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Article ; Online: How to fix a broken protein: restoring function to mutant human cystathionine β-synthase.

Kruger, Warren D

2021 Volume 141, Issue 7, Page(s) 1299–1308

Abstract: Inborn errors of metabolism (IEM) comprise a large class of recessive genetic diseases involving disorders of cellular metabolism that tend to be caused by missense mutations in which a single incorrect amino acid is substituted in the polypeptide chain. ...

Abstract	Inborn errors of metabolism (IEM) comprise a large class of recessive genetic diseases involving disorders of cellular metabolism that tend to be caused by missense mutations in which a single incorrect amino acid is substituted in the polypeptide chain. Cystathionine beta-synthase (CBS) deficiency is an example of an IEM that causes large elevations of blood total homocysteine levels, resulting in phenotypes in several tissues. Current treatment strategies involve dietary restriction and vitamin therapy, but these are only partially effective and do not work in all patients. Over 85% of the described mutations in CBS-deficient patients are missense mutations in which the mutant protein fails to fold into an active conformation. The ability of CBS to achieve an active conformation is affected by a variety of intracellular protein networks including the chaperone system and the ubiquitin/proteasome system, collectively referred to as the proteostasis network. Proteostasis modulators are drugs that perturb various aspects of these networks. In this article, we will review the evidence that modulation of the intracellular protein folding environment can be used as a potential therapeutic strategy to treat CBS deficiency and discuss the pros and cons of such a strategy.
MeSH term(s)	Cystathionine beta-Synthase/genetics ; Cystathionine beta-Synthase/metabolism ; Homocystinuria/drug therapy ; Homocystinuria/therapy ; Humans ; Molecular Chaperones/genetics ; Mutation ; Phenotype
Chemical Substances	Molecular Chaperones ; Cystathionine beta-Synthase (EC 4.2.1.22)
Language	English
Publishing date	2021-10-12
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	223009-4
ISSN	1432-1203 ; 0340-6717
ISSN (online)	1432-1203
ISSN	0340-6717
DOI	10.1007/s00439-021-02386-w
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Article ; Online: Examination of two different proteasome inhibitors in reactivating mutant human cystathionine β-synthase in mice.

Gupta, Sapna / Lee, Hyung-Ok / Wang, Liqun / Kruger, Warren D

PloS one

2023 Volume 18, Issue 6, Page(s) e0286550

Abstract: Classic homocystinuria is an inborn error of metabolism caused mainly by missense mutations leading to misfolded and/or unstable human cystathionine β-synthase (CBS) protein, causing the accumulation of excess total homocysteine (tHcy) in tissues. ... ...

Abstract	Classic homocystinuria is an inborn error of metabolism caused mainly by missense mutations leading to misfolded and/or unstable human cystathionine β-synthase (CBS) protein, causing the accumulation of excess total homocysteine (tHcy) in tissues. Previously, it has been shown that certain missense containing human CBS proteins can be functionally rescued in mouse models of CBS deficiency by treatment with proteasome inhibitors. The rescue by proteasome inhibitors is thought to work both by inhibiting the degradation of misfolded CBS protein and by inducing the levels of heat-shock chaperone proteins in the liver. Here we examine the effectiveness of two FDA approved protease inhibitors, carfilzomib and bortezomib, on various transgenic mouse models of human CBS deficiency. Our results show that although both drugs are effective in inducing the liver chaperone proteins Hsp70 and Hsp27, and are effective in inhibiting proteasome function, bortezomib was somewhat more robust in restoring the mutant CBS function. Moreover, there was no significant correlation between proteasome inhibition and CBS activity, suggesting that some of bortezomib's effects are via other mechanisms. We also test the use of low-doses of bortezomib and carfilzomib on various mouse models for extended periods of time and find that while low-doses are less toxic, they are also less effective at restoring CBS function. Overall, these results show that while restoration of mutant CBS function is possible with proteasome inhibitors, the exact mechanism is complicated and it will likely be too toxic for long-term patient treatment.
MeSH term(s)	Humans ; Mice ; Animals ; Cystathionine beta-Synthase/genetics ; Cystathionine beta-Synthase/metabolism ; Proteasome Inhibitors/pharmacology ; Proteasome Inhibitors/therapeutic use ; Homocystinuria/drug therapy ; Homocystinuria/genetics ; Homocystinuria/metabolism ; Bortezomib/pharmacology ; Bortezomib/therapeutic use ; Proteasome Endopeptidase Complex ; Mice, Transgenic
Chemical Substances	Cystathionine beta-Synthase (EC 4.2.1.22) ; Proteasome Inhibitors ; Bortezomib (69G8BD63PP) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2023-06-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0286550
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Article ; Online: Cystathionine β-synthase deficiency: Of mice and men.

Kruger, Warren D

Molecular genetics and metabolism

2017 Volume 121, Issue 3, Page(s) 199–205

Abstract: Cystathionine β-synthase (CBS) deficiency (Online Mendelian Inheritance in Man [OMIM] 236,200) is an autosomal recessive disorder that is caused by mutations in the CBS gene. It is the most common inborn error of sulfur metabolism and is the cause of ... ...

Abstract	Cystathionine β-synthase (CBS) deficiency (Online Mendelian Inheritance in Man [OMIM] 236,200) is an autosomal recessive disorder that is caused by mutations in the CBS gene. It is the most common inborn error of sulfur metabolism and is the cause of classical homocystinuria, a condition characterized by very high levels of plasma total homocysteine and methionine. Although recognized as an inborn error of metabolism over 60years ago, these is still much we do not understand related to how this specific metabolic defect gives rise to its distinct phenotypes. To try and answer these questions, several groups have developed mouse models on CBS deficiency. In this article, we will review various mouse models of CBS deficiency and discuss how these mouse models compare to human CBS deficient patients.
MeSH term(s)	Animals ; Animals, Newborn ; Cystathionine beta-Synthase/deficiency ; Cystathionine beta-Synthase/genetics ; Disease Models, Animal ; Genotype ; Homocysteine/blood ; Homocystinuria/genetics ; Homocystinuria/physiopathology ; Humans ; Male ; Metabolism, Inborn Errors/genetics ; Metabolism, Inborn Errors/metabolism ; Methionine/metabolism ; Mice ; Mutation ; Phenotype ; Pyridoxine/administration & dosage
Chemical Substances	Homocysteine (0LVT1QZ0BA) ; Methionine (AE28F7PNPL) ; Cystathionine beta-Synthase (EC 4.2.1.22) ; Pyridoxine (KV2JZ1BI6Z)
Language	English
Publishing date	2017
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	1418518-0
ISSN	1096-7206 ; 1096-7192
ISSN (online)	1096-7206
ISSN	1096-7192
DOI	10.1016/j.ymgme.2017.05.011
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Article ; Online: Recent therapeutic approaches to cystathionine beta-synthase-deficient homocystinuria.

Majtan, Tomas / Kožich, Viktor / Kruger, Warren D

British journal of pharmacology

2022 Volume 180, Issue 3, Page(s) 264–278

Abstract: Cystathionine beta-synthase (CBS)-deficient homocystinuria (HCU) is the most common inborn error of sulfur amino acid metabolism. The pyridoxine non-responsive form of the disease manifests itself by massively increasing plasma and tissue concentrations ... ...

Abstract	Cystathionine beta-synthase (CBS)-deficient homocystinuria (HCU) is the most common inborn error of sulfur amino acid metabolism. The pyridoxine non-responsive form of the disease manifests itself by massively increasing plasma and tissue concentrations of homocysteine, a toxic intermediate of methionine metabolism that is thought to be the major cause of clinical complications including skeletal deformities, connective tissue defects, thromboembolism and cognitive impairment. The current standard of care involves significant dietary interventions that, despite being effective, often adversely affect quality of life of HCU patients, leading to poor adherence to therapy and inadequate biochemical control with clinical complications. In recent years, the unmet need for better therapeutic options has resulted in development of novel enzyme and gene therapies and exploration of pharmacological approaches to rescue CBS folding defects caused by missense pathogenic mutations. Here, we review scientific evidence and current state of affairs in development of recent approaches to treat HCU.
MeSH term(s)	Humans ; Homocystinuria/drug therapy ; Homocystinuria/genetics ; Homocystinuria/metabolism ; Cystathionine beta-Synthase/genetics ; Cystathionine beta-Synthase/metabolism ; Quality of Life ; Thromboembolism ; Mutation, Missense
Chemical Substances	Cystathionine beta-Synthase (EC 4.2.1.22)
Language	English
Publishing date	2022-12-08
Publishing country	England
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80081-8
ISSN	1476-5381 ; 0007-1188
ISSN (online)	1476-5381
ISSN	0007-1188
DOI	10.1111/bph.15991
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Article: NEDD9 sustains hexokinase expression to promote glycolysis.

Deneka, Alexander Y / Nikonova, Anna S / Lee, Hyung-Ok / Kruger, Warren D / Golemis, Erica A

Oncogenesis

2022 Volume 11, Issue 1, Page(s) 15

Abstract: Elevated rates of glycolysis in cancer cells support tumor growth, in a process that typically depends on oncogene-induced increases in the expression and/or activity of enzymes in the glycolytic pathway. The NEDD9 scaffolding protein is upregulated in ... ...

Abstract	Elevated rates of glycolysis in cancer cells support tumor growth, in a process that typically depends on oncogene-induced increases in the expression and/or activity of enzymes in the glycolytic pathway. The NEDD9 scaffolding protein is upregulated in many advanced tumors, with increased NEDD9 promoting the activity of SRC and other effectors that promote invasion and metastasis. We here define a new role for NEDD9 in support of glycolysis. NEDD9 knockdown significantly impaired glycolysis in multiple lung cancer cell lines This was accompanied by post-transcriptional downregulation of steady-state levels of hexokinases (HK1 and HK2), which catalyze early steps in the glycolytic cascade, key rate limiting enzyme phosphofructokinase (PFK1), and downstream glyceraldehyde phosphate dehydrogenase (GAPDH). In mice, protein levels of HK1, HK2, PFK1, and GAPDH were depressed in Kras
Language	English
Publishing date	2022-04-11
Publishing country	United States
Document type	Journal Article
ZDB-ID	2674437-5
ISSN	2157-9024
ISSN	2157-9024
DOI	10.1038/s41389-022-00391-w
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Article ; Online: The effect of dietary modulation of sulfur amino acids on cystathionine β synthase-deficient mice.

Kruger, Warren D / Gupta, Sapna

Annals of the New York Academy of Sciences

2016 Volume 1363, Page(s) 80–90

Abstract: Cystathionine β synthase (CBS) is a key enzyme in the methionine and cysteine metabolic pathway, acting as a metabolic gatekeeper to regulate the flow of fixed sulfur from methionine to cysteine. Mutations in the CBS gene cause clinical CBS deficiency, a ...

Abstract	Cystathionine β synthase (CBS) is a key enzyme in the methionine and cysteine metabolic pathway, acting as a metabolic gatekeeper to regulate the flow of fixed sulfur from methionine to cysteine. Mutations in the CBS gene cause clinical CBS deficiency, a disease characterized by elevated plasma total homocysteine (tHcy) and methionine and decreased plasma cysteine. The treatment goal for CBS-deficient patients is to normalize the metabolic values of these three metabolites using a combination of vitamin therapy and dietary manipulation. To better understand the effectiveness of nutritional treatment strategies, we have performed a series of long-term dietary manipulation studies using our previously developed Tg-I278T Cbs(-/-) mouse model of CBS deficiency and sibling Tg-I278T Cbs(+/-) controls. Tg-I278T Cbs(-/-) mice have undetectable levels of CBS activity, extremely elevated plasma tHcy, modestly elevated plasma methionine, and low plasma cysteine. They exhibit several easily assayable phenotypes, including osteoporosis, loss of fat mass, reduced life span, and facial alopecia. The diets used in these studies differed in the amounts of sulfur amino acids or sulfur amino acid precursors. In this review, we will discuss our findings and their relevance to CBS deficiency and the concept of gene-diet interaction.
MeSH term(s)	Acetylcysteine/administration & dosage ; Amino Acids, Sulfur/metabolism ; Animals ; Betaine/administration & dosage ; Cystathionine beta-Synthase/deficiency ; Cystathionine beta-Synthase/genetics ; Diet ; Dietary Supplements ; Disease Models, Animal ; Genotype ; Homocystinuria/diet therapy ; Homocystinuria/genetics ; Homocystinuria/metabolism ; Humans ; Metabolic Networks and Pathways ; Methionine/administration & dosage ; Methionine/metabolism ; Mice ; Mice, Knockout ; Mutation ; Phenotype
Chemical Substances	Amino Acids, Sulfur ; Betaine (3SCV180C9W) ; Methionine (AE28F7PNPL) ; Cystathionine beta-Synthase (EC 4.2.1.22) ; Acetylcysteine (WYQ7N0BPYC)
Language	English
Publishing date	2016-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	211003-9
ISSN	1749-6632 ; 0077-8923
ISSN (online)	1749-6632
ISSN	0077-8923
DOI	10.1111/nyas.12967
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Article ; Online: Extracellular 5'-methylthioadenosine inhibits intracellular symmetric dimethylarginine protein methylation of FUSE-binding proteins.

Tang, Baiqing / Lee, Hyung-Ok / Gupta, Sapna / Wang, Liqun / Kurimchak, Alison M / Duncan, James S / Kruger, Warren D

The Journal of biological chemistry

2022 Volume 298, Issue 9, Page(s) 102367

Abstract: Methylthioadenosine phosphorylase (MTAP) is a key enzyme in the methionine salvage pathway that converts the polyamine synthesis byproduct 5'-deoxy-5'-methylthioadenosine (MTA) into methionine. Inactivation of MTAP, often by homozygous deletion, is found ...

Abstract	Methylthioadenosine phosphorylase (MTAP) is a key enzyme in the methionine salvage pathway that converts the polyamine synthesis byproduct 5'-deoxy-5'-methylthioadenosine (MTA) into methionine. Inactivation of MTAP, often by homozygous deletion, is found in both solid and hematologic malignancies and is one of the most frequently observed genetic alterations in human cancer. Previous work established that MTAP-deleted cells accumulate MTA and contain decreased amounts of proteins with symmetric dimethylarginine (sDMA). These findings led to the hypothesis that accumulation of intracellular MTA inhibits the protein arginine methylase (PRMT5) responsible for bulk protein sDMAylation. Here, we confirm that MTAP-deleted cells have increased MTA accumulation and reduced protein sDMAylation. However, we also show that addition of extracellular MTA can cause a dramatic reduction of the steady-state levels of sDMA-containing proteins in MTAP+ cells, even though no sustained increase in intracellular MTA is found because of catabolism of MTA by MTAP. We determined that inhibition of protein sDMAylation by MTA occurs within 48 h, is reversible, and is specific. In addition, we have identified two enhancer-binding proteins, FUBP1 and FUBP3, that are differentially sDMAylated in response to MTAP and MTA. These proteins work via the far upstream element site located upstream of Myc and other promoters. Using a transcription reporter construct containing the far upstream element site, we demonstrate that MTA addition can reduce transcription, suggesting that the reduction in FUBP1 and FUBP3 sDMAylation has functional consequences. Overall, our findings show that extracellular MTA can inhibit protein sDMAylation and that this inhibition can affect FUBP function.
MeSH term(s)	Arginine/analogs & derivatives ; DNA-Binding Proteins/metabolism ; Deoxyadenosines ; Humans ; Methionine/metabolism ; Methylation ; Polyamines ; Protein-Arginine N-Methyltransferases/genetics ; Protein-Arginine N-Methyltransferases/metabolism ; Purine-Nucleoside Phosphorylase/genetics ; Purine-Nucleoside Phosphorylase/metabolism ; RNA-Binding Proteins/metabolism ; Sequence Deletion ; Thionucleosides
Chemical Substances	DNA-Binding Proteins ; Deoxyadenosines ; FUBP1 protein, human ; Polyamines ; RNA-Binding Proteins ; Thionucleosides ; symmetric dimethylarginine (49787G1ULV) ; 5'-methylthioadenosine (634Z2VK3UQ) ; Arginine (94ZLA3W45F) ; Methionine (AE28F7PNPL) ; PRMT5 protein, human (EC 2.1.1.319) ; Protein-Arginine N-Methyltransferases (EC 2.1.1.319) ; Purine-Nucleoside Phosphorylase (EC 2.4.2.1)
Language	English
Publishing date	2022-08-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.102367
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Article ; Online: The c.797 G>A (p.R266K) cystathionine β-synthase mutation causes homocystinuria by affecting protein stability.

Gupta, Sapna / Wang, Liqun / Kruger, Warren D

Human mutation

2017 Volume 38, Issue 7, Page(s) 863–869

Abstract: Mutations in the cystathionine beta-synthase (CBS) gene are the cause of classical homocystinuria, the most common inborn error in sulfur metabolism. The c.797 G>A (p.R266K) mutation in CBS was originally described in several Norwegian pyridoxine ... ...

Abstract	Mutations in the cystathionine beta-synthase (CBS) gene are the cause of classical homocystinuria, the most common inborn error in sulfur metabolism. The c.797 G>A (p.R266K) mutation in CBS was originally described in several Norwegian pyridoxine responsive CBS deficient patients, and heterologous gene expression studies have shown that the protein has near wild-type levels of enzyme activity. Here, we characterize a transgenic mouse lacking endogenous Cbs and expressing p.R266K human CBS protein from a zinc inducible metallothionein promoter (Tg-R266K Cbs
MeSH term(s)	Alleles ; Animals ; Bortezomib/pharmacology ; Cystathionine beta-Synthase/genetics ; DNA Mutational Analysis ; Female ; Homocysteine/blood ; Homocystinuria/genetics ; Humans ; Male ; Mice ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Mice, Transgenic ; Mutation ; Proteasome Inhibitors/chemistry ; Pyridoxine/chemistry
Chemical Substances	Proteasome Inhibitors ; Homocysteine (0LVT1QZ0BA) ; Bortezomib (69G8BD63PP) ; Cystathionine beta-Synthase (EC 4.2.1.22) ; Pyridoxine (KV2JZ1BI6Z)
Language	English
Publishing date	2017
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1126646-6
ISSN	1098-1004 ; 1059-7794
ISSN (online)	1098-1004
ISSN	1059-7794
DOI	10.1002/humu.23240
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Article ; Online: Analysis of differential neonatal lethality in cystathionine β-synthase deficient mouse models using metabolic profiling.

Gupta, Sapna / Wang, Liqun / Slifker, Michael J / Cai, Kathy Q / Maclean, Kenneth N / Wasek, Brandi / Bottiglieri, Teodoro / Kruger, Warren D

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2021 Volume 35, Issue 6, Page(s) e21629

Abstract: Cystathionine beta-synthase (CBS) is a key enzyme of the trans-sulfuration pathway that converts homocysteine to cystathionine. Loss of CBS activity due to mutation results in CBS deficiency, an inborn error of metabolism characterized by extreme ... ...

Abstract	Cystathionine beta-synthase (CBS) is a key enzyme of the trans-sulfuration pathway that converts homocysteine to cystathionine. Loss of CBS activity due to mutation results in CBS deficiency, an inborn error of metabolism characterized by extreme elevation of plasma total homocysteine (tHcy). C57BL6 mice containing either a homozygous null mutation in the cystathionine β-synthase (Cbs
MeSH term(s)	Animals ; Animals, Newborn ; Cystathionine beta-Synthase/physiology ; Disease Models, Animal ; Female ; Liver Failure/etiology ; Liver Failure/metabolism ; Liver Failure/pathology ; Male ; Metabolome ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Mutation ; Phenotype
Chemical Substances	Cystathionine beta-Synthase (EC 4.2.1.22)
Language	English
Publishing date	2021-05-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.202100302R
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Article ; Online: Long-term functional correction of cystathionine β-synthase deficiency in mice by adeno-associated viral gene therapy.

Lee, Hyung-Ok / Salami, Christiana O / Sondhi, Dolan / Kaminsky, Stephen M / Crystal, Ronald G / Kruger, Warren D

Journal of inherited metabolic disease

2021 Volume 44, Issue 6, Page(s) 1382–1392

Abstract: Cystathionine β-synthase (CBS) deficiency is a recessive inborn error of sulfur metabolism characterized by elevated blood levels of total homocysteine (tHcy). Patients diagnosed with CBS deficiency are currently treated by a combination of vitamin ... ...

Abstract	Cystathionine β-synthase (CBS) deficiency is a recessive inborn error of sulfur metabolism characterized by elevated blood levels of total homocysteine (tHcy). Patients diagnosed with CBS deficiency are currently treated by a combination of vitamin supplementation and restriction of foods containing the homocysteine precursor methionine, but the effectiveness of this therapy is limited due to poor compliance. A mouse model for CBS deficiency (Tg-I278T Cbs
MeSH term(s)	Animals ; Cystathionine beta-Synthase/blood ; Cystathionine beta-Synthase/deficiency ; Cystathionine beta-Synthase/genetics ; Dependovirus/genetics ; Disease Models, Animal ; Female ; Gene Expression ; Gene Transfer Techniques ; Genetic Therapy ; Genetic Vectors/administration & dosage ; Genetic Vectors/genetics ; Homocystinuria/genetics ; Homocystinuria/metabolism ; Homocystinuria/therapy ; Liver/metabolism ; Liver/pathology ; Male ; Mice ; Mice, Knockout ; Phenotype
Chemical Substances	Cystathionine beta-Synthase (EC 4.2.1.22)
Language	English
Publishing date	2021-10-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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.12437
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