Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0001511 (Adhesion)
5,955 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This prospective 1-year follow-up investigated the efficacy of temporomandibular joint lysis and lavage in relation to arthroscopic diagnoses. The study comprised 42 patients. Clinical evaluation was performed before surgery and at regular intervals up to 1 year postoperatively. Diagnostic arthroscopy and immediately subsequent lysis and lavage were performed under local anesthesia in all patients. Only unilateral upper compartment arthroscopies were executed. The results were evaluated according to the 1984 criteria of the American Association of Oral and Maxillofacial Surgeons. Osteoarthrosis was diagnosed arthroscopically in 30 joints (71%), 21 of which (70%) had more pronounced changes. Synovitis, mainly of a mild, localized type, was diagnosed in 39 joints (93%). More pronounced synovitis was found arthroscopically in 12 (31%). Adhesions were found in 20 joints (48%) and were significantly correlated with joints displaying osteoarthrosis (P < 0.001). The overall success rate for arthroscopic lysis and lavage was 50% (21/42 joints). The best response to lysis and lavage was in joints with arthroscopic diagnosis of pronounced synovitis (8/12 joints; 67%). All 21 joints regarded as unsuccessful were operated with diskectomy without implants. The success rate at 1-year follow-up was 18 joints (86%).
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PMID:Efficacy of arthroscopic lysis and lavage in patients with chronic locking of the temporomandibular joint. 789 Sep 64

Rheumatoid arthritis (RA) is characterized by marked infiltration of the synovium by T-cells. The mediator of joint inflammation has been shown to be both cellular and soluble and the concept of cross-talk between adhesion molecules and cytokines, and its relevance to inflammation, is emerging. The expression and function of adhesion molecules are tightly regulated via intracellular signaling induced by cytokine or chemokine stimulation, a process which is designated "inside-to-out signaling". Such regulation is particularly important in inflammatory processes in which T-cells migrate from the circulation into the tissue. Adhesion molecules not only function as glue, but also transduce extracellular information into cytoplasmic organelles via the "outside-to-in signal", resulting in cell activation and cytokine production. For instance, the abundant intracellular adhesion molecule ICAM-1 and CD44 on RA synoviocytes not only potentially facilitate the interaction with T-cells or extracellular matrix, but also induce cytokine gene transcription in synovial cells. Thus, the two-directional cross-talk among adhesion molecules and cytokines appears to be significant for the initiation and prolongation of inflammatory processes through T-cell migration into RA synovial tissues and activation of both T-cells and synovial cells in this region. The concept proposed would greatly help in clarifying the pathological processes in rheumatoid synovitis, as well as in discovering new pharmacological approaches to more specifically control synovial inflammation. (c) 2001 Prous Science. All rights reserved.
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PMID:The role of chemokines and adhesion molecules in the pathogenesis of rheumatoid arthritis. 1275 Jul 65

In osteoarthritis (OA), cartilage and bone fragments have been described within the synovial tissue which are surrounded by synovial cells (i.e. detritus synovitis). These cells appear to attach actively to the cartilage and bone fragments. In rheumatoid arthritis (RA), on the other hand, synovial fibroblasts (SF) have also been shown to be localized at sites of invasion into cartilage and bone and to degrade extracellular matrix (ECM) by secreting proteolytic enzymes. One prerequisite for exerting their aggressive properties is the attachment to cartilage and bone ECM. This attachment appears to be mediated by the expression of different adhesion molecules for which corresponding binding sites on ECM components are known. As it has not been addressed to which ECM proteins SF adhere and with which affinity this process takes place, we investigated the adherence of SF from patients with OA and RA to different cartilage and bone matrix proteins. Synovial tissue samples were obtained during synovectomy or arthroplastic surgery and used for isolating and culturing SF. Synovial cells attaching to cartilage/bone fragments were characterized using immunohistochemistry. The adherence of SF to ECM proteins was examined using an adhesion assay with the following proteins coated on 96-well plates: aggrecan (AGG), bone sialoprotein (BSP), cartilage oligomeric matrix protein (COMP), collagen type I, II and VI, proline arginine-rich, end leucine-rich repeat protein (PRELP), osteopontin (OPN) and recombinant chondroadherin (CHAD). Bovine serum albumin was used as negative control. In addition, adhering fibroblasts were photographed using a phase-contrast microscope. As compared with RA-SF, significantly higher numbers of OA-SF adhering to collagen type II, OPN and CHAD could be detected (P < 0.05). In contrast, RA-SF showed increased attachment to collagen type II, OPN and BSP. Adhesion to AGG, COMP and PRELP appeared not to be significantly increased and differed widely among the SF samples, and, apart from one exception (BSP), OA-SF adhered in higher numbers to the matrix proteins than did RA-SF. Using immunohistochemistry, synovial cells attached to cartilage/bone fragments could be shown to predominantly express CD68 (>/=50%). The CD68-negative population was of the fibroblast phenotype (AS02 positive). The study demonstrates that the binding pattern of OA-SF and RA-SF to ECM proteins differs considerably and therefore provides novel insights into the difficult pathophysiology of OA and RA. In general, it appeared that SF adhere primarily to ECM proteins that contain known binding sites for adhesion molecules (e.g. integrins: collagen/integrin alpha(2)beta(1)) and that higher numbers of OA-SF adhered to the cartilage and bone matrix proteins than did RA-SF.
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PMID:Differential adherence of osteoarthritis and rheumatoid arthritis synovial fibroblasts to cartilage and bone matrix proteins and its implication for osteoarthritis pathogenesis. 1554 Oct 45