Alterations in a cartilage matrix glycoprotein in canine osteoarthritis

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

A number of biochemical abnormalities have been described in osteoarthritic (OA) cartilage, but little study has been devoted to changes in the noncollagenous, nonproteoglycan proteins of cartilage in this condition. Using a canine model of OA produced by transection of the anterior cruciate ligament of the knee, we have demonstrated that distinct alterations occur in a 550,000-dalton cartilage matrix glycoprotein in OA canine cartilage. This protein is a major protein constituent of normal articular cartilage. Fragments which are immunologically cross-reactive with the 550,000-dalton protein were more abundant in OA cartilage than in normal articular cartilage. Immunofluorescence studies revealed that staining with specific antiserum to the protein was absent in OA cartilage. This was the only noncollagenous, nonproteoglycan protein noted to undergo significant changes in this model of OA.

Original languageEnglish
Pages (from-to)1493-1500
Number of pages8
JournalArthritis and Rheumatism
Volume29
Issue number12
StatePublished - 1986

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Matrilin Proteins
Osteoarthritis
Canidae
Cartilage
Proteins
Articular Cartilage
Anterior Cruciate Ligament
Fluorescent Antibody Technique
Immune Sera
Knee
Staining and Labeling

ASJC Scopus subject areas

  • Immunology
  • Rheumatology

Cite this

Alterations in a cartilage matrix glycoprotein in canine osteoarthritis. / Fife, Rose.

In: Arthritis and Rheumatism, Vol. 29, No. 12, 1986, p. 1493-1500.

Research output: Contribution to journalArticle

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