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 et al., 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, British journal of rheumatology, 37(3), 1998, pp. 287-291
The monoclonal antibody 5B5 reacts with the beta subunit of proline-4-
hydroxylase, the enzyme which catalyses the formation of 4-hydroxyl pr
oline in collagen and other proteins with collagen-like amino acid seq
uences. This study aims to assess the production and tissue distributi
on of this enzyme in normal and diseased synovia from patients with va
rious joint diseases, on the basis that it is a putative marker of col
lagen-producing cells and, therefore, in this context, of fibroblasts.
Sections from five normal, 10 osteoarthritic (OA) and 26 rheumatoid a
rthritic (RA) synovia were labelled with a mouse monoclonal antibody t
o proline-4-hydroxylase. The enzyme was found to be expressed by a pro
portion of synovial intimal cells and by fibroblasts in the underlying
connective tissue in normal, OA and RA synovia. Labelling was more pr
onounced in OA and RA cases. The intimal cells labelling positively sh
owed type B synoviocyte morphology, which was confirmed by subsequent
double immunolabelling with 5B5 and antibody against type IV collagen
using immunocytochemistry and immunoelectron microscopy.