Monoclonal antibodies against human fibroblast collagenase and the design of an enzyme-linked immunosorbent assay to measure total collagenase

Clark, Ian M.; Powell, Liz; Wright, John; Cawston, Tim E.; Hazleman, B. L.

doi:10.1016/s0934-8832(11)80092-2

Cited by 38 publications

(24 citation statements)

References 23 publications

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“…The assay measures proenzyme, active enzyme, and enzyme complexed with tissue inhibitor of metalloproteinases (TIMP). The methods used were similar to those described elsewhere (12,13), although recombinant human MMP-1 is now utilized as a standard in the assay. Samples were initially run in duplicate at a 1:8 dilution in an assay with standards ranging between 0.25 ng/ml and 10 ng/ml (intraassay coefficient of variation [CV] 3.4-17.9%, interassay CV 0.05-15.0%).…”

Section: Methodsmentioning

confidence: 99%

Biomarkers predict radiographic progression in early rheumatoid arthritis and perform well compared with traditional markers

Young-Min¹,

Cawston²,

Marshall³

et al. 2007

Arthritis & Rheumatism

113

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Objective. To evaluate the performance of biochemical and traditional markers in predicting radiographic progression in rheumatoid arthritis (RA).Methods. One hundred thirty-two patients with early RA were treated with nonbiologic therapies for 2 years and studied longitudinally. Genomic DNA was analyzed for presence of the shared epitope. Conclusion. These results indicate that biochemical markers are useful predictors of radiographic progression in RA and that serum MMP-3 levels decrease significantly with MTX therapy. Multivariate models that include MMP-3 and CTX-II perform better than existing traditional markers in predicting radiographic outcome in RA.

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Section: Methodsmentioning

confidence: 99%

Biomarkers predict radiographic progression in early rheumatoid arthritis and perform well compared with traditional markers

Young-Min¹,

Cawston²,

Marshall³

et al. 2007

Arthritis & Rheumatism

113

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“…Collagenase, TIMP, and collagenase-TIMP complex were assayed using double-antibody sandwich ELISAs as previously described (16)(17)(18). The TIMP assay measures free TIMP only, whereas the collagenase assay measures free enzyme (both latent and active), as well as all collagenase-containing complexes except that with a , M .…”

Section: Elisamentioning

confidence: 99%

“…In recent years we have developed specific enzyme-linked immunosorbent assays (ELISAs) to measure the levels of total collagenase, free TIMP, and collagenase-TIMP complex in human cell culture medium and body fluids (16)(17)(18). In the present study we used these ELISAs to accurately measure the amounts of collagenase, TIMP, and collagenase-TIMP complex in SF from patients with either osteoarthritis (OA) or RA.…”

mentioning

confidence: 99%

The measurement of collagenase, tissue inhibitor of metalloproteinases (timp), and collagenase—timp complex in synovial fluids from patients with osteoarthritis and rheumatoid arthritis

Clark

Powell

Ramsey

et al. 1993

Arthritis & Rheumatism

152

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Objective. To compare the levels of collagenase, tissue inhibitor of metalloproteinases (TIMP), and collagenase-TIMP complex in synovial fluid (SF) from patients with rheumatoid arthritis (RA) and patients with osteoarthritis (OA). This study aims to clarify existing data from previously used enzyme or inhibitor activity assays performed following separation by gel filtration, by using a 1-step enzyme-linked immunosorbent assay (ELISA) for each component.Methods. Total collagenase, free TIMP, and collagenase-TIMP complex were measured using a newly developed, specific double-antibody sandwich ELISA.Results. Levels of both collagenase and TIMP were significantly higher in RA patients (collagenase 1,560 f 150 ng/ml [mean f SEMI, TIMP 1,610 f 130 ng/ml; n = 80) than OA patients (collagenase 420 f 90 ng/ml, TIMP 1,050 f 60 ng/ml; n = SO), with the difference being especially striking for collagenase. Sixteen RA fluids had detectable levels of collagenase-TIMP complex, compared with only 3 OA fluids.Conckusion. The level of total collagenase in SF is greater in RA than OA, while levels of free TIMP show more overlap between the 2 diseases; this may simply ~~ --

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“…These methods do not allow for the differentiation of the collagenases involved in the cleavage of these substrates. ELISAs have been developed using specific anticollagenase antibodies allowing the detection of collagenase and tissue inhibitor of metalloproteinase (TIMP)-collagenase complexes (36)(37)(38). However, the presence of enzyme in body fluids and tissues does not necessarily imply activity, as the collagenases are secreted as zymogens, they require activation, and their catalytic potential is determined by the presence of inhibitors such as tissue inhibitor of metalloproteinase and alpha 2 macroglobulin.…”

Section: Introductionmentioning

confidence: 99%

Enhanced cleavage of type II collagen by collagenases in osteoarthritic articular cartilage.

Billinghurst¹,

Dahlberg²,

Ionescu³

et al. 1997

J. Clin. Invest.

911

837

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We demonstrate the direct involvement of increased collagenase activity in the cleavage of type II collagen in osteoarthritic human femoral condylar cartilage by developing and using antibodies reactive to carboxy-terminal (COL2-3/ 4C short ) and amino-terminal (COL2-1/4N1) neoepitopes generated by cleavage of native human type II collagen by collagenase matrix metalloproteinase (MMP)-1 (collagenase-1), MMP-8 (collagenase-2), and MMP-13 (collagenase-3). A secondary cleavage followed the initial cleavage produced by these recombinant collagenases. This generated neoepitope COL2-1/4N2. There was significantly more COL2-3/ 4C short neoepitope in osteoarthritis (OA) compared to adult nonarthritic cartilages as determined by immunoassay of cartilage extracts. A synthetic preferential inhibitor of MMP-13 significantly reduced the unstimulated release in culture of neoepitope COL2-3/4C short from human osteoarthritic cartilage explants. These data suggest that collagenase(s) produced by chondrocytes is (are) involved in the cleavage and denaturation of type II collagen in articular cartilage, that this is increased in OA, and that MMP-13 may play a significant role in this process. ( J. Clin. Invest. 1997. 99:1534-1545.)

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Monoclonal antibodies against human fibroblast collagenase and the design of an enzyme-linked immunosorbent assay to measure total collagenase

Cited by 38 publications

References 23 publications

Biomarkers predict radiographic progression in early rheumatoid arthritis and perform well compared with traditional markers

Biomarkers predict radiographic progression in early rheumatoid arthritis and perform well compared with traditional markers

The measurement of collagenase, tissue inhibitor of metalloproteinases (timp), and collagenase—timp complex in synovial fluids from patients with osteoarthritis and rheumatoid arthritis

Enhanced cleavage of type II collagen by collagenases in osteoarthritic articular cartilage.

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