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The British Journal of Rheumatology, Vol 37, 287-291, Copyright © 1998 by British Society for Rheumatology

ORIGINAL PAPERS

An immunocytochemical study of the distribution of proline-4- hydroxylase in normal, osteoarthritic and rheumatoid arthritic synovium at both the light and electron microscopic level

SC Smith, VA Folefac, DK Osei and PA Revell
Department of Histopathology, Royal Free Hospital and School of Medicine, London.

The monoclonal antibody 5B5 reacts with the beta subunit of proline-4- hydroxylase, the enzyme which catalyses the formation of 4-hydroxyl proline in collagen and other proteins with collagen-like amino acid sequences. This study aims to assess the production and tissue distribution of this enzyme in normal and diseased synovia from patients with various joint diseases, on the basis that it is a putative marker of collagen-producing cells and, therefore, in this context, of fibroblasts. Sections from five normal, 10 osteoarthritic (OA) and 26 rheumatoid arthritic (RA) synovia were labelled with a mouse monoclonal antibody to proline-4-hydroxylase. The enzyme was found to be expressed by a proportion of synovial intimal cells and by fibroblasts in the underlying connective tissue in normal, OA and RA synovia. Labelling was more pronounced in OA and RA cases. The intimal cells labelling positively showed type B synoviocyte morphology, which was confirmed by subsequent double immunolabelling with 5B5 and antibody against type IV collagen using immunocytochemistry and immunoelectron microscopy.
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