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1.
J Rheumatol ; 22(1): 16-23, 1995 Jan.
Article in English | MEDLINE | ID: mdl-7535359

ABSTRACT

OBJECTIVE: The lining cell layer of the synovium proliferates strongly in rheumatoid arthritis. It has been suggested that it has a central role in the destruction of cartilage. We have analyzed the structure of the extracellular matrix and the adhesion molecules of normal, osteoarthritic and rheumatoid lining cell layer. METHODS: We localized the alpha v integrin subunit and its 4 putative partner beta subunits in synovial samples by using indirect immunofluorescence. The specimens were also analyzed by confocal microscopy. Indirect immunofluorescence was also used to analyze the ligands of alpha v integrins, namely fibronectin and vitronectin. RESULTS: The alpha v integrin was abundant in the lining cell layer of normal and osteoarthritic synovia, whereas it was not expressed in the proliferating rheumatoid lining cell layers. A similar expression pattern was found for beta 5 subunit, suggesting that it is the major partner for alpha v. However, also some alpha v beta 1 and alpha v beta 3 heterodimers may be present. The confocal microscopy revealed the presence of both alpha v beta 5 positive and negative lining cells. The putative ligands for alpha v integrins, namely fibronectin and vitronectin were found in the lining cell layer of all the synovial specimens. CONCLUSION: In spite of the proliferation of the lining cell layer in rheumatoid inflammation, the extracellular matrix stays very similar to that in normal and osteoarthritic synovium, whereas the pattern of the adhesion receptors is completely altered.


Subject(s)
Arthritis, Rheumatoid/pathology , Integrin beta Chains , Integrins/analysis , Osteoarthritis , Synovial Membrane/chemistry , Aged , Basement Membrane/chemistry , Cell Adhesion Molecules, Neuronal/analysis , Collagen/analysis , Cytokines/immunology , Extracellular Matrix/chemistry , Extracellular Matrix/pathology , Extracellular Matrix Proteins/analysis , Fibronectins/analysis , Fluorescent Antibody Technique , Glycoproteins/analysis , Humans , Hyperplasia/pathology , Integrin alphaV , Laminin/analysis , Middle Aged , Osteoarthritis/pathology , Synovial Membrane/pathology , Tenascin , Vitronectin
2.
J Rheumatol ; 21(12): 2179-83, 1994 Dec.
Article in English | MEDLINE | ID: mdl-7699615

ABSTRACT

OBJECTIVE: To investigate whether adenoviral DNA is present in synovial specimens from patients with rheumatoid arthritis (RA). METHODS: Synovial fluid (SF) cells from 53 patients with early RA (duration less than 1 year) and synovial tissue samples of 20 patients with advanced RA were studied by using polymerase chain reaction for the presence of adenoviral DNA. The controls were 21 patients with other arthropathies. RESULTS: No adenoviral DNA was found in the SF leukocytes or synovial tissue of any of the patients with arthritis. CONCLUSION: These findings do not indicate that adenoviruses play a role in the etiology of RA. However, they do not exclude adenoviruses as an occasional cause of persistent or recurrent inflammatory arthritis.


Subject(s)
Adenoviruses, Human/isolation & purification , Arthritis, Rheumatoid/virology , Capsid Proteins , Capsid/genetics , DNA, Viral/analysis , Synovial Fluid/virology , Synovial Membrane/virology , Adenoviruses, Human/genetics , Adult , Arthritis, Rheumatoid/pathology , Base Sequence , Female , Humans , Male , Middle Aged , Molecular Sequence Data , Polymerase Chain Reaction , Sensitivity and Specificity , Synovial Fluid/cytology
3.
Am J Pathol ; 142(4): 1019-27, 1993 Apr.
Article in English | MEDLINE | ID: mdl-7682757

ABSTRACT

Integrins are heterodimeric cell adhesion receptors. The beta 1 integrin subunit can be in a complex with multiple a subunits and form receptors for collagen, laminin, fibronectin, and vitronectin. We have characterized the distribution of eight integrin subunits in rheumatoid synovium, with special interest in the lining cell layer. The beta 1 integrin subunit was found in abundance in synovial stroma and in lining cells. The only alpha subunit seen constantly in lining cells was alpha 6. In complex with alpha beta subunit, alpha 6 forms a laminin receptor usually seen in epithelial or endothelial cells or in macrophages. The fact that laminin was found in the extracellular matrix around synovial cells suggests the importance of alpha 6 integrin in the adhesion of synovial lining cells. Furthermore, alpha 6 expression was noticeably weaker in strongly proliferative lining cell layers, indicating that the inflammatory process may regulate integrin expression. A potential connection between altered expression of cell adhesion receptors and the pathological behavior of rheumatoid lining cells is suggested.


Subject(s)
Arthritis, Rheumatoid/metabolism , Integrins/metabolism , Synovial Membrane/metabolism , Adolescent , Adult , Arthritis, Rheumatoid/pathology , Child , Child, Preschool , Female , Humans , Hyperplasia , Immunohistochemistry/methods , Integrins/classification , Male , Reference Values , Staining and Labeling , Synovial Membrane/pathology , Tissue Distribution
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