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The intra- and extracellular distribution and relative density of lamellar bodies (LBs) were determined by electron microscopy in synovial biopsies from 20 non-rheumatoid arthritis (RA) patients. LBs were found on the synovial surface, in Lntimal cells, throughout intimal matrix, in blood vessel walls, in endothelial cytoplasm and within vascular lumena. Lamellar profiles were observed in type B synoviocytes within rough cndopLasmic reticulum (RER), in association with the Golgi apparatus, and embedded in electron dense matrix (projection cores) in multivesicular bodies. Exocytotic release of mature LBs into intimal matrix was observed. In type A synoviocytes the outer lamellae of LBs were frequently found in contiguity with the limiting membrane of lysosomes. An investigation of the ultrastructural features of LB formation in cultured type B synoviocytes (from 3 non-RA patients) gave results similar to those obtained in biopsies. These studies provide ultrastructural evidence of synoviocyte activity in secreting and degrading phospholipid lubricant in a sophisticated system whose function and pathological derangements are largely unknown. [ABSTRACT FROM PUBLISHER]

Intracytoplasmic lamellar organelles identical in ultrastructure to surfactant-containing lamellar bodies found in type II pneumocytes, have been demonstrated in other tissues, in synoviocytes and mesothelial cells, in a distribution pattern which reflects the systemic expression of rheumatoid disease. Antibodies raised against surfactant protein A (SP-A), exhibit a ranking of tissue reactivity in area, intensity and density of cells which also parallels the frequency and degree of pathological involvement characteristic of rheumatoid disease, showing in ascending order of immunopositivity, lachrymal and salivary epithelia, pulmonary parenchyma, mesothelium and synoviocytes. Maximal tissue reactivity to anti-SP-A antibodies was found in the synovium of 55 rheumatoid patients exhibiting classical histopathological appearances of RA, in a pattern of immunostaining identical to that obtained with ML30, an antibody to mycobacterial heat shock protein 65kDa which, in turn, cross-reacted with SP-A in dot blot testing. [ABSTRACT FROM PUBLISHER]