Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0003864 (arthritis)
 69,039 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Peripheral blood lymphocyte functions were evaluated in 20 patients with active polymyalgia rheumatica (PMR) and/or giant cell arteritis (GCA) by determining the percent of E-rosette-forming cells and by measuring the uptake of tritiated thymidine by peripheral blood lymphocytes after exposure to common infectious antigens and to homogenates of homologous and heterologous artery, muscle, and elastin. Although lymphocytes from patients with PMR and/or GCA were stimulated slightly by artery and muscle homogenates, no differences in lymphocyte responses were found when the results were compared with 22 normal controls and 16 patients with rheumatoid arthritis. The hypothesis that GCA results from a cellular immune reaction to normal or diseased arterial wall antigens is not supported by these studies.
Arthritis Rheum 1979 Jul
PMID:Cellular immunity in polymyalgia rheumatica and giant cell arteritis: lack of response to muscle or artery homogenates. 45 1

One prediction of the protease-antiprotease hypothesis of chronic obstructive pulmonary disease (COPD) pathogenesis is the appearance of elastin-derived degradation products in the plasmas of affected patients that are due to the breakdown of alveolar interstitial elastin by an excess of elastolytic activity in the lung. We previously demonstrated a significant elevation of plasma elastin-derived peptides (EDP) in subjects with COPD in comparison with asymptomatic smokers with normal spirometry or normal nonsmokers. To better determine the selectivity of the assay for EDP as a marker of COPD, we measured plasma EDP levels in different patient populations. These included subjects with COPD, subjects with diseases that may involve accelerated elastolysis (pneumonia, atherosclerotic vascular disease, and inflammatory arthritis), subjects with diseases hypothesized to involve pulmonary inflammation without elastolysis (asthma and acute tracheobronchitis), asymptomatic smokers with normal spirometry, and healthy, nonsmoking subjects. Mean plasma EDP levels in subjects with COPD were elevated above those in all other subjects (p less than 0.01). The prospective analyses of specificity and sensitivity of plasma EDP levels as markers of COPD gave values of 91 and 65%, respectively. Utilizing receiver operating characteristic curve analysis to assess the diagnostic and screening performance of plasma EDP as a test for COPD (perfect test equals an area under the curve of 1.0), the area under the curve was 0.87, which compares favorably with many widely used clinical tests. These data demonstrate that the assay for plasma EDP is a quantitative, easily measured, and highly specific marker for subjects with COPD.
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PMID:Specificity and sensitivity of the assay for elastin-derived peptides in chronic obstructive pulmonary disease. 846 8

Collagens and gelatins were isolated from human post-menopausal uterus, puerperal (post-partum) uterus, rheumatoid-arthritis-nodule and ox tendon. Different means of purifying collagen were studied and a method was devised that enables highly purified collagen to be obtained, even from the uterus. This method involves the use of a number of aqueous and organic extractants as well as digestion with elastase to eliminate elastin. The purity of the collagen preparations was assessed and they were used to study the amino acid composition of collagen. The amino acid compositions of all the collagens studied were similar to those of human bone and tendon collagen, but certain small differences were noted and are discussed. The soluble collagen extracted from some of the tissues was also studied.
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PMID:The purification and amino acid composition of human uterus collagens, rheumatoid-arthritis-nodule collagen and ox tendon collagen. 563 30

The incidence of rice bodies (RB) in synovial effusions has been studied in 36 patients with rheumatoid arthritis (RA) and in 12 patients with seronegative inflammatory arthritis (7 cases of Still's disease, 3 of psoriatic arthritis, and 2 of ankylosing spondylitis). In the RA group 50 joints were aspirated before and after saline lavage with a specially designed wide-bore needle. RB were found in 72% overall of the joints studied in this group, 14% on initial simple aspiration and an additional 58% after lavage. In contrast no rice bodies were found in 31 aspirations with lavage by an identical technique in the 12 patients with seronegative synovitis. The RB in RA synovitis occurred both early and late in the course of the disease and were not related to the severity of clinical or radiological changes. However, removal of rice bodies was accompanied by clinical improvement and reduction of synovitis. Macroscopically RB varied in shape and size, some being so large as to preclude effective removal by needles of the gauge customarily employed for joint aspirations. Microscopically the majority of RB were composed of coarsely reticular material reacting immunologically with antifibrinogen and antifibronectin and containing mononuclear cells. Some showed vacuolation suggestive of fibrinolysis, but many showed organisation like that seen in established connective tissues, with the formation of mature collagen, reticulin, and elastin. These findings are discussed in relation to the origin, development, and significance of rice bodies in rheumatoid synovitis.
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PMID:Frequency of occurrence, mode of development, and significance or rice bodies in rheumatoid joints. 617 92

Detrimental effects of the natural aging process on the human cricoarytenoid joint have been hypothesized as a possible etiology for the voice changes seen in the aging population. Cellular events occurring at the histologic level, such as cricoarytenoid joint erosion or arthritis may lead to alterations in laryngeal structure which ultimately affect its function and performance. Seven normal human larynges of varying ages ranging from 29 to 69 years of age were examined histopathologically for changes in the cricoarytenoid joint. The synovium, joint space, periarticular muscle, and respiratory epithelium were evaluated for the presence of inflammatory changes or edema and degree of vascularity. The location and amount of ossification, elastin, and collagen formation were also noted. There were no appreciable changes noted in the synovium or joint space itself with increasing age. No differences were observed in the degree of elastin or collagen formation. However, there was progressive cricoid and arytenoid ossification and periarticular muscular atrophy and fibrosis. These findings suggest that other laryngeal changes may play a greater role in determining senescent vocal quality rather than changes within the cricoarytenoid joint itself.
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PMID:Histopathologic changes in the aging human cricoarytenoid joint. 818 82

Gelatinase B (matrix metalloproteinase-9) is able to degrade several extracellular matrix proteins, including gelatin, elastin, and collagen types IV, V, XI, and XIV. This enzyme contains a "fibronectin-like" domain which is composed of three tandem copies of a fibronectin type 2 homology unit inserted into its catalytic domain. We have studied the involvement of this domain in the substrate specificity of gelatinase B by expressing a mutant of the enzyme, in Escherichia coli, in which this domain has been deleted. This mutant enzyme retained its ability to cleave the peptide substrate Mca-PLGL(Dpa)AR-NH2, possessing K(m) and kcat values similar to those of the wild-type enzyme. In addition, the NH2-terminal, 14-kDa, inhibitory domain of recombinant tissue inhibitor of metalloproteinase-2 was able to inhibit the mutant and the wild-type enzymes with the same potency. The mutant's gelatinolytic activity was also retained but reduced in comparison to that of the wild-type enzyme. However, contrary to the wild-type enzyme, the mutant was not able to digest or bind fibrillar collagen types V and XI. These data indicate that the fibronectin-like domain of gelatinase B is an important determinant of the enzyme's fibrillar collagen substrate specificity. It allows the enzyme to bind to and cleave collagen types V and XI, events which are thought to be involved in several normal physiological and pathological processes such as metastasis and arthritis.
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PMID:The fibronectin-like domain is required for the type V and XI collagenolytic activity of gelatinase B. 963 94

Collagen, gelatin, elastin, fibronectin, proteoglycans and vitronectin are just a few proteins which form the "mesh" that holds a multicellular organism together. The matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade the extracellular matrix. Over several decades it has been clearly established that MMPs are the key molecules associated with matrix remodeling. The remodeling of this matrix is important for physiological and pathological processes such as pregnancy, wound repair, cancer and arthritis. The identification of new non-matrix MMP substrates involved in inflammation, highlights the diverse role of MMPs. These enzymes can enhance leukocyte invasion and regulate the inflammatory activity of serine proteases, cytokines and chemokines. Interestingly, the MMP family appears to have a "dual personality" in that several MMPs such as MMP-2 and -9 can favour either anti- or pro-inflammatory action, respectively. The extent of this dual functionality of MMPs is yet to be realized. Elucidating these processes may assist in the development of drugs for the treatment of inflammatory diseases such as arthritis, cancer and chronic wounds.
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PMID:The dual personalities of matrix metalloproteinases in inflammation. 1712 95

Rheumatoid arthritis (RA) is a sexually dimorphic, autoimmune inflammatory disorder affecting the joints. Joint disability in RA results primarily from loss of matrix components (collagen and glycosoaminoglycan) in the cartilage and synovium. This study was carried out to understand the effect of physiological levels of testosterone, estrogen, and progesterone on oxidative stress-induced changes in matrix composition in rat synovium in arthritis. Arthritis induction in castrated and ovariectomized rats resulted in enhanced oxidative stress and this was assessed by lipid peroxidation levels and depletion of antioxidants. This, in turn, led to significantly (p < 0.01) increased levels of TNF-alpha and matrix metalloproteinase-2 (MMP-2), subsequently resulting in loss of collagen, elastin, and glycosoaminoglycan (GAG) and disorganization of reticulin as evidenced by biochemical quantitation and also by staining for collagen, reticulin, and elastin. Treatment with physiological doses of dihydrotestosterone (25 mg topically) and estrogen (5 microg/0.1 ml subcutaneously) restored the antioxidant levels significantly (p < 0.05) and reduced the levels of TNF-alpha and MMP-2, with estrogen exhibiting a higher potency. This, in turn, attenuated the damage to reticulin organization as well as the loss of collagen and GAG in the articular tissues. However, elastin loss could not be attenuated by either treatment. Progesterone (2 mg/0.1 ml subcutaneously) was not shown to have any significance in disease modification, and on the contrary, it inhibited the protective effects of estrogen. However, progesterone contributed to increased collagen levels in the tissues.
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PMID:Estrogen and testosterone attenuate extracellular matrix loss in collagen-induced arthritis in rats. 1893 19

Matrix metalloproteinases (MMPs), also known as matrixins, belong to a group of zinc-dependent proteins, which are thought to play a central role in the breakdown of extracellular matrix. Collagen, elastin, gelatin and casein are major components cleaved by MMPs. The breakdown of these components is essential for many physiological processes such as embryonic development, morphogenesis, reproduction, and tissue resorption and remodelling. MMPs also participate in pathological processes such as arthritis, cancer, cardiovascular and neurological diseases. This review summarizes current knowledge regarding these proteins, their participation in physiological and pathophysiological roles, their involvement in activation and inhibition, and their interactions with other metal-binding proteins including metallothioneins.
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PMID:Matrix metalloproteinases. 2084 7

In the present study, we examined the effect of a marine bioactive compound containing high-purity caviar-derived DNA, collagen elastin and protein extracts from sturgeon (LD-1227, Caviarlieri, Laboratoires Dom, Switzerland) on IL-1beta-induced activation and production of TNFalpha and MMP-13 in human osteo-arthritis (OA) chondrocytes and intracellular signaling factors. Human chondrocytes were derived from OA cartilage and stimulated with IL-1beta. Gene expression of TNFalpha, MMP-13, MMP-1 and Col10A1 was measured by quantitative RT-PCR. TNFalpha protein in culture medium was determined using cytokine-specific ELISA. Western immunoblotting was used to analyze the MMP-13 production in the culture medium and the activation of NF-kB. DNA binding activity of NF-kB p65 was determined using a highly sensitive and specific ELISA. MMP-13 activity in the culture medium was assayed by gelatine zymography. LD-1227 significantly decreased IL-1beta-stimulated gene expression and production of TNFalpha, MMP-1, MMP-13 and Col10A1 in human chondrocytes. The inhibitory effect of LD-1227 on the IL-1beta-induced expression of these genes was mediated at least in part via suppression of NF-kB p65. These data show that LD-1227 can inhibit IL-1beta-induced proliferation and inflammatory reactions via inhibited activation of the transcription factor NF-kB pathway in human chondrocytes derived from OA patients. These novel pharmacological actions of LD-1227 on IL-1beta-stimulated human OA chondrocytes provide suggestions that this marine biology compound may inhibit cartilage degradation by suppressing IL-1beta-mediated activation and the catabolic response in human chondrocytes.
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PMID:Beneficial effect of a sturgeon-based bioactive compound on gene expression of tumor necrosis factor-alpha, matrix metalloproteinases and type-10 collagen in human chondrocytes. 2303 53


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