A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 2 (72-kDa gelatinase/type IV collagenase) using monoclonal antibodies

Fujimoto, Noboru; Mouri, N.; Iwata, Kazushi; Ohuchi, Eiko; Okada, Yasunori; Hayakawa, Taro

doi:10.1016/0009-8981(93)90024-x

Cited by 158 publications

(92 citation statements)

References 27 publications

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“…The relationship between the normal ranges of MMPs and TIMPs and age or sex has not yet been thoroughly investigated (9)(10)(11)(12). Among the MMPs and TIMPs we examined, one published study has shown that serum levels of MMP-1 and TIMP-1 were unrelated to age (19).…”

Section: Discussionmentioning

confidence: 99%

“…Concentrations of MMPs 1, 2, 3, and 9, and TIMPs 1 and 2 in blood and tissue samples were measured by a single-step sandwich EIA system using a solid-phase monoclonal antibody and a horseradish peroxidase-labeled monoclonal antibody as previously described (9)(10)(11)(12)(13). For MMP-9, plasma samples instead of serum samples were used for EIA (12).…”

Section: Methodsmentioning

confidence: 99%

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Significant increases in serum and plasma concentrations of matrix metalloproteinases 3 and 9 in patients with rapidly destructive osteoarthritis of the hip

Masuhara

Nakai

Yamaguchi

et al. 2002

Arthritis & Rheumatism

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Objective. Rapidly destructive osteoarthritis (OA) of the hip is an uncommon subset of OA that affects mainly elderly women. Previous studies indicate that elevated levels of matrix metalloproteinases (MMPs) are produced within the tissue of patients with the condition. In the present study, we sought to determine whether serum and plasma levels of MMPs and tissue inhibitors of metalloproteinases (TIMPs) are also elevated.Methods. Blood samples were obtained from 16 patients with rapidly destructive hip OA and from 20 patients with OA before total hip arthroplasty was performed. Synovial specimens were obtained during surgery. Synovial fibroblasts that had migrated sufficiently from explants were subcultured in vitro for 72 hours after confluency, and harvested supernatants were collected. Blood, tissue samples, and fibroblasts were assayed for MMPs 1, 2, 3, and 9, and TIMPs 1 and 2 by sandwich enzyme immunoassay.Results. In blood samples, the levels of MMP-3 and MMP-9 in the group with rapidly destructive hip OA were significantly higher than the normal range and were also significantly higher than those in the OA group. In tissue samples, the levels of MMP-1, MMP-3, MMP-9, and TIMP-1 in the group with rapidly destructive hip OA were significantly higher than those in the OA group. Conclusion.The results of this study show that serum and plasma levels of MMP-3 and MMP-9 are significantly increased in patients with rapidly destructive hip OA. Significantly large amounts of these MMPs produced in synovial tissues within the hip joint could contribute in part to elevation of blood levels. Detection of increased levels of MMP-3 and MMP-9 in patients with painful, disabling hip OA may be of diagnostic value for rapidly destructive hip OA.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Significant increases in serum and plasma concentrations of matrix metalloproteinases 3 and 9 in patients with rapidly destructive osteoarthritis of the hip

Masuhara

Nakai

Yamaguchi

et al. 2002

Arthritis & Rheumatism

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“…The concentration of serum MMP-2 was measured by a onestep sandwich enzyme immunoassay (EIA) system using murine monoclonal antibodies raised against the purified proMMP-2 and an oligopeptide from residue 17 to 35 of the amino terminal region on the human MMP-2 sequence, as previously described (Fujimoto et al, 1993a). The sensitivity of this EIA system was 2.4 pg per assay (0.24 ng ml-'), and linearity was obtained between 10 and 5000 pg per assay (1.0-500 ng ml-').…”

Section: Methodsmentioning

confidence: 99%

“…The maximum diameter of each bladder tumour was determined endoscopically. The clinicopathological features of the patients are shown in Table 1.The concentration of serum MMP-2 was measured by a onestep sandwich enzyme immunoassay (EIA) system using murine monoclonal antibodies raised against the purified proMMP-2 and an oligopeptide from residue 17 to 35 of the amino terminal region on the human MMP-2 sequence, as previously described (Fujimoto et al, 1993a). The sensitivity of this EIA system was 650…”

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confidence: 99%

Imbalance between serum matrix metalloproteinase-2 and its inhibitor as a predictor of recurrence of urothelial cancer

Gohji

Fujimoto²,

Ohkawa³

et al. 1998

Br J Cancer

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Summary Serum levels of matrix metalloproteinase-2 (MMP-2) and tissue inhibitor of metalloproteinases-2 (TIMP-2) were evaluated as prognostic indicators of the recurrence of urothelial cancer. Sera were obtained from 127 healthy control subjects and 97 urothelial cancer patients who underwent complete resection and were measured for MMP-2 and TIMP-2 using a one-step enzyme immunoassay. The relationship between the serum MMP-2/TIMP-2 ratio and the recurrence of urothelial cancer was examined. The mean serum MMP-2/TIMP-2 ratio in the 31 advanced urothelial cancer patients with recurrence was significantly higher than that in the 22 patients without recurrence (P = 0.0029) and in the 44 superficial bladder cancer patients (P < 0.0001). The 1-and 3-year disease-free survival rates in the patients with high MMP-2/TIMP-2 ratios (50% and 12%) were significantly poorer than those of the patients with normal ratios (82% and 56%) (P=0.0152). Univariate and multivariate analyses of recurrence demonstrated that the serum MMP-2/TIMP-2 ratio is a significant independent indicator of advanced urothelial cancer. Our results indicate that an imbalance between the serum levels of MMP-2 and TIMP-2 could be a new predictor of recurrence in advanced urothelial cancer patients.Keywords: serum; matrix metalloproteinase-2; tissue inhibitor of metalloproteinases-2; urothelial cancer; recurrence Matrix metalloproteinases (MMPs) has been shown to play a role in the degradation of the vascular basement membrane, whose major component is type IV collagen Nakajima et al, 1991). Matrix metalloproteinase-2 (MMP-2, gelatinase A, a 72-kDa type IV collagenase) is produced by both malignant cells and stromal cells such as fibroblasts, macrophages and vascular endothelial cells (Nakajima et al, 1991). Many investigators have demonstrated that human and rodent metastatic malignant cells produce larger amounts of MMP-2 than do non-metastatic cells, both in vitro and in vivo (Liotta et al, 1980;. Tissue inhibitor of metalloproteinases-2 (TIMP-2), an unglycosylated protein of 21-kDa molecular weight, strongly inhibits the biological activity of MMP-2, and was shown to strongly inhibit cancer invasion, metastasis, growth and angiogenesis in some rodent and human tumours (Stetler-Stevenson et al, 1989;DeClerck et al, 1992). Therefore, it is likely that an imbalance in the MMP-2 and TIMP-2 ratio plays an important role in cancer invasion, metastasis and angiogenesis DeClerck et al, 1994). Some investigators have revealed a relationship between the recurrence and the expression of MMP-2 and TIMP-2 in bladder cancer tissues (Davies et al, 1993;Grignon et al, 1996). However, there are no previous reports concerning the relationship between the serum MMP-2/TIMP-2 ratio and the recurrence of human urothelial cancer. In this study, the serum levels of MMP-2 and TIMP-2 were determined in human urothelial cancer patients, and the relationship between the serum MMP-2/TIMP-2 ratio and invasion and metastasis in urothelial cancer was examined. We discuss the diagno...

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“…The intra-and interassays CsV for measuring MMP-2 levels were 5.4% and 8.3%, respectively. 23 The intra-and interassay CsV to evaluate MMP-9 levels were 4.9% and 8.6%, respectively. 24 …”

Section: Assessmentsmentioning

confidence: 97%

Different actions of losartan and ramipril on adipose tissue activity and vascular remodeling biomarkers in hypertensive patients

et al. 2010

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We planned a randomized, double blind clinical trial to evaluate whether an antihypertensive intervention at the proximal or distal level of the renin-angiotensin-aldosterone system could have different effects on a broad range of innovative cardiovascular risk biomarkers. A total of 288 hypertensive Caucasian patients (115 men and 113 women), aged X18 years, were enrolled in this study. They were randomized to take losartan 50 mg per day or ramipril 5 mg per day for 1 month and titrated up to 100 mg per day and 10 mg per day for 13 months, respectively. At baseline, 1, 2 and 14 months after therapy initiation, we evaluated the following parameters: body weight, body mass index (BMI), systolic blood pressure (SBP), diastolic blood pressure (DBP), fasting plasma glucose (FPG), M-value, adiponectin (ADN), resistin (r), retinol binding protein-4 (RBP-4), visfatin, vaspin, high-sensitivity C-reactive protein (Hs-CRP), matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9). No variation of body weight, BMI, FPG or vaspin was obtained with either treatment. We recorded a similar improvement in SBP, DBP and Hs-CRP with both treatments; however, losartan also increased M-value, ADN and visfatin, whereas ramipril did not. Furthermore, losartan decreased r, RBP-4, MMP-2 and MMP-9, whereas ramipril did not have any effect on these parameters. In conclusion, we observed that short-term treatment with losartan improved several metabolic parameters (M-value, ADN, RBP-4, r and visfatin) and decreased vascular remodeling biomarkers (MMP-2 and MMP-9) in hypertensive subjects, whereas ramipril did not.

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A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 2 (72-kDa gelatinase/type IV collagenase) using monoclonal antibodies

Cited by 158 publications

References 27 publications

Significant increases in serum and plasma concentrations of matrix metalloproteinases 3 and 9 in patients with rapidly destructive osteoarthritis of the hip

Significant increases in serum and plasma concentrations of matrix metalloproteinases 3 and 9 in patients with rapidly destructive osteoarthritis of the hip

Imbalance between serum matrix metalloproteinase-2 and its inhibitor as a predictor of recurrence of urothelial cancer

Different actions of losartan and ramipril on adipose tissue activity and vascular remodeling biomarkers in hypertensive patients

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