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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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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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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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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DOI: https://doi.org/10.1007/s11033-022-07334-z