Sugar-coated bullets: Unveiling the enigmatic mystery ‘sweet arsenal’ in osteoarthritis
Glycosylation is a crucial post-translational modification process where sugar molecules (glycans) are covalently linked to proteins, lipids, or other biomolecules. In this highly regulated and complex process, a series of enzymes are involved in adding, modifying, or removing sugar residues. This p...
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| Format: | Article |
| Language: | English |
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Elsevier
2024-03-01
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| Series: | Heliyon |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2405844024036557 |
| _version_ | 1797224211810353152 |
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| author | Hong-zhi Liu Xin-qiu Song Hongmei Zhang |
| author_facet | Hong-zhi Liu Xin-qiu Song Hongmei Zhang |
| author_sort | Hong-zhi Liu |
| collection | DOAJ |
| description | Glycosylation is a crucial post-translational modification process where sugar molecules (glycans) are covalently linked to proteins, lipids, or other biomolecules. In this highly regulated and complex process, a series of enzymes are involved in adding, modifying, or removing sugar residues. This process plays a pivotal role in various biological functions, influencing the structure, stability, and functionality of the modified molecules. Glycosylation is essential in numerous biological processes, including cell adhesion, signal transduction, immune response, and biomolecular recognition. Dysregulation of glycosylation is associated with various diseases. Glycation, a post-translational modification characterized by the non-enzymatic attachment of sugar molecules to proteins, has also emerged as a crucial factor in various diseases. This review comprehensively explores the multifaceted role of glycation in disease pathogenesis, with a specific focus on its implications in osteoarthritis (OA). Glycosylation and glycation alterations wield a profound influence on OA pathogenesis, intertwining with disease onset and progression. Diverse studies underscore the multifaceted role of aberrant glycosylation in OA, particularly emphasizing its intricate relationship with joint tissue degradation and inflammatory cascades. Distinct glycosylation patterns, including N-glycans and O-glycans, showcase correlations with inflammatory cytokines, matrix metalloproteinases, and cellular senescence pathways, amplifying the degenerative processes within cartilage. Furthermore, the impact of advanced glycation end-products (AGEs) formation in OA pathophysiology unveils critical insights into glycosylation-driven chondrocyte behavior and extracellular matrix remodeling. These findings illuminate potential therapeutic targets and diagnostic markers, signaling a promising avenue for targeted interventions in OA management. In this comprehensive review, we aim to thoroughly examine the significant impact of glycosylation or AGEs in OA and explore its varied effects on other related conditions, such as liver-related diseases, immune system disorders, and cancers, among others. By emphasizing glycosylation's role beyond OA and its implications in other diseases, we uncover insights that extend beyond the immediate focus on OA, potentially revealing novel perspectives for diagnosing and treating OA. |
| first_indexed | 2024-04-24T13:49:31Z |
| format | Article |
| id | doaj.art-9754c5db6ae44c079a4dbaf8d2aa0950 |
| institution | Directory Open Access Journal |
| issn | 2405-8440 |
| language | English |
| last_indexed | 2024-04-24T13:49:31Z |
| publishDate | 2024-03-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Heliyon |
| spelling | doaj.art-9754c5db6ae44c079a4dbaf8d2aa09502024-04-04T05:05:18ZengElsevierHeliyon2405-84402024-03-01106e27624Sugar-coated bullets: Unveiling the enigmatic mystery ‘sweet arsenal’ in osteoarthritisHong-zhi Liu0Xin-qiu Song1Hongmei Zhang2Department of Orthopaedics, Wangjing Hospital, China Academy of Chinese Medical Sciences, Beijing, ChinaThe Third Affiliated Hospital of Sun Yat-sen University, Guangzhou, 510630, ChinaDepartment of Orthopaedics, Wangjing Hospital, China Academy of Chinese Medical Sciences, Beijing, China; Corresponding author.Glycosylation is a crucial post-translational modification process where sugar molecules (glycans) are covalently linked to proteins, lipids, or other biomolecules. In this highly regulated and complex process, a series of enzymes are involved in adding, modifying, or removing sugar residues. This process plays a pivotal role in various biological functions, influencing the structure, stability, and functionality of the modified molecules. Glycosylation is essential in numerous biological processes, including cell adhesion, signal transduction, immune response, and biomolecular recognition. Dysregulation of glycosylation is associated with various diseases. Glycation, a post-translational modification characterized by the non-enzymatic attachment of sugar molecules to proteins, has also emerged as a crucial factor in various diseases. This review comprehensively explores the multifaceted role of glycation in disease pathogenesis, with a specific focus on its implications in osteoarthritis (OA). Glycosylation and glycation alterations wield a profound influence on OA pathogenesis, intertwining with disease onset and progression. Diverse studies underscore the multifaceted role of aberrant glycosylation in OA, particularly emphasizing its intricate relationship with joint tissue degradation and inflammatory cascades. Distinct glycosylation patterns, including N-glycans and O-glycans, showcase correlations with inflammatory cytokines, matrix metalloproteinases, and cellular senescence pathways, amplifying the degenerative processes within cartilage. Furthermore, the impact of advanced glycation end-products (AGEs) formation in OA pathophysiology unveils critical insights into glycosylation-driven chondrocyte behavior and extracellular matrix remodeling. These findings illuminate potential therapeutic targets and diagnostic markers, signaling a promising avenue for targeted interventions in OA management. In this comprehensive review, we aim to thoroughly examine the significant impact of glycosylation or AGEs in OA and explore its varied effects on other related conditions, such as liver-related diseases, immune system disorders, and cancers, among others. By emphasizing glycosylation's role beyond OA and its implications in other diseases, we uncover insights that extend beyond the immediate focus on OA, potentially revealing novel perspectives for diagnosing and treating OA.http://www.sciencedirect.com/science/article/pii/S2405844024036557GlycosylationGlycationOsteoarthritisProtein modificationDisease pathogenesis |
| spellingShingle | Hong-zhi Liu Xin-qiu Song Hongmei Zhang Sugar-coated bullets: Unveiling the enigmatic mystery ‘sweet arsenal’ in osteoarthritis Heliyon Glycosylation Glycation Osteoarthritis Protein modification Disease pathogenesis |
| title | Sugar-coated bullets: Unveiling the enigmatic mystery ‘sweet arsenal’ in osteoarthritis |
| title_full | Sugar-coated bullets: Unveiling the enigmatic mystery ‘sweet arsenal’ in osteoarthritis |
| title_fullStr | Sugar-coated bullets: Unveiling the enigmatic mystery ‘sweet arsenal’ in osteoarthritis |
| title_full_unstemmed | Sugar-coated bullets: Unveiling the enigmatic mystery ‘sweet arsenal’ in osteoarthritis |
| title_short | Sugar-coated bullets: Unveiling the enigmatic mystery ‘sweet arsenal’ in osteoarthritis |
| title_sort | sugar coated bullets unveiling the enigmatic mystery sweet arsenal in osteoarthritis |
| topic | Glycosylation Glycation Osteoarthritis Protein modification Disease pathogenesis |
| url | http://www.sciencedirect.com/science/article/pii/S2405844024036557 |
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