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Glycolytic enzymes in non-glycolytic web: functional analysis of the key players

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Abstract

To survive in the tumour microenvironment, cancer cells undergo rapid metabolic reprograming and adaptability. One of the key characteristics of cancer is increased glycolytic selectivity and decreased oxidative phosphorylation (OXPHOS). Apart from ATP synthesis, glycolysis is also responsible for NADH regeneration and macromolecular biosynthesis, such as amino acid biosynthesis and nucleotide biosynthesis. This allows cancer cells to survive and proliferate even in low-nutrient and oxygen conditions, making glycolytic enzymes a promising target for various anti-cancer agents. Oncogenic activation is also caused by the uncontrolled production and activity of glycolytic enzymes. Nevertheless, in addition to conventional glycolytic processes, some glycolytic enzymes are involved in non-canonical functions such as transcriptional regulation, autophagy, epigenetic changes, inflammation, various signaling cascades, redox regulation, oxidative stress, obesity and fatty acid metabolism, diabetes and neurodegenerative disorders, and hypoxia. The mechanisms underlying the non-canonical glycolytic enzyme activities are still not comprehensive. This review summarizes the current findings on the mechanisms fundamental to the non-glycolytic actions of glycolytic enzymes and their intermediates in maintaining the tumor microenvironment.

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Abbreviations

2-DG:

2-deoxy-D-glucose

5-TG:

5-thioglucose

6-PGDH:

6-Phosphogluconate dehydrogenase

6-PGL:

6-Phosphogluconolactonase

ACC:

Acetyl CoA Carboxylase

ACS 1:

Acetyl-CoA synthetase

AD:

Alzheimer’s disease

AKT S1:

AKT1 Substrate 1

ALS:

Amyotrophic lateral sclerosis

AMF:

Autocrine motility factor

AMFR:

Autocrine motility factor receptor

AMP:

Adenosine monophosphate

AMPK:

AMP-activated protein kinase

ANLS:

Astrocyte neuron lactate shuttle

APC:

Axin-Adenomatosis Polyposis Coli

APP:

Amyloid precursor protein

ARE:

Anti-oxidant responsive elements

ARNT:

Aryl hydrocarbon receptor nuclear translocator

ATM:

Ataxia- telangiectasia mutant

ATP:

Adenosine triphosphate

BECN1:

Beclin-1

c-AMP:

Cyclic AMP

CBP:

CREB-binding protein

CNS:

Central nervous system

CPT 1:

Carnitine palmitoyl transferase 1

Cyt c:

-Cytochrome c

DNA:

Deoxyribonucleic acid

DVL:

Dishevelled

EGF:

Epidermal growth factor

EGFR:

Epidermal growth factor receptor

ENO1:

Enolase 1

ER:

Endoplasmic reticulum

ERK:

Extracellular signal-regulated kinase

ETC:

Electron transport chain

FAS:

Fatty acid synthesis

FDG-PET:

Fluorodeoxyglucose positron emission tomography

FDH:

Fumarate dehydrogenase

FDH:

Folate dehydrogenase

FIH:

Factor inhibiting HIF

FZD:

Frizzled

G-3-P:

Glyceraldehyde-3-phosphate

GAPD:

Glyceraldehyde 3-phosphate dehydrogenase

GAPDH:

Glyceraldehyde 3-phosphate dehydrogenase

G-CSF:

Granulocyte colony stimulating factor

GFAP:

Glial fibrillary acidic protein

GLK:

Glucokinase

GLP 1:

Glucagon like peptide 1

GLUT 1:

Glucose transporter 1

GM CSF:

Granulocyte-macrophage colony-stimulating factor

GPI:

Glucose 6 phosphate isomerase

GR:

Glutathione reductase

Grx:

Glutaredoxin

GSH:

Glutathione (Reduced)

GSSG:

Glutathione (Oxidized)

GSK 3:

Glycogen synthase kinase 3

HDAC:

Histone deacetylases

HGP:

Hepatic glucose production

HIF:

Hypoxia-inducible factor

HRE:

Hypoxia-responsive elements

Hsp:

Heat shock protein

HXK:

Hexokinase

IDH:

Isocitrate dehydrogenase

IGF 1:

Insulin-like growth factor 1

IL:

Interleukin

JNK:

Jun N-terminal kinase

LAP:

LC3-associated phagocytosis

LC 3:

Microtubule-associated protein 1 A/1B-light chain 3

LDH:

Lactate dehydrogenase

LKB 1:

Liver kinase B1

MBP-1:

c-Myc binding protein 1

MCT 1:

Monocarboxylate transporter 1

ME:

Malic enzyme

MIP 2A:

Macrophage Inflammatory Protein 2

MLOC:

Mitochondrial lactate oxidation complex

mTORC:

Mammalian target of rapamycin

NAC:

N-Acetyl cystine

NAD:

Nicotinamide adenine dinucleotide

NADH:

Nicotinamide adenine dinucleotide (reduced)

NAFLD:

Non-alcoholic fatty liver disease

ND:

Neurodegenerative disease

NGF:

Nerve Growth Factor

NOX:

NADH oxidase

NRF-2:

Nuclear factor erythroid 2- related factor 2

OMM:

Outer mitochondrial membrane

OXPHOS:

Oxidative phosphorylation

PC:

Prostate cancer

PCAF:

p300/CBP associated Factor

PD:

Perkinson’s disease

PDC:

Pyruvate dehydrogenase complex

PDK 1:

Pyruvate dehydrogenase kinase 1

PEP:

Phosphoenolpyruvate

PFK:

Phosphofructokinase

PFKL:

Phosphofructokinase liver type

PGK:

Phosphoglycerate kinase

PHD:

Prolyl Hydroxylase Domain

PIKK:

Phosphatidylinositol-3- kinase

PKM 2:

Pyruvate kinase M2

PPP:

Pentose phosphate pathway

PYK 1:

Pyruvate Kinase

RBC:

Red blood corpuscles

RNA:

Ribonucleic acid

ROS:

Reactive oxygen species

SAICAR:

Succinyl-5-aminoimidazole-4-carboxamide-1-ribose-5’-phosphate

SAM:

S-Adenosyl methionine

SCD 1:

Stearoyl CoA desaturase 1

SDH:

Succinate dehydrogenase

SGLT:

Sodium glucose co-transporter

SOD:

Superoxide dismutase

STAT:

Signal transducer and activator of transcription

STZ:

Streptozotocin

T1DM/T2DM:

Type 1/2 diabetes mellitus

TAZ:

Yes-associated protein 1

TCA:

Tricarboxylic acid cycle

THF:

Tetrahydrofolic acid

TFAM:

Transcription factor A mitochondrial

TPA:

12-O -tetradecanoyl-phorbol-13- acetate

Trx:

Thioredoxin

TXNIP:

Thioredoxin interacting protein

ULK 1:

Unc-51 like autophagy activating kinase

UTR:

Untranslated region

VEGF:

Vascular endothelial growth factor

VHL:

Von-Hippel-Lindau

WNT:

Wingless-related integration site

YAP:

Yes-associated protein 1

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Acknowledgements

We would like to thank the Council of Scientific and Industrial Research [CSIR File no-09/028(1112)/2019-EMR-I] for funding AM’s fellowship.

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  1. Department of Biophysics, Molecular Biology and Bioinformatics, University of Calcutta, Kolkata, India

    Avirup Malla & Runa Sur

  2. Department of Aquaculture Management, Khejuri college, West Bengal, Baratala, India

    Suvroma Gupta

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Conceptualization of the project was done by S.G., R.S. and A.M. A.M. prepared the original draft, which was edited by S.G. and R.S. S.G. and R.S. are corresponding authors of this manuscript. All approve the final version of the submitted manuscript.

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Malla, A., Gupta, S. & Sur, R. Glycolytic enzymes in non-glycolytic web: functional analysis of the key players. Cell Biochem Biophys (2024). https://doi.org/10.1007/s12013-023-01213-5

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