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The role of protein glycosylation in muscle diseases

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Abstract

Introduction

As a post-translational modification, glycosylation plays vital role in regulating the folding and function of proteins necessary for many biological processes. Unlike glycation, glycosylation is an enzymatic process; glycosyltransferases transfer sugars to proteins, forming glycosidic bonds with amino acid residues on proteins. Changes that interfere with the enzymatic reaction and result in abnormal glycosylation can spatio-temporally affect the balance of glycosylation, leading to disease states. Muscle diseases have been associated with dysfunctional protein glycosylation, and many studies have focused on the pathophysiology underlying this association. This review aims to summarize the research progress on protein glycosylation in the pathogenesis of muscle diseases and provides new insight into the muscle research field.

Methods

Literatures were reviewed comparatively and data were organized to find information about protein glycosylation and its role in muscle disease.

Results

Protein glycosylation modification is closely related to the occurrence of muscle diseases. α-DG is a key protein in the study of inherited muscle diseases and has a wide range of glycosylation, including O-linked glycosylation and N-linked glycosylation. Besides, O-GlcNAc glycosylation is an important mechanism of protein glycosylation, helping maintaining the structure and function of skeletal muscle and participating in multiple biological processes. Protein glycosylation is also connected to muscle disease and neurodegenerative diseases, especially Alzheimer’s disease.

Conclusions

Taken together, better understanding of protein glycosylation and its implication in muscle disease would help provide new perspectives in the prevention and treatment measures for human muscle diseases.

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Data Availability Statement

Data sharing is not applicable to this article, as no new data were created or analyzed in this study.

Abbreviations

AGP:

arabingalactose protein

p75NTR:

human neurotrophin receptor P75

PMD:

progressive muscular dystrophy

CMD:

congenital muscular dystrophy

FCMD:

Fukuyama congenital muscular dystrophy

MDC1C:

congenital muscular dystrophy type 1C

MDC1D:

congenital muscular dystrophy type 1D

FKRP:

Fukutin-related protein

LARGE1:

like-acetylglucosaminyltransferase

LGMD2I:

limb girdle muscular dystrophy Type 2I

GC:

Golgi complex

POMT1:

O-mannosyltransferase 1

DG:

dystroglycan

MD:

muscular dystrophy

AAV9:

adeno-associated virus serotype 9

RPTPζ:

receptor protein-tyrosine phosphatase ζ

CMS:

congenital myasthenic syndrome

GFPT1:

glutamine fructose-6-phosphate transaminase

DPAGT1:

dolichyl-phosphate (UDP-N-acetylglucosamine

ALG2:

alpha-1,3-mannosyl ransferase

ALG14:

UDP-N-acetylglucosaminyltransferase subunit

GNE:

UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase

DMRV:

distal myopathy with rimmed vacuoles

hIBM2:

hereditary inclusion body myopathy

RV:

rimmed vacuoles

DMD:

Duchenne muscular dystrophy

OGT:

O-GlcNAc transferase

OGA:

O-GlcNAcase

HRT:

hormone replacement therapy

SCs:

satellite cells

s-IBM:

sporadic inclusion-body myositis

MHC:

myosin heavy chain

IIM:

idiopathic inflammatory myopathies

LEMS:

Lambert-Eaton myasthenic syndrome

cGvHD:

chronic graft-versus-host disease

PM:

polymyositis

CCIM:

citical illness myopathy

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Acknowledgements

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Funding

This work was supported by the Natural Science Foundation of China (82072106, 32071517), the Natural Science Basic Research Plan in Shaanxi Province of China (2020JM-100), and the Shaanxi Provincial Key R&D Program (2018KWZ-10).

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  1. Lab for Bone Metabolism, Xi’an Key Laboratory of Special Medicine and Health Engineering, Key Lab for Space Biosciences and Biotechnology, Research Center for Special Medicine and Health Systems Engineering, NPU-UAB Joint Laboratory for Bone Metabolism, School of Life Sciences, Northwestern Polytechnical University, 710072, Xi’an, Shaanxi, China

    Kai Dang, Shanfeng Jiang, Yuan Gao & Airong Qian

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  1. Kai Dang
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  2. Shanfeng Jiang
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  4. Airong Qian
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KD designed the review and drafted the manuscript. KD, SFJ, and YG conducted the research. ARQ conceived the study, participated in its design and coordination, and helped in drafting the manuscript.

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Correspondence to Airong Qian.

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Dang, K., Jiang, S., Gao, Y. et al. The role of protein glycosylation in muscle diseases. Mol Biol Rep 49, 8037–8049 (2022). https://doi.org/10.1007/s11033-022-07334-z

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