Erratum to: ω-Amidase: an underappreciated, but important enzyme in l-glutamine and l-asparagine metabolism; relevance to sulfur and nitrogen metabolism, tumor biology and hyperammonemic diseases

Cooper, Arthur J. L.; Shurubor, Yevgeniya I.; Dorai, Thambi; Pinto, John T.; Исакова, Е. П.; Deryabina, Yulia I.; Denton, Travis T.; Krasnikov, Boris F.

doi:10.1007/s00726-015-2115-x

Cited by 16 publications

(3 citation statements)

References 121 publications

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“…16 Aminotransferase was reported as an important alternative path involved in glutaminolysis. 5 Among these proteins, the binding affinity of GatCAB to the biotinylated CPD-3B has a K D of 5.4 nM and might be a novel protein target for CPD-3B. Under the same conditions, the biotinylated BPTES (Figure 4) showed significant binding…”

Section: Cpd-3b-treated Cells Showed Dose-dependent Disruption Of Mitochondrial Membrane Potential (Mmp)mentioning

confidence: 96%

“…4 The predominant glutaminolysis pathway in most cancer cells is through formation of glutamate (Glu) by the ratelimiting glutaminase (isomers: KGA/GAC) and then, to αketoglutarate (α-KG) by GDH or by aminotransferase in the presence of other amino acids. 2 Another alternative pathway for Gln metabolism is first transamination to α-ketoglutar-amate (KGM) followed by hydrolysis of KGM to αketoglutarate by an amidase, 5 and finally into the TCA cycle. The relative contribution of each pathway varies among different cell types and tissues.…”

Section: ■ Introductionmentioning

confidence: 99%

“…CB-839 is a successful compound in stage II clinical investigation for triple negative breast cancer therapeutics. However, it remains to be investigated whether the limited efficacy is the result of a bypass through an alternative pathway involving aminotransferase 5 or through improved glycolytic flux. 13 In addition, Ebselen was initially reported as a very potent nM level allosteric KGA inhibitor, 14 but lacks significant anticancer activity in cell based assay.…”

Section: ■ Introductionmentioning

confidence: 99%

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Kidney-Type Glutaminase Inhibitor Hexylselen Selectively Kills Cancer Cells via a Three-Pronged Mechanism

Ruan

Hou

et al. 2019

ACS Pharmacol. Transl. Sci.

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Tumor metabolism has been deeply investigated for cancer therapeutics. Here, we demonstrate that glutamine deficiency alone could not completely inhibit cancer cell growth and that many potent kidney-type glutaminase (KGA) inhibitors did not show satisfying in vivo efficacy. The potent KGA allosteric inhibitor, CB-839, resulted in up to 80% growth inhibition of all tested cell lines, whereas Hexylselen (CPD-3B), a KGA/glutamate dehydrogenase (GDH) inhibitor, showed essentially no toxicity to normal cells up to a 10 μM concentration and could completely inhibit the growth of many aggressive cell lines. Further analyses showed that CPD-3B targets not only KGA and GDH but also thioredoxin reductase (TrxR) and amidotransferase (GatCAB), which results in corresponding regulation of Akt/Erk/caspase-9 signaling pathways. In an aggressive liver cancer xenograft model, CPD-3B significantly reduced tumor size, caused massive tumor tissue damage, and prolonged survival rate. These provide important information for furthering the drug design of an effective anticancer KGA allosteric inhibitor.

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Section: Cpd-3b-treated Cells Showed Dose-dependent Disruption Of Mitochondrial Membrane Potential (Mmp)mentioning

confidence: 96%

Section: ■ Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Kidney-Type Glutaminase Inhibitor Hexylselen Selectively Kills Cancer Cells via a Three-Pronged Mechanism

Ruan

Hou

et al. 2019

ACS Pharmacol. Transl. Sci.

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Upregulation of the Glutaminase II Pathway Contributes to Glutamate Production upon Glutaminase 1 Inhibition in Pancreatic Cancer

et al. 2019

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The targeting of glutamine metabolism specifically via pharmacological inhibition of glutaminase 1 (GLS1) has been translated into clinical trials as a novel therapy for several cancers. The results, though encouraging, show room for improvement in terms of tumor reduction. In this study, the glutaminase II pathway is found to be upregulated for glutamate production upon GLS1 inhibition in pancreatic tumors. Moreover, genetic suppression of glutamine transaminase K (GTK), a key enzyme of the glutaminase II pathway, leads to the complete inhibition of pancreatic tumorigenesis in vivo unveiling GTK as a new metabolic target for cancer therapy. These results suggest that current trials using GLS1 inhibition as a therapeutic approach targeting glutamine metabolism in cancer should take into account the upregulation of other metabolic pathways that can lead to glutamate production; one such pathway is the glutaminase II pathway via GTK.

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Serum Amino Acid Profiling in Citrin-Deficient Children Exhibiting Normal Liver Function During the Apparently Healthy Period

et al. 2018

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In the citrin-deficient children during the healthy stage, the characteristics of serum amino acids, including decrease of glucogenic amino acids, and increase of ketogenic amino acids, BCAAs, valine intermediate, and β-alanine, were found by comparison to the age-matched healthy control children, and it suggested that the characteristic alteration of serum amino acids may be resulted from compensation for energy metabolism and ammonia detoxification.

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Erratum to: ω-Amidase: an underappreciated, but important enzyme in l-glutamine and l-asparagine metabolism; relevance to sulfur and nitrogen metabolism, tumor biology and hyperammonemic diseases

Cited by 16 publications

References 121 publications

Kidney-Type Glutaminase Inhibitor Hexylselen Selectively Kills Cancer Cells via a Three-Pronged Mechanism

Kidney-Type Glutaminase Inhibitor Hexylselen Selectively Kills Cancer Cells via a Three-Pronged Mechanism

Upregulation of the Glutaminase II Pathway Contributes to Glutamate Production upon Glutaminase 1 Inhibition in Pancreatic Cancer

Serum Amino Acid Profiling in Citrin-Deficient Children Exhibiting Normal Liver Function During the Apparently Healthy Period

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