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Diet-inducing hypercholesterolemia show decreased O-GlcNAcylation of liver proteins through modulation of AMPK

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Abstract

O-GlcNAcylation, a nutritionally driven, post-translational modification of proteins, is gaining importance because of its health implications. Changes in O-GlcNAcylation are observed in various disease conditions. Changes in O-GlcNAcylation by diet that causes hypercholesterolemia are not critically looked into in the liver. To address it, both in vitro and in vivo approaches were employed. Hypercholesterolemia was induced individually by feeding cholesterol (H)/high-fat (HF) diet. Global O-GlcNAcylation levels and modulation of AMPK activation in both preventive and curative approaches were looked into. Diet-induced hypercholesterolemia resulted in decreased O-GlcNAcylation of liver proteins which was associated with decreased O-linked N-acetylglucosaminyltransferase (OGT) and Glutamine fructose-6-phosphate amidotransferase-1 (GFAT1). Activation of AMPK by metformin in preventive mode restored the O-GlcNAcylation levels; however, metformin treatment of HepG2 cells in curative mode restored O-GlcNAcylation levels in HF but failed to in H condition (at 24 h). Further, maternal faulty diet resulted in decreased O-GlcNAcylation in pup liver despite feeding normal diet till adulthood. A faulty diet modulates global O-GlcNAcylation of liver proteins which is accompanied by decreased AMPK activation which could exacerbate metabolic syndromes through fat accumulation in the liver.

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Abbreviations

AMPK:

AMP-activated protein kinase

ACC:

Acetyl-CoA carboxylase

C:

Control

CC:

Compound C

CH:

Cholesterol–methyl-β-cyclodextrin

CH + M:

Cholesterol–methyl-β-cyclodextrin + metformin

ff BSA:

Fat-free BSA

FAS:

Fatty acid synthase

H:

Hypercholesterolemic

H+M:

Hypercholesterolemic + metformin

GFAT-1:

Glutamine fructose-6-phosphate amidotransferase 1

HF:

High-fat

HF+M:

High Fat + metformin

HBP:

Hexosamine biosynthetic pathway

HMGCoAS1:

3-hydroxy-3-methyl-glutaryl coenzyme A synthase 1

ML:

Mother liver

OGT:

O-Linked N-acetylglucosaminyltransferase

OGA:

O-GlcNAcase

PA:

Palmitic acid

PA+M:

Palmitic acid + metformin

PTM:

Post-translational modifications

SREBP 1:

Sterol regulatory element-binding protein

UDP-GlcNAc:

Uridine diphosphate N-acetylglucosamine

8W:

8 weeks

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Acknowledgements

SJ thanks Indian Council of Medical Research (ICMR) for the Senior Research Fellowship. The authors acknowledge the Director, CSIR-CFTRI, for keen interest.

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Authors and Affiliations

  1. Department of Molecular Nutrition, CSIR-Central Food Technological Research Institute, Mysore, Karnataka, 570020, India

    Sanjana Jagannath, Smitha Honnalagere Mallanna & C. D. Nandini

  2. Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, 201002, India

    Sanjana Jagannath, Smitha Honnalagere Mallanna & C. D. Nandini

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  1. Sanjana Jagannath
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  3. C. D. Nandini
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Contributions

SJ: carried out bench work, analyzed data, and wrote manuscript. SHM: helped with experiments pertaining to animal studies. NCD: conceptualized, interpreted data, and wrote manuscript. The authors declare that all data were generated in-house and that no paper mill was used.

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Correspondence to C. D. Nandini.

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Highlights

•O-GlcNAcylation is a highly context-dependent post-translational modification.

•High-cholesterol and high-fat diet individually resulted in decreased O-GlcNAcylation of liver proteins.

•Modulation of AMPK using pharmacological AMPK activator resulted in the restoration of O-GlcNAcylation levels when given as a preventive dose.

•Maternal hypercholesterolemia resulted in decreased O-GlcNAcylation in liver proteins of offspring in adulthood.

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Jagannath, S., Mallanna, S.H. & Nandini, C.D. Diet-inducing hypercholesterolemia show decreased O-GlcNAcylation of liver proteins through modulation of AMPK. J Physiol Biochem 80, 205–218 (2024). https://doi.org/10.1007/s13105-023-00997-7

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