Multiplexed mass spectrometry monitoring of biomarker candidates for osteoarthritis

Fernández-Puente, Patricia; Calamia, V.; González-Rodríguez, L.; Lourido, L.; Camacho-Encina, M.; Oreiro, N.; Ruiz-Romero, Cristina; Blanco, Francisco J.

doi:10.1016/j.jprot.2016.11.012

Cited by 28 publications

(25 citation statements)

References 54 publications

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“…Multiple Reaction Monitoring (MRM) targeted 14 candidate proteins from Fern andez-Puente and colleagues' previous studies 64,65 . MRM is a quantitative proteomic approach, comparing with co-elution of a known isotope-labelled peptide.…”

Section: Proteomicsmentioning

confidence: 99%

Osteoarthritis biomarkers: year in review

Watt

2018

Osteoarthritis and Cartilage

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Discovery, characterisation and qualification of various biomarkers is ongoing; several novel protein and non-protein candidate biomarkers have been reported this year. Biomarkers provide us with an opportunity to better diagnose and stratify the disease, via established panels or new discovery approaches. Improving quality of sampling and testing, and measuring large numbers of markers simultaneously in large cohorts would seem likely to identify new clinically applicable biomarkers, which are still much needed in this disease.

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Section: Proteomicsmentioning

confidence: 99%

Osteoarthritis biomarkers: year in review

Watt

2018

Osteoarthritis and Cartilage

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“…Multiple reaction monitoring (MRM) is a powerful tool for targeted proteomics and is an emerging field of proteomics with high reproducibility across complex samples. To date, several studies have demonstrated the feasibility of using targeted MRM-MS for quantitative proteomic analyses, which could realize highly multiplex, precise, specific and standardized proteomic quantification [ 20 , 21 ]. Also, iTRAQ discovery combined with subsequent MRM conformation has recently been adopted for disease biomarker quantification studies [ 22 , 23 ], but it has rarely been used for the salivary proteomic analysis of childhood caries.…”

Section: Introductionmentioning

confidence: 99%

Comparative salivary proteomics analysis of children with and without dental caries using the iTRAQ/MRM approach

Wang

et al. 2018

J Transl Med

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BackgroundDental caries is a major worldwide oral disease afflicting a large proportion of children. As an important host factor of caries susceptibility, saliva plays a significant role in the occurrence and development of caries. The aim of the present study was to characterize the healthy and cariogenic salivary proteome and determine the changes in salivary protein expression of children with varying degrees of active caries, also to establish salivary proteome profiles with a potential therapeutic use against dental caries.MethodsIn this study, unstimulated saliva samples were collected from 30 children (age 10–12 years) with no dental caries (NDC, n = 10), low dental caries (LDC, n = 10), and high dental caries (HDC, n = 10). Salivary proteins were extracted, reduced, alkylated, trypsin digested and labeled with isobaric tags for relative and absolute quantitation, and then they were analyzed with GO annotation, biological pathway analysis, hierarchical clustering analysis, and protein–protein interaction analysis. Targeted verifications were then performed using multiple reaction monitoring mass spectrometry.ResultsA total of 244 differentially expressed proteins annotated with GO annotation in biological processes, cellular component and molecular function were identified in comparisons among children with varying degrees of active caries. A number of caries-related proteins as well as pathways were identified in this study. As compared with caries-free children, the most significantly enriched pathways involved by the up-regulated proteins in LDC and HDC were the ubiquitin mediated proteolysis pathway and African trypanosomiasis pathway, respectively. Subsequently, we selected 53 target proteins with differential expression in different comparisons, including mucin 7, mucin 5B, histatin 1, cystatin S and cystatin SN, basic salivary proline rich protein 2, for further verification using MRM assays. Protein–protein interaction analysis of these proteins revealed complex protein interaction networks, indicating synergistic action of salivary proteins in caries resistance or cariogenicity.ConclusionsOverall, our results afford new insight into the salivary proteome of children with dental caries. These findings might have bright prospect in future in developing novel biomimetic peptides with preventive and therapeutic benefits for childhood caries.Electronic supplementary materialThe online version of this article (10.1186/s12967-018-1388-8) contains supplementary material, which is available to authorized users.

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“…Together, the biomarker studies have gradually increased our understanding of pathophysiology and underlying mechanisms of disease. Encouraged by these findings, recent studies have focused on the identification of new markers, more specifically addressing early diagnosis, and the development of new targets for disease modifying drugs . Furthermore, biomarkers may also be a means to predict disease progression and optimize individual treatments …”

mentioning

confidence: 99%

“…Encouraged by these findings, recent studies have focused on the identification of new markers, more specifically addressing early diagnosis, and the development of new targets for disease modifying drugs. 5,[11][12][13] Furthermore, biomarkers may also be a means to predict disease progression and optimize individual treatments. 14,15 Abbreviations: ASPN, asporin; AUGN, augurin; Col, collagen; pN Col III, N-propeptide collagen type III; CILP1, cartilage intermediate layer protein 1; CILP2, cartilage intermediate layer protein 2; CHAD, chondroadherin; COMP, cartilage oligomeric matrix protein; CHADL, chondroadherin link protein; CSPG2, versican core protein; COBA2, collagen alpha-2 (XI) chain; DERM, dermatopontin; ECM, extracellular martix; FMOD, fibromodulin; Fx, fracture; FINC, fibronectin; GAGs, glycosaminoglycans; HPLN, hyaluronan and PG link protein; HTRA1, serine protease HTRA1; LC, liquid chromatography; LUM, lumican; MS, mass spectrometry; MRM, multiple reaction monitoring; MATN1, matrilin-1; MATN3, matrilin-3; MIME, mimecan; MGP, matrix Gla protein; OA, osteoarthritis; OMD, osteomodulin; OSTP, osteopontin; PGs, proteoglycans; PGCA, aggrecan core protein; PGS1, biglycan; PGS2, decorin; PRG4, lubricin; PRELP, prolargin; PGBM, basement membrane specific heparin sulfate PG core protein; TSP1, thrombospondin-1; TSP4, thrombospondin-4; SLRPs, small leucine rich repeat proteoglycans; TENA, tenascin-C; TENX, tenascin-X; TGF-b, Transforming growth factor-beta Patrik The aim of this study was to explore candidate proteins in early events of osteoarthritic cartilage which may predict development of OA.…”

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confidence: 99%

Targeted proteomics of hip articular cartilage in OA and fracture patients

Hosseininia

Önnerfjord

Dahlberg

2019

Journal Orthopaedic Research

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Osteoarthritis (OA) is a common chronic disease, causing joint pain and reduced physical function. OA progresses slowly over a period of several years; to avoid an exacerbation of symptoms, it is critical to able to diagnose the disease as early as possible. The identification of disease‐specific biomarkers may enable such an early diagnosis. The aim of this study was to investigate potential biomarkers of cartilage metabolism in OA using a targeted multiplex approach by single reaction monitoring. Intact looking cartilage of femoral heads from patients with OA (n = 9) or femoral neck fractures (n = 12) was examined. Variations and relative quantifications of 35 selected extracellular matrix (ECM) proteins were analyzed using nano‐LC coupled to tandem mass spectrometry. Our study showed statistically significantly increased levels of asporin (ASPN), mimecan (MIME), matrilin‐3 (MATN3), cartilage intermediate layer protein 2 (CILP‐2), collagen VI, collagen II, and collagen III N‐propeptide in OA cartilage compared with non‐OA cartilage. The other proteins in the protein panel did not appear to be different between the two groups. In conclusion, we identified a number of cartilage matrix proteins which may represent early molecular changes in the OA process and may have potential to predict the development of OA. © 2018 Orthopaedic Research Society. Published by Wiley Periodicals, Inc. J Orthop Res

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Multiplexed mass spectrometry monitoring of biomarker candidates for osteoarthritis

Cited by 28 publications

References 54 publications

Osteoarthritis biomarkers: year in review

Osteoarthritis biomarkers: year in review

Comparative salivary proteomics analysis of children with and without dental caries using the iTRAQ/MRM approach

Targeted proteomics of hip articular cartilage in OA and fracture patients

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