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Article ; Online: Yeast phospholipase C is required for stability of casein kinase I Yck2p and expression of hexose transporters.

Zhang, Tiantian / Galdieri, Luciano / Hasek, Jiri / Vancura, Ales

2017 Volume 364, Issue 22

Abstract: Phospholipase C (Plc1p) in Saccharomyces cerevisiae is required for normal degradation of repressor Mth1p and expression of the HXT genes encoding cell membrane transporters of glucose. Plc1p is also required for normal localization of glucose ... ...

Abstract	Phospholipase C (Plc1p) in Saccharomyces cerevisiae is required for normal degradation of repressor Mth1p and expression of the HXT genes encoding cell membrane transporters of glucose. Plc1p is also required for normal localization of glucose transporters to the cell membrane. Consequently, plc1Δ cells display histone hypoacetylation and transcriptional defects due to reduced uptake and metabolism of glucose to acetyl-CoA, a substrate for histone acetyltransferases. In the presence of glucose, Mth1p is phosphorylated by casein kinase I Yck1/2p, ubiquitinated by the SCFGrr1 complex and degraded by the proteasome. Here, we show that while Plc1p does not affect the function of the SCFGrr1 complex or the proteasome, it is required for normal protein level of Yck2p. Since stability of Yck1/2p is regulated by a glucose-dependent mechanism, PLC1 inactivation results in destabilization of Yck1/2p and defect in Mth1p degradation. Based on our results and published data, we propose a model in which plc1Δ mutation causes increased internalization of glucose transporters, decreased transport of glucose into the cells, and consequently decreased stability of Yck1/2p, increased stability of Mth1p and decreased expression of the HXT genes.
MeSH term(s)	Casein Kinase I/chemistry ; Casein Kinase I/metabolism ; Enzyme Stability ; Monosaccharide Transport Proteins/genetics ; Monosaccharide Transport Proteins/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism ; Type C Phospholipases/metabolism
Chemical Substances	Monosaccharide Transport Proteins ; Recombinant Proteins ; Saccharomyces cerevisiae Proteins ; Casein Kinase I (EC 2.7.11.1) ; YCK2 protein, S cerevisiae (EC 2.7.11.1) ; Type C Phospholipases (EC 3.1.4.-) ; Plc1 protein, S cerevisiae (EC 3.1.4.3)
Language	English
Publishing date	2017-10-30
Publishing country	England
Document type	Journal Article
ZDB-ID	752343-9
ISSN	1574-6968 ; 0378-1097
ISSN (online)	1574-6968
ISSN	0378-1097
DOI	10.1093/femsle/fnx227
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Article ; Online: Reduced Histone Expression or a Defect in Chromatin Assembly Induces Respiration.

Galdieri, Luciano / Zhang, Tiantian / Rogerson, Daniella / Vancura, Ales

Molecular and cellular biology

2016 Volume 36, Issue 7, Page(s) 1064–1077

Abstract: Regulation of mitochondrial biogenesis and respiration is a complex process that involves several signaling pathways and transcription factors as well as communication between the nuclear and mitochondrial genomes. Here we show that decreased expression ... ...

Abstract	Regulation of mitochondrial biogenesis and respiration is a complex process that involves several signaling pathways and transcription factors as well as communication between the nuclear and mitochondrial genomes. Here we show that decreased expression of histones or a defect in nucleosome assembly in the yeast Saccharomyces cerevisiae results in increased mitochondrial DNA (mtDNA) copy numbers, oxygen consumption, ATP synthesis, and expression of genes encoding enzymes of the tricarboxylic acid (TCA) cycle and oxidative phosphorylation (OXPHOS). The metabolic shift from fermentation to respiration induced by altered chromatin structure is associated with the induction of the retrograde (RTG) pathway and requires the activity of the Hap2/3/4/5p complex as well as the transport and metabolism of pyruvate in mitochondria. Together, our data indicate that altered chromatin structure relieves glucose repression of mitochondrial respiration by inducing transcription of the TCA cycle and OXPHOS genes carried by both nuclear and mitochondrial DNA.
MeSH term(s)	Adenosine Triphosphate/biosynthesis ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/metabolism ; CCAAT-Binding Factor/metabolism ; Chromatin Assembly and Disassembly ; DNA Copy Number Variations ; DNA, Fungal/metabolism ; DNA, Mitochondrial/metabolism ; Fermentation ; Gene Expression Regulation, Fungal ; Histones/biosynthesis ; Histones/genetics ; Mitochondria/metabolism ; Oxidative Phosphorylation ; Oxygen Consumption ; Pyruvic Acid/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; CCAAT-Binding Factor ; DNA, Fungal ; DNA, Mitochondrial ; HAP4 protein, S cerevisiae ; Histones ; RTG1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Pyruvic Acid (8558G7RUTR) ; Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2016-01-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.00770-15
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Article ; Online: Activation of AMP-activated Protein Kinase by Metformin Induces Protein Acetylation in Prostate and Ovarian Cancer Cells.

Galdieri, Luciano / Gatla, Himavanth / Vancurova, Ivana / Vancura, Ales

The Journal of biological chemistry

2016 Volume 291, Issue 48, Page(s) 25154–25166

Abstract: AMP-activated protein kinase (AMPK) is an energy sensor and master regulator of metabolism. AMPK functions as a fuel gauge monitoring systemic and cellular energy status. Activation of AMPK occurs when the intracellular AMP/ATP ratio increases and leads ... ...

Abstract	AMP-activated protein kinase (AMPK) is an energy sensor and master regulator of metabolism. AMPK functions as a fuel gauge monitoring systemic and cellular energy status. Activation of AMPK occurs when the intracellular AMP/ATP ratio increases and leads to a metabolic switch from anabolism to catabolism. AMPK phosphorylates and inhibits acetyl-CoA carboxylase (ACC), which catalyzes carboxylation of acetyl-CoA to malonyl-CoA, the first and rate-limiting reaction in de novo synthesis of fatty acids. AMPK thus regulates homeostasis of acetyl-CoA, a key metabolite at the crossroads of metabolism, signaling, chromatin structure, and transcription. Nucleocytosolic concentration of acetyl-CoA affects histone acetylation and links metabolism and chromatin structure. Here we show that activation of AMPK with the widely used antidiabetic drug metformin or with the AMP mimetic 5-aminoimidazole-4-carboxamide ribonucleotide increases the inhibitory phosphorylation of ACC and decreases the conversion of acetyl-CoA to malonyl-CoA, leading to increased protein acetylation and altered gene expression in prostate and ovarian cancer cells. Direct inhibition of ACC with allosteric inhibitor 5-(tetradecyloxy)-2-furoic acid also increases acetylation of histones and non-histone proteins. Because AMPK activation requires liver kinase B1, metformin does not induce protein acetylation in liver kinase B1-deficient cells. Together, our data indicate that AMPK regulates the availability of nucleocytosolic acetyl-CoA for protein acetylation and that AMPK activators, such as metformin, have the capacity to increase protein acetylation and alter patterns of gene expression, further expanding the plethora of metformin's physiological effects.
MeSH term(s)	AMP-Activated Protein Kinases/genetics ; AMP-Activated Protein Kinases/metabolism ; Acetyl Coenzyme A/genetics ; Acetyl Coenzyme A/metabolism ; Acetylation/drug effects ; Female ; Gene Expression Regulation, Neoplastic/drug effects ; Gene Expression Regulation, Neoplastic/genetics ; HeLa Cells ; Humans ; Male ; Malonyl Coenzyme A/genetics ; Malonyl Coenzyme A/metabolism ; Metformin/pharmacology ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Ovarian Neoplasms/genetics ; Ovarian Neoplasms/metabolism ; Prostatic Neoplasms/genetics ; Prostatic Neoplasms/metabolism ; Protein Processing, Post-Translational/drug effects ; Protein Processing, Post-Translational/genetics
Chemical Substances	Neoplasm Proteins ; Malonyl Coenzyme A (524-14-1) ; Acetyl Coenzyme A (72-89-9) ; Metformin (9100L32L2N) ; AMP-Activated Protein Kinases (EC 2.7.11.31)
Language	English
Publishing date	2016-10-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M116.742247
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Article ; Online: Reduced Histone Expression or a Defect in Chromatin Assembly Induces Respiration

Galdieri, Luciano / Zhang, Tiantian / Rogerson, Daniella / Vancura, Ales

Molecular and Cellular Biology. 2016 Apr. 1, v. 36, no. 7 p.1064-1077

2016

Abstract	Regulation of mitochondrial biogenesis and respiration is a complex process that involves several signaling pathways and transcription factors as well as communication between the nuclear and mitochondrial genomes. Here we show that decreased expression of histones or a defect in nucleosome assembly in the yeast Saccharomyces cerevisiae results in increased mitochondrial DNA (mtDNA) copy numbers, oxygen consumption, ATP synthesis, and expression of genes encoding enzymes of the tricarboxylic acid (TCA) cycle and oxidative phosphorylation (OXPHOS). The metabolic shift from fermentation to respiration induced by altered chromatin structure is associated with the induction of the retrograde (RTG) pathway and requires the activity of the Hap2/3/4/5p complex as well as the transport and metabolism of pyruvate in mitochondria. Together, our data indicate that altered chromatin structure relieves glucose repression of mitochondrial respiration by inducing transcription of the TCA cycle and OXPHOS genes carried by both nuclear and mitochondrial DNA.
Keywords	Saccharomyces cerevisiae ; biogenesis ; fermentation ; glucose ; histones ; mitochondria ; mitochondrial DNA ; mitochondrial genome ; nucleosomes ; oxidative phosphorylation ; oxygen consumption ; pyruvic acid ; tricarboxylic acid cycle ; yeasts
Language	English
Dates of publication	2016-0401
Size	p. 1064-1077.
Publishing place	Taylor & Francis
Document type	Article ; Online
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.00770-15
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Acetyl-CoA carboxylase regulates global histone acetylation.

Galdieri, Luciano / Vancura, Ales

The Journal of biological chemistry

2012 Volume 287, Issue 28, Page(s) 23865–23876

Abstract: Histone acetylation depends on intermediary metabolism for supplying acetyl-CoA in the nucleocytosolic compartment. However, because nucleocytosolic acetyl-CoA is also used for de novo synthesis of fatty acids, histone acetylation and synthesis of fatty ... ...

Abstract	Histone acetylation depends on intermediary metabolism for supplying acetyl-CoA in the nucleocytosolic compartment. However, because nucleocytosolic acetyl-CoA is also used for de novo synthesis of fatty acids, histone acetylation and synthesis of fatty acids compete for the same acetyl-CoA pool. The first and rate-limiting reaction in de novo synthesis of fatty acids is carboxylation of acetyl-CoA to form malonyl-CoA, catalyzed by acetyl-CoA carboxylase. In yeast Saccharomyces cerevisiae, acetyl-CoA carboxylase is encoded by the ACC1 gene. In this study, we show that attenuated expression of ACC1 results in increased acetylation of bulk histones, globally increased acetylation of chromatin histones, and altered transcriptional regulation. Together, our data indicate that Acc1p activity regulates the availability of acetyl-CoA for histone acetyltransferases, thus representing a link between intermediary metabolism and epigenetic mechanisms of transcriptional regulation.
MeSH term(s)	Acetyl-CoA Carboxylase/genetics ; Acetyl-CoA Carboxylase/metabolism ; Acetylation ; Blotting, Western ; Chromatin/drug effects ; Chromatin/genetics ; Chromatin/metabolism ; Doxycycline/pharmacology ; Gene Expression Regulation, Enzymologic/drug effects ; Gene Expression Regulation, Fungal/drug effects ; Histone Acetyltransferases/genetics ; Histone Acetyltransferases/metabolism ; Histones/metabolism ; Mutation ; Reverse Transcriptase Polymerase Chain Reaction ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Chromatin ; Histones ; Saccharomyces cerevisiae Proteins ; Histone Acetyltransferases (EC 2.3.1.48) ; Acetyl-CoA Carboxylase (EC 6.4.1.2) ; Doxycycline (N12000U13O)
Language	English
Publishing date	2012-05-11
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	10.1074/jbc.M112.380519
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Article ; Online: The yeast AMPK homolog SNF1 regulates acetyl coenzyme A homeostasis and histone acetylation.

Zhang, Man / Galdieri, Luciano / Vancura, Ales

Molecular and cellular biology

2013 Volume 33, Issue 23, Page(s) 4701–4717

Abstract: Acetyl coenzyme A (acetyl-CoA) is a key metabolite at the crossroads of metabolism, signaling, chromatin structure, and transcription. Concentration of acetyl-CoA affects histone acetylation and links intermediary metabolism and transcriptional ... ...

Abstract	Acetyl coenzyme A (acetyl-CoA) is a key metabolite at the crossroads of metabolism, signaling, chromatin structure, and transcription. Concentration of acetyl-CoA affects histone acetylation and links intermediary metabolism and transcriptional regulation. Here we show that SNF1, the budding yeast ortholog of the mammalian AMP-activated protein kinase (AMPK), plays a role in the regulation of acetyl-CoA homeostasis and global histone acetylation. SNF1 phosphorylates and inhibits acetyl-CoA carboxylase, which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the first and rate-limiting reaction in the de novo synthesis of fatty acids. Inactivation of SNF1 results in a reduced pool of cellular acetyl-CoA, globally decreased histone acetylation, and reduced fitness and stress resistance. The histone acetylation and transcriptional defects can be partially suppressed and the overall fitness improved in snf1Δ mutant cells by increasing the cellular concentration of acetyl-CoA, indicating that the regulation of acetyl-CoA homeostasis represents another mechanism in the SNF1 regulatory repertoire.
MeSH term(s)	Acetyl Coenzyme A/metabolism ; Acetylation ; Acetyltransferases/genetics ; Acetyltransferases/metabolism ; Chromatin/metabolism ; Coenzyme A Ligases/genetics ; Coenzyme A Ligases/metabolism ; DNA, Fungal/genetics ; DNA, Intergenic/genetics ; Epigenetic Repression ; Gene Expression Regulation, Fungal ; Gene Knockout Techniques ; Histone Acetyltransferases/metabolism ; Histone Deacetylases/metabolism ; Histones/metabolism ; Homeostasis ; Malonyl Coenzyme A/metabolism ; Promoter Regions, Genetic ; Protein Processing, Post-Translational ; Protein-Serine-Threonine Kinases/physiology ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/growth & development ; Stress, Physiological
Chemical Substances	Chromatin ; DNA, Fungal ; DNA, Intergenic ; Histones ; Malonyl Coenzyme A (524-14-1) ; Acetyl Coenzyme A (72-89-9) ; Acetyltransferases (EC 2.3.1.-) ; aminoglycoside N1-acetyltransferase (EC 2.3.1.-) ; Histone Acetyltransferases (EC 2.3.1.48) ; SNF1-related protein kinases (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Histone Deacetylases (EC 3.5.1.98) ; Coenzyme A Ligases (EC 6.2.1.-) ; Acsl1 protein, rat (EC 6.2.1.3)
Language	English
Publishing date	2013-09-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.00198-13
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Zs.A 1666: Show issues

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Article ; Online: Yeast phospholipase C is required for normal acetyl-CoA homeostasis and global histone acetylation.

Galdieri, Luciano / Chang, Jennifer / Mehrotra, Swati / Vancura, Ales

The Journal of biological chemistry

2013 Volume 288, Issue 39, Page(s) 27986–27998

Abstract: Phospholipase C (Plc1p) is required for the initial step of inositol polyphosphate (InsP) synthesis, and yeast cells with deletion of the PLC1 gene are completely devoid of any InsPs and display aberrations in transcriptional regulation. Here we show ... ...

Abstract	Phospholipase C (Plc1p) is required for the initial step of inositol polyphosphate (InsP) synthesis, and yeast cells with deletion of the PLC1 gene are completely devoid of any InsPs and display aberrations in transcriptional regulation. Here we show that Plc1p is required for a normal level of histone acetylation; plc1Δ cells that do not synthesize any InsPs display decreased acetylation of bulk histones and global hypoacetylation of chromatin histones. In accordance with the role of Plc1p in supporting histone acetylation, plc1Δ mutation is synthetically lethal with mutations in several subunits of SAGA and NuA4 histone acetyltransferase (HAT) complexes. Conversely, the growth rate, sensitivity to multiple stresses, and the transcriptional defects of plc1Δ cells are partially suppressed by deletion of histone deacetylase HDA1. The histone hypoacetylation in plc1Δ cells is due to the defect in degradation of repressor Mth1p, and consequently lower expression of HXT genes and reduced conversion of glucose to acetyl-CoA, a substrate for HATs. The histone acetylation and transcriptional defects can be partially suppressed and the overall fitness improved in plc1Δ cells by increasing the cellular concentration of acetyl-CoA. Together, our data indicate that Plc1p and InsPs are required for normal acetyl-CoA homeostasis, which, in turn, regulates global histone acetylation.
MeSH term(s)	Acetyl Coenzyme A/metabolism ; Acetylation ; Biological Transport ; Chromatin/metabolism ; Gene Expression Regulation, Enzymologic ; Glucose/metabolism ; Histone Acetyltransferases/metabolism ; Histone Deacetylases/metabolism ; Histones/metabolism ; Homeostasis ; Inositol Phosphates/metabolism ; Mutation ; Phenotype ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae Proteins/metabolism ; Temperature ; Transcription, Genetic ; Type C Phospholipases/metabolism
Chemical Substances	Chromatin ; Histones ; Inositol Phosphates ; Saccharomyces cerevisiae Proteins ; Acetyl Coenzyme A (72-89-9) ; Histone Acetyltransferases (EC 2.3.1.48) ; Type C Phospholipases (EC 3.1.4.-) ; Plc1 protein, S cerevisiae (EC 3.1.4.3) ; Histone Deacetylases (EC 3.5.1.98) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2013-08-02
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	10.1074/jbc.M113.492348
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Article ; Online: Determination of histone acetylation status by chromatin immunoprecipitation.

Galdieri, Luciano / Moon, John / Vancura, Ales

Methods in molecular biology (Clifton, N.J.)

2012 Volume 809, Page(s) 255–265

Abstract: Histone acetylation is the most studied posttranslation modification of nucleosomes. Understanding the mechanisms involved in global and promoter-specific histone acetylation will shed light on the control of transcriptional regulation. Chromatin ... ...

Abstract	Histone acetylation is the most studied posttranslation modification of nucleosomes. Understanding the mechanisms involved in global and promoter-specific histone acetylation will shed light on the control of transcriptional regulation. Chromatin immunoprecipitation is a powerful technique to study protein-DNA interactions in vivo. Proteins and DNA are cross-linked with formaldehyde, cells are lysed, and DNA is sheared by sonication. Protein-DNA complexes are immunoprecipitated with antibodies specific for total and acetylated histones and the relative occupancy of acetylated and total histones at selected loci is assessed by real-time PCR of the purified DNA.
MeSH term(s)	Acetylation ; Chromatin Immunoprecipitation/methods ; Histones/metabolism ; Real-Time Polymerase Chain Reaction ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism
Chemical Substances	Histones
Language	English
Publishing date	2012
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-61779-376-9_17
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Article ; Online: Protein acetylation and acetyl coenzyme a metabolism in budding yeast.

Galdieri, Luciano / Zhang, Tiantian / Rogerson, Daniella / Lleshi, Rron / Vancura, Ales

Eukaryotic cell

2014 Volume 13, Issue 12, Page(s) 1472–1483

Abstract: Cells sense and appropriately respond to the physical conditions and availability of nutrients in their environment. This sensing of the environment and consequent cellular responses are orchestrated by a multitude of signaling pathways and typically ... ...

Abstract	Cells sense and appropriately respond to the physical conditions and availability of nutrients in their environment. This sensing of the environment and consequent cellular responses are orchestrated by a multitude of signaling pathways and typically involve changes in transcription and metabolism. Recent discoveries suggest that the signaling and transcription machineries are regulated by signals which are derived from metabolism and reflect the metabolic state of the cell. Acetyl coenzyme A (CoA) is a key metabolite that links metabolism with signaling, chromatin structure, and transcription. Acetyl-CoA is produced by glycolysis as well as other catabolic pathways and used as a substrate for the citric acid cycle and as a precursor in synthesis of fatty acids and steroids and in other anabolic pathways. This central position in metabolism endows acetyl-CoA with an important regulatory role. Acetyl-CoA serves as a substrate for lysine acetyltransferases (KATs), which catalyze the transfer of acetyl groups to the epsilon-amino groups of lysines in histones and many other proteins. Fluctuations in the concentration of acetyl-CoA, reflecting the metabolic state of the cell, are translated into dynamic protein acetylations that regulate a variety of cell functions, including transcription, replication, DNA repair, cell cycle progression, and aging. This review highlights the synthesis and homeostasis of acetyl-CoA and the regulation of transcriptional and signaling machineries in yeast by acetylation.
MeSH term(s)	Acetyl Coenzyme A/metabolism ; Acetylation ; Animals ; Homeostasis ; Humans ; Protein Processing, Post-Translational ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Saccharomyces cerevisiae Proteins ; Acetyl Coenzyme A (72-89-9)
Language	English
Publishing date	2014-10-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2077635-4
ISSN	1535-9786 ; 1535-9778
ISSN (online)	1535-9786
ISSN	1535-9778
DOI	10.1128/EC.00189-14
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Zs.A 5779: Show issues

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Article ; Online: Defining phenotypic and functional heterogeneity of glioblastoma stem cells by mass cytometry.

Galdieri, Luciano / Jash, Arijita / Malkova, Olga / Mao, Diane D / DeSouza, Patrick / Chu, Yunli E / Salter, Amber / Campian, Jian L / Naegle, Kristen M / Brennan, Cameron W / Wakimoto, Hiroaki / Oh, Stephen T / Kim, Albert H / Chheda, Milan G

JCI insight

2021 Volume 6, Issue 4

Abstract: Most patients with glioblastoma (GBM) die within 2 years. A major therapeutic goal is to target GBM stem cells (GSCs), a subpopulation of cells that contribute to treatment resistance and recurrence. Since their discovery in 2003, GSCs have been isolated ...

Abstract	Most patients with glioblastoma (GBM) die within 2 years. A major therapeutic goal is to target GBM stem cells (GSCs), a subpopulation of cells that contribute to treatment resistance and recurrence. Since their discovery in 2003, GSCs have been isolated using single-surface markers, such as CD15, CD44, CD133, and α6 integrin. It remains unknown how these single-surface marker-defined GSC populations compare with each other in terms of signaling and function and whether expression of different combinations of these markers is associated with different functional capacity. Using mass cytometry and fresh operating room specimens, we found 15 distinct GSC subpopulations in patients, and they differed in their MEK/ERK, WNT, and AKT pathway activation status. Once in culture, some subpopulations were lost and previously undetectable ones materialized. GSCs that highly expressed all 4 surface markers had the greatest self-renewal capacity, WNT inhibitor sensitivity, and in vivo tumorigenicity. This work highlights the potential signaling and phenotypic diversity of GSCs. Larger patient sample sizes and antibody panels are required to confirm these findings.
MeSH term(s)	AC133 Antigen ; Animals ; Brain Neoplasms/genetics ; Female ; Gene Expression Regulation, Neoplastic ; Genetic Heterogeneity ; Glioblastoma/genetics ; Glioblastoma/immunology ; Humans ; Hyaluronan Receptors ; Lewis X Antigen ; Mice ; Neoplastic Stem Cells/metabolism
Chemical Substances	AC133 Antigen ; Hyaluronan Receptors ; Lewis X Antigen
Language	English
Publishing date	2021-02-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2379-3708
ISSN (online)	2379-3708
DOI	10.1172/jci.insight.128456
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