Topographic localization of a 116,000-dalton protein in cartilage

R. S. Fife, G. L. Hook, K. D. Brandt

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

A disulfide-bonded >400,000-dalton (>400-kD) protein with 116-kD subunits in hyaline cartilage from several species has recently been described. It constitutes 2-4% of the total noncollagenous protein in 4 M guanidinium chloride extracts of normal articular cartilage and accounts for most of the total noncollagen, nonproteoglycan protein synthesized in short-term organ cultures of canine articular cartilage. In the present study, immunofluorensce techniques were used to examine the topographic distribution of the 116-kD subunit protein in normal cartilage. In specimens of normal adult articular cartilage from several species, the protein was located throughout the matrix. More intense staining was observed at the articular surface than in the remainder of the uncalcified cartilage. In contrast, in fetal cartilage, the protein was uniformly distributed throughout the matrix without a marked increase in surface staining. Normal canine menisci and annulus fibrosus also demonstrated moderate fluorescence after incubation with the antiserum to the 116-kD subunit protein. Normal canine nucleus pulposus, synovium, aorta, and monolayer cultures of canine synovial cells exhibited only weak immunofluorescence after incubation with the antiserum. Therefore, the 116-kD subunit protein appears to be a ubiquitous matrix protein in cartilage.

Original languageEnglish (US)
Pages (from-to)127-133
Number of pages7
JournalJournal of Histochemistry and Cytochemistry
Volume33
Issue number2
DOIs
StatePublished - Jan 1 1985

ASJC Scopus subject areas

  • Anatomy
  • Histology

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