Targeted proteomics of hip articular cartilage in OA and fracture patients
(2019) In Journal of Orthopaedic Research 37(1). p.131-135- Abstract
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... (More)
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.
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- author
- Hosseininia, Shahrzad LU ; Önnerfjord, Patrik LU and Dahlberg, Leif E. LU
- organization
- publishing date
- 2019
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- extracellular matrix, hip osteoarthritis, mass spectrometry, proteomics
- in
- Journal of Orthopaedic Research
- volume
- 37
- issue
- 1
- pages
- 131 - 135
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- pmid:30307059
- scopus:85059556122
- ISSN
- 0736-0266
- DOI
- 10.1002/jor.24158
- language
- English
- LU publication?
- yes
- id
- 33f31536-bcde-44de-8d68-1796e6956fcb
- date added to LUP
- 2019-01-21 13:49:56
- date last changed
- 2024-10-01 14:45:16
@article{33f31536-bcde-44de-8d68-1796e6956fcb, abstract = {{<p>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.</p>}}, author = {{Hosseininia, Shahrzad and Önnerfjord, Patrik and Dahlberg, Leif E.}}, issn = {{0736-0266}}, keywords = {{extracellular matrix; hip osteoarthritis; mass spectrometry; proteomics}}, language = {{eng}}, number = {{1}}, pages = {{131--135}}, publisher = {{John Wiley & Sons Inc.}}, series = {{Journal of Orthopaedic Research}}, title = {{Targeted proteomics of hip articular cartilage in OA and fracture patients}}, url = {{http://dx.doi.org/10.1002/jor.24158}}, doi = {{10.1002/jor.24158}}, volume = {{37}}, year = {{2019}}, }