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Identification of proteins and N-glycosylation sites of knee cartilage in Kashin-Beck Disease compared with osteoarthritis
School of Public Health, Health Science Center, Xi'an Jiaotong University, Xi'an, Shaanxi, People's Republic of China.
School of Public Health, Health Science Center, Xi'an Jiaotong University, Xi'an, Shaanxi, People's Republic of China.
Umeå universitet, Medicinska fakulteten, Institutionen för odontologi.ORCID-id: 0000-0002-1710-7715
School of Public Health, Health Science Center, Xi'an Jiaotong University, Xi'an, Shaanxi, People's Republic of China.
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2022 (Engelska)Ingår i: International Journal of Biological Macromolecules, ISSN 0141-8130, E-ISSN 1879-0003, Vol. 210, s. 128-138Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The aim of this study was to identify crucial proteins and N-glycosylated sites in the pathological mechanism of Kashin-Beck Disease (KBD) compared with osteoarthritis (OA). Nine KBD knee subjects and nine OA knee subjects were selected for the study. Quantitative proteomics and N-glycoproteomics data of KBD and OA were obtained by protein and N-glycoprotein enrichment and LC-MS/MS analysis. Differentially expressed proteins or N-glycosylation sites were examined with a comparative analysis between KBD and OA. Total 2205 proteins were identified in proteomic analysis, of which 375 were significantly different. Among these, 121 proteins were up-regulated and 254 were down-regulated. In N-glycoproteomic analysis, 278 different N-glycosylated sites that were related to 187 N-glycoproteins were identified. Proteins and their N-glycosylated sites are associated with KBD pathological process including ITGB1, LRP1, ANO6, COL1A1, MXRA5, DPP4, and CSPG4. CRLF1 and GLG1 are proposed to associate with both KBD and OA pathological processes. Key pathways in KBD vs. OA proteomic and N-glycoproteomic analysis contained extracellular matrix receptor interaction, focal adhesion, phagosome, protein digestion, and absorption. N-glycosylation may influence the pathological process by affecting the integrity of chondrocytes or cartilage. It regulated the intercellular signal transduction pathway, which contributes to cartilage destruction in KBD.

Ort, förlag, år, upplaga, sidor
Elsevier, 2022. Vol. 210, s. 128-138
Nyckelord [en]
Kashin-Beck disease, N-glycoproteomics, N-glycosylated sites, Osteoarthritis, Proteomics
Nationell ämneskategori
Biokemi och molekylärbiologi Cell- och molekylärbiologi Ortopedi
Forskningsämne
biokemi; reumatologi; ortopedi
Identifikatorer
URN: urn:nbn:se:umu:diva-194606DOI: 10.1016/j.ijbiomac.2022.05.014ISI: 000806361400005PubMedID: 35526762Scopus ID: 2-s2.0-85129751455OAI: oai:DiVA.org:umu-194606DiVA, id: diva2:1657588
Tillgänglig från: 2022-05-11 Skapad: 2022-05-11 Senast uppdaterad: 2023-09-05Bibliografiskt granskad

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Qu, ChengjuanLammi, Mikko

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Qu, ChengjuanLammi, Mikko
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Institutionen för odontologiInstitutionen för integrativ medicinsk biologi (IMB)
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International Journal of Biological Macromolecules
Biokemi och molekylärbiologiCell- och molekylärbiologiOrtopedi

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