Interaction of polymorphonuclear leukocytes with immune complexes trapped in rheumatoid articular cartilage

Ugai, Kazuhiro; Ishikawa, Hitoshi; Hirohata, Kazushi; Shirane, Hirofumi

doi:10.1002/art.1780261204

Cited by 70 publications

(19 citation statements)

References 13 publications

(5 reference statements)

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“…The observations that treatment of cartilage with supernatants obtained from activated neutrophils increases synovial fibroblast adherence and that the enhanced adherence is inhibited when the supernatant is treated with EGTA and DFP suggest that neutrophil proteases are at least in part responsible for the observed enhancement of fibroblast adherence. These results are consistent with findings of previous studies demonstrating that when neutrophils are exposed to cartilage from patients with RA, there is degradation of subjacent cartilage (18,19) and that neutrophils in synovial fluid interacting with surface-adherent IgG can degrade cartilage (20). Immunohistologic studies demonstrating neutrophil proteases on the surface of rheumatoid articular cartilage (2 1) provide further evidence that this process may be operative in vivo.…”

Section: Isupporting

confidence: 93%

Rheumatoid synovial fibroblast adhesion to human articular cartilage

McCurdy¹,

Chatham

Blackburn

1995

Arthritis & Rheumatism

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Objective. To determine if preexposure of human articular cartilage to activated neutrophils alters rheumatoid synovial fibroblast adhesion to human articular cartilage.Methods. Human articular cartilage was exposed to either activated neutrophils, interleukin-1, or supernatants obtained from activated neutrophils that had been treated with different protease inhibitors. Radiolabeled rheumatoid synovial fibroblasts were then incubated with the cartilage and the number of counts associated with the cartilage was determined.Results. Pretreatment of human articular cartilage with either activated neutrophils or supernatants obtained from activated neutrophils enhanced subsequent rheumatoid synovial fibroblast adhesion. In contrast, interleukin-1 treatment of cartilage did not alter the adhesion of synovial fibroblasts. The enhanced adhesion could be attenuated by pretreatment of the neutrophil supernatants with either diisopropylfluorophosphonate or EGTA and almost completely abolished by using both inhibitors.Conclusion. This study demonstrates that adhesion of rheumatoid synovial fibroblasts to human articular cartilage can be enhanced by exposing the cartilage to proteases released by neutrophils. These results suggest that neutrophil products may play a role in enhancing adhesion of rheumatoid synovium to cartilage in vivo. Rheumatoid arthritis (RA) is characterized by the growth of synovium over the articular surface with attendant degradation of the subjacent cartilage. In histologic studies of rheumatoid joints, degradation of the articular surface occurs primarily at sites of synovial attachment to the articular surface. Previous work has demonstrated that adherence of synovium to cartilage varies depending on the state of the articular cartilage surface.The surface of articular cartilage differs from the subjacent layers of cartilage (1-5). An amorphous layer over the surface of normal articular cartilage called the lamina splendens, primarily comprising synovial fluid-derived macromolecules and highly organized collagen fibrils, has been described (1,6,7). Enzymatic degradation of lamina splendens constituents may alter the adhesive properties of the articular surface because rheumatoid synovium adheres more readily to articular cartilage treated with hyaluronidase than to intact articular cartilage (8). Electron microscopic studies indicate that treatment of articular cartilage with proteases also results in structural alteration of the cartilage surface (2). Immunohistologic studies have shown that antibodies with specificity for types V, VI, and IX collagen, but not for type I1 collagen, react with the surface of intact articular cartilage (4). In contrast, when the surface of bovine articular cartilage is treated with proteases, binding of antibodies to type I1 collagen is significantly enhanced (5). Conceivably, exposure of new epitopes could account for enhanced synovial attachment to articular cartilage.In cartilage from patients with RA, there are surface changes in areas that appear to be free of...

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Section: Isupporting

confidence: 93%

Rheumatoid synovial fibroblast adhesion to human articular cartilage

McCurdy¹,

Chatham

Blackburn

1995

Arthritis & Rheumatism

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“…RA pannus, the site of characteristic periarticular erosions, contains relatively few neutrophils, but these cells have been identified at the cartilage-pannus junction (30)(31)(32)(33). Immune complexes, including rheumatoid factor and antibodies to type II collagen, are embedded in the superficial layers of RA cartilage (34)(35)(36)(37). Such complexes may effectively act as cartilage opsonins (36), allowing neutrophils to adhere and discharge their contents directly against cartilage in a process termed "frustrated phagocytosis" (29).…”

Section: Discussionmentioning

confidence: 99%

“…Immune complexes, including rheumatoid factor and antibodies to type II collagen, are embedded in the superficial layers of RA cartilage (34)(35)(36)(37). Such complexes may effectively act as cartilage opsonins (36), allowing neutrophils to adhere and discharge their contents directly against cartilage in a process termed "frustrated phagocytosis" (29). Granulocyte contents with degradative potential include matrix metalloproteinase 1 (MMP-1; collagenase), which is released from active neutrophils in a latent form (38,39) that is readily activated by cathepsin G (40,41), and HOCl, which is generated by released myeloperoxidase and H 2 O 2 (41)(42)(43).…”

Section: Discussionmentioning

confidence: 99%

Reduction of chemokine levels and leukocyte traffic to joints by tumor necrosis factor α blockade in patients with rheumatoid arthritis

Taylor

Peters

Paleolog

et al. 2000

Arthritis & Rheumatism

366

194

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Objective. To verify the hypothesis that in rheu-matoid arthritis (RA), tumor necrosis factor (TNF) plays a critical role in regulating leukocyte trafficking and chemokine levels. Methods. Ten patients with longstanding RA received a single 10 mg/kg infusion of anti-TNF mono-clonal antibody (cA2). The articular localization of autologous granulocytes, separated in vitro and labeled with 111 In, was studied by analysis of gamma-camera images both before and 2 weeks after treatment. At the same sequential time points, synovial biopsy samples were assessed for infiltrating CD3 T cells, CD22 B cells, and CD68 macrophages. Synovial tissue expression of the chemokines interleukin-8 (IL-8), monocyte chemotactic protein 1 (MCP-1), macrophage inflamma-tory protein 1 (MIP-1), MIP-1, Gro, and RANTES was also determined. Serum IL-8 and MCP-1 concentrations were measured by enzyme-linked immunosor-bent assay. Results. Anti-TNF therapy in RA significantly reduced 111 In-labeled granulocyte migration into affected joints. There was a simultaneous and significant reduction in the numbers of infiltrating synovial CD3 T cells, CD22 B cells, and CD68 macrophages and in the expression of IL-8 and MCP-1, with a trend toward a reduction in serum concentrations of these chemokines. Conclusion. TNF blockade reduces synovial expression of the chemokines IL-8 and MCP-1 and diminishes inflammatory cell migration into RA joints.

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“…This collagen degradation may be caused by proteolytic enzymes originating from the synovial fluid which are capable of degrading collagen. Obvious candidates are the collagen-degrading proteases, elastase and cathepsin G (40, 42), which can be released by polymorphonuclear leukocytes upon attachment to articular cartilage which results in the degradation of the more superficial articular cartilage (43,44). In one specimen (K.E.…”

Section: Discussionmentioning

confidence: 99%

Immunohistochemical detection and immunochemical analysis of type II collagen degradation in human normal, rheumatoid, and osteoarthritic articular cartilages and in explants of bovine articular cartilage cultured with interleukin 1.

Dodge¹,

Poole²

1989

J. Clin. Invest.

276

153

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Articular cartilage destruction and loss of function in arthritic diseases involves proteolytic degradation of the connective tissue matrix. We have investigated the degradation of cartilage collagen by developing immunochemical methods that permit the identification and analysis of type II collagen degradation in situ. Previously, a technique to specifically identify type II collagen degradation in situ in articular cartilage did not exist. These methods utilize a polyclonal antiserum (R181) that specifically reacts with unwound a-chains and CNBr-derived peptides, al(II)CB11 and al(II)CB8, of human and bovine type II collagens. The experimental approach is based on the fact that when fibrillar collagens are cleaved the helical collagen molecule unwinds, exposing hidden epitopes. Here we demonstrate the use of R181 in studying type II collagen degradation in bovine articular cartilage that has been cultured with or without IL-1 and in human normal, rheumatoid, and osteoarthritic articular cartilages. Compared to cartilages either freshly isolated or cultured without IL-1, bovine cartilage cultured with IL-1 for 3-5 d showed an increase in both pericellular and intercellular immunohistochemical staining. Extracts of these cartilages contained type II collagen a chains that were increased in amount after culture with IL-1 for 11 d. In addition, culture with IL-1 resulted in the appearance of a chain fragments of lower molecular weight. All human arthritic tissues examined showed areas of pronounced pericellular and territorial staining for collagen degradation as compared with nondiseased tissues, indicating that chondrocytes are responsible in part for this degradation as compared with nondiseased tissues. In most cases rheumatoid cartilage was stained most intensely at the articular surface and in the deep and midzones, whereas osteoarthritic cartilage usually stained more in the superficial and mid-zones, but less intensely. Distinct patterns of sites of collagen degradation reflect differences in collagen destruction in these diseases, suggesting possible different sources of chondrocyte activation. These experiments demonstrate the application of immunological methods to detect collagen degradation and demonstrate an increase of collagen degradation in human arthritides and in IL-1-treated viable bovine cartilage.

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Interaction of polymorphonuclear leukocytes with immune complexes trapped in rheumatoid articular cartilage

Cited by 70 publications

References 13 publications

Rheumatoid synovial fibroblast adhesion to human articular cartilage

Rheumatoid synovial fibroblast adhesion to human articular cartilage

Reduction of chemokine levels and leukocyte traffic to joints by tumor necrosis factor α blockade in patients with rheumatoid arthritis

Immunohistochemical detection and immunochemical analysis of type II collagen degradation in human normal, rheumatoid, and osteoarthritic articular cartilages and in explants of bovine articular cartilage cultured with interleukin 1.

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