Expression of cartilage oligomeric matrix protein by human synovium

Paul E. Di Cesare, Cathy S. Carlson, Elliot S. Stollerman, Frank S. Chen, Michael Leslie, Roberto Perris

Research output: Contribution to journalArticlepeer-review

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Abstract

Human synovium was analyzed for the possible expression of cartilage oligomeric matrix protein (COMP). Immunostaining with polyclonal antiserum to COMP demonstrated positive staining within the synovial cells and immediately subjacent connective tissue, with less intense staining in the deeper connective tissue. Western blot analysis using either polyclonal or monodonal antibodies to human COMP confirmed the presence of COMP by immunoreactive bands with the same molecular mass (approximately 110 kDa) as purified articular cartilage COMP. PCR using oligonucleotides that span human COMP exons 7-13 revealed identical amplification products from cDNA prepared from either human chondrocytes or synovium. Northern blot analysis using a biotinylated-probe to human COMP, spanning exons 12-13, also reveal an identical hybridization product to either human chondrocyte or synovium total RNA. Human synovium should be considered as a potential tissue source of COMP in any investigation of biological markers of cartilage metabolism.

Original languageEnglish (US)
Pages (from-to)249-252
Number of pages4
JournalFEBS Letters
Volume412
Issue number1
DOIs
StatePublished - Jul 21 1997

Bibliographical note

Funding Information:
This study was supported by a career development award from the Orthopaedic Research and Education Foundation (P.E.D.); grants from the New York Chapter of the Arthritis Foundation, Anne and Harry J. Reicher Foundation, and Grant # RR08562 (C.S.C) from the National Center for Research Resources of the N.I.H. We wish to thank Hermina Tulli for technical assistance.

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