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  • Skiöldebrand, EvaSwedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin,Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine,Inst för biomedicin och veterinär folkhälsovetenskap,Department of Biomedical Science and Veterinary Public Health,University of Gothenburg,Sahlgrenska University Hospital (author)

Cartilage oligomeric matrix protein neoepitope in the synovial fluid of horses with acute lameness: A new biomarker for the early stages of osteoarthritis

  • Article/chapterEnglish2017

Publisher, publication year, extent ...

  • 2017-02-28
  • Wiley,2017
  • electronicrdacarrier

Numbers

  • LIBRIS-ID:oai:gup.ub.gu.se/256872
  • https://gup.ub.gu.se/publication/256872URI
  • https://doi.org/10.1111/evj.12666DOI
  • https://res.slu.se/id/publ/83141URI
  • https://lup.lub.lu.se/record/6ae03793-2438-4f1d-b029-577bd1fd1b99URI

Supplementary language notes

  • Language:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • BackgroundClinical tools to diagnose the early changes of osteoarthritis (OA) that occur in the articular cartilage are lacking. ObjectivesWe sought to identify and quantify a novel cartilage oligomeric matrix protein (COMP) neoepitope in the synovial fluid from the joints of healthy horses and those with different stages of OA. Study designIn vitro quantitative proteomics and assay development with application in synovial fluids samples obtained from biobanks of well-characterised horses. MethodsArticular cartilage explants were incubated with or without interleukin-1 for 25 days. Media were analysed via quantitative proteomics. Synovial fluid was obtained from either normal joints (n = 15) or joints causing lameness (n = 17) or with structural OA lesions (n = 7) and analysed for concentrations of the COMP neoepitope using a custom-developed inhibition enzyme-linked immunosorbent assay (ELISA). Explants were immunostained with polyclonal antibodies against COMP and the COMP neoepitopes. ResultsSemitryptic COMP peptides were identified and quantified in cell culture media from cartilage explants. A rabbit polyclonal antibody was raised against the neoepitope of the N-terminal portion of one COMP fragment (sequence SGPTHEGVC). An inhibition ELISA was developed to quantify the COMP neoepitope in synovial fluid. The mean concentration of the COMP neoepitope significantly increased in the synovial fluid from the joints responsible for acute lameness compared with normal joints and the joints of chronically lame horses and in joints with chronic structural OA. Immunolabelling for the COMP neoepitope revealed a pericellular staining in the interleukin-1-stimulated explants. Main limitationsThe ELISA is based on polyclonal antisera rather than a monoclonal antibody. ConclusionsThe increase in the COMP neoepitope in the synovial fluid from horses with acute lameness suggests that this neoepitope has the potential to be a unique candidate biomarker for the early molecular changes in articular cartilage associated with OA.

Subject headings and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Ekman, StinaSwedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Inst för biomedicin och veterinär folkhälsovetenskap,Department of Biomedical Science and Veterinary Public Health(Swepub:slu)47073 (author)
  • Hulten, L. M.Sahlgrenska University Hospital (author)
  • Svala, EmiliaSwedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin,Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine,Inst för biomedicin och veterinär folkhälsovetenskap,Department of Biomedical Science and Veterinary Public Health,University of Gothenburg,Sahlgrenska University Hospital(Swepub:slu)48811 (author)
  • Bjorkman, K.Sahlgrenska University Hospital (author)
  • Lindahl, Anders,1954University of Gothenburg,Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin,Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine,Sahlgrenska University Hospital(Swepub:gu)xlandy (author)
  • Lundqvist, A.Sahlgrenska University Hospital (author)
  • Önnerfjord, P.Lund University,Lunds universitet,Reumatologi och molekylär skelettbiologi,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Molekylär skelettbiologi,Forskargrupper vid Lunds universitet,Rheumatology,Section III,Department of Clinical Sciences, Lund,Faculty of Medicine,Molecular Skeletal Biology,Lund University Research Groups(Swepub:lu)akem-pon (author)
  • Sihlbom, Carina,1973University of Gothenburg,Gothenburg University,Göteborgs universitet,Core Facilities, Proteomics,Core Facilities, Proteomics(Swepub:gu)xsihca (author)
  • Ruetschi, UllaGothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin,Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine,Sahlgrenska University Hospital(Swepub:gu)xrueul (author)
  • Göteborgs universitetInstitutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin (creator_code:org_t)
  • Sveriges lantbruksuniversitet

Related titles

  • In:Equine Veterinary Journal: Wiley49:5, s. 662-6670425-16442042-3306

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