosoma brucei, Leishmania major and Giardia lamblia.

Abendroth, Jan / Choi, Ryan / Wall, Abigail / Clifton, Matthew C / Lukacs, Christine M / Staker, Bart L / Van Voorhis, Wesley / Myler, Peter / Lorimer, Don D / Edwards, Thomas E

Acta crystallographica. Section F, Structural biology communications

2015 Volume 71, Issue Pt 5, Page(s) 566–571

Abstract: The structures of three aspartate aminotransferases (AATs) from eukaryotic pathogens were solved within the Seattle Structural Genomics Center for Infectious Disease (SSGCID). Both the open and closed conformations of AAT were observed. Pyridoxal ... ...

Abstract	The structures of three aspartate aminotransferases (AATs) from eukaryotic pathogens were solved within the Seattle Structural Genomics Center for Infectious Disease (SSGCID). Both the open and closed conformations of AAT were observed. Pyridoxal phosphate was bound to the active site via a Schiff base to a conserved lysine. An active-site mutant showed that Trypanosoma brucei AAT still binds pyridoxal phosphate even in the absence of the tethering lysine. The structures highlight the challenges for the structure-based design of inhibitors targeting the active site, while showing options for inhibitor design targeting the N-terminal arm.
MeSH term(s)	Aspartate Aminotransferases/chemistry ; Crystallization ; Giardia lamblia/chemistry ; Giardia lamblia/enzymology ; Leishmania major/chemistry ; Leishmania major/enzymology ; Protein Structure, Secondary ; Trypanosoma brucei brucei/chemistry ; Trypanosoma brucei brucei/enzymology
Chemical Substances	Aspartate Aminotransferases (EC 2.6.1.1)
Language	English
Publishing date	2015-04-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	2053-230X
ISSN (online)	2053-230X
DOI	10.1107/S2053230X15001831
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Article ; Online: Systemic Messenger RNA Therapy as a Treatment for Methylmalonic Acidemia.

An, Ding / Schneller, Jessica L / Frassetto, Andrea / Liang, Shi / Zhu, Xuling / Park, Ji-Sun / Theisen, Matt / Hong, Sue-Jean / Zhou, Jenny / Rajendran, Raj / Levy, Becca / Howell, Rebecca / Besin, Gilles / Presnyak, Vladimir / Sabnis, Staci / Murphy-Benenato, Kerry E / Kumarasinghe, E Sathyajith / Salerno, Timothy / Mihai, Cosmin /

Lukacs, Christine M / Chandler, Randy J / Guey, Lin T / Venditti, Charles P / Martini, Paolo G V

Cell reports

2018 Volume 24, Issue 9, Page(s) 2520

Language	English
Publishing date	2018-09-11
Publishing country	United States
Document type	Published Erratum
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2018.08.049
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Article ; Online: Systemic Messenger RNA Therapy as a Treatment for Methylmalonic Acidemia.

Lukacs, Christine M / Chandler, Randy J / Guey, Lin T / Venditti, Charles P / Martini, Paolo G V

Cell reports

2018 Volume 21, Issue 12, Page(s) 3548–3558

Abstract: Isolated methylmalonic acidemia/aciduria (MMA) is a devastating metabolic disorder with poor outcomes despite current medical treatments. Like other mitochondrial enzymopathies, enzyme replacement therapy (ERT) is not available, and although promising, ... ...

Abstract	Isolated methylmalonic acidemia/aciduria (MMA) is a devastating metabolic disorder with poor outcomes despite current medical treatments. Like other mitochondrial enzymopathies, enzyme replacement therapy (ERT) is not available, and although promising, AAV gene therapy can be limited by pre-existing immunity and has been associated with genotoxicity in mice. To develop a new class of therapy for MMA, we generated a pseudoU-modified codon-optimized mRNA encoding human methylmalonyl-CoA mutase (hMUT), the enzyme most frequently mutated in MMA, and encapsulated it into biodegradable lipid nanoparticles (LNPs). Intravenous (i.v.) administration of hMUT mRNA in two different mouse models of MMA resulted in a 75%-85% reduction in plasma methylmalonic acid and was associated with increased hMUT protein expression and activity in liver. Repeat dosing of hMUT mRNA reduced circulating metabolites and dramatically improved survival and weight gain. Additionally, repeat i.v. dosing did not increase markers of liver toxicity or inflammation in heterozygote MMA mice.
MeSH term(s)	Administration, Intravenous ; Amino Acid Metabolism, Inborn Errors/therapy ; Animals ; Female ; Genetic Therapy/methods ; Humans ; Lipids/chemistry ; Liver/metabolism ; Male ; Methylmalonyl-CoA Mutase/genetics ; Methylmalonyl-CoA Mutase/metabolism ; Mice ; Nanoparticles/administration & dosage ; Nanoparticles/chemistry ; RNA, Messenger/genetics ; RNA, Messenger/metabolism
Chemical Substances	Lipids ; RNA, Messenger ; Methylmalonyl-CoA Mutase (EC 5.4.99.2)
Language	English
Publishing date	2018-02-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2017.11.081
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Article ; Online: Systemic messenger RNA as an etiological treatment for acute intermittent porphyria.

Nature medicine

2018 Volume 24, Issue 12, Page(s) 1899–1909

Abstract: Acute intermittent porphyria (AIP) results from haploinsufficiency of porphobilinogen deaminase (PBGD), the third enzyme in the heme biosynthesis pathway. Patients with AIP have neurovisceral attacks associated with increased hepatic heme demand. ... ...

Abstract	Acute intermittent porphyria (AIP) results from haploinsufficiency of porphobilinogen deaminase (PBGD), the third enzyme in the heme biosynthesis pathway. Patients with AIP have neurovisceral attacks associated with increased hepatic heme demand. Phenobarbital-challenged mice with AIP recapitulate the biochemical and clinical characteristics of patients with AIP, including hepatic overproduction of the potentially neurotoxic porphyrin precursors. Here we show that intravenous administration of human PBGD (hPBGD) mRNA (encoded by the gene HMBS) encapsulated in lipid nanoparticles induces dose-dependent protein expression in mouse hepatocytes, rapidly normalizing urine porphyrin precursor excretion in ongoing attacks. Furthermore, hPBGD mRNA protected against mitochondrial dysfunction, hypertension, pain and motor impairment. Repeat dosing in AIP mice showed sustained efficacy and therapeutic improvement without evidence of hepatotoxicity. Finally, multiple administrations to nonhuman primates confirmed safety and translatability. These data provide proof-of-concept for systemic hPBGD mRNA as a potential therapy for AIP.
MeSH term(s)	Animals ; Disease Models, Animal ; Female ; Genetic Therapy ; Haploinsufficiency/genetics ; Heme/genetics ; Heme/metabolism ; Hepatocytes/drug effects ; Humans ; Hydroxymethylbilane Synthase/genetics ; Hydroxymethylbilane Synthase/therapeutic use ; Liver/drug effects ; Liver/metabolism ; Male ; Porphyria, Acute Intermittent/genetics ; Porphyria, Acute Intermittent/pathology ; Porphyria, Acute Intermittent/therapy ; RNA, Messenger/administration & dosage ; RNA, Messenger/genetics
Chemical Substances	RNA, Messenger ; Heme (42VZT0U6YR) ; Hydroxymethylbilane Synthase (EC 2.5.1.61)
Language	English
Publishing date	2018-10-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1220066-9
ISSN	1546-170X ; 1078-8956
ISSN (online)	1546-170X
ISSN	1078-8956
DOI	10.1038/s41591-018-0199-z
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Article: Identification of an Adamantyl Azaquinolone JNK Selective Inhibitor.

Haynes, Nancy-Ellen / Scott, Nathan R / Chen, Li C / Janson, Cheryl A / Li, Jia Kui / Lukacs, Christine M / Railkar, Aruna / Tozzo, Effie / Whittard, Toni / Brown, Nicholas F / Cheung, Adrian Wai-Hing

ACS medicinal chemistry letters

2012 Volume 3, Issue 9, Page(s) 764–768

Abstract: 3-[4-((1S,2S,3R,5S,7S)-5-Hydroxyadamantan-2-ylcarbamoyl)benzyl]-4-oxo-1-phenyl-1,4-dihydro-[1,8]naphthyridine-2-carboxylic acid methyl ester (4) was identified as a novel, druglike and selective quinolone pan JNK inhibitor. In this communication, some of ...

Abstract	3-[4-((1S,2S,3R,5S,7S)-5-Hydroxyadamantan-2-ylcarbamoyl)benzyl]-4-oxo-1-phenyl-1,4-dihydro-[1,8]naphthyridine-2-carboxylic acid methyl ester (4) was identified as a novel, druglike and selective quinolone pan JNK inhibitor. In this communication, some of the structure-activity relationship of the azaquinolone analogues leading to 4 is discussed. The focus is on how changes at the amide functionality affected the biochemical potency, cellular potency, metabolic properties, and solubility of this class of JNK inhibitors. Optimization of these properties led to the identification of the adamantyl analogue, 4. 4 achieved proof of mechanism in both rat and mouse TNF-α challenge models.
Language	English
Publishing date	2012-08-08
Publishing country	United States
Document type	Journal Article
ISSN	1948-5875
ISSN	1948-5875
DOI	10.1021/ml300175c
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