ArticleClinical & experimental metastasis1996
Sequential activation and production of matrix metalloproteinase-2 during breast cancer progression.
Article in Clinical & experimental metastasis, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 44 citations in OpenAlex.
- Doxorubicin conjugated with a trastuzumab epitope and an MMP-2 sensitive peptide linker for the treatment of HER2-positive breast cancer.Drug delivery · 2018Article
- Antiangiogenic mechanisms and factors in breast cancer treatment.Journal of carcinogenesis · 2016Review
- Leptin utilizes Jun N-terminal kinases to stimulate the invasion of MCF-7 breast cancer cells.Clinical & experimental metastasis · 2009Article
- Expression analysis of carbohydrate antigens in ductal carcinoma in situ of the breast by lectin histochemistry.BMC cancer · 2008Article
- The influence of MMP-14, TIMP-2 and MMP-2 expression on breast cancer prognosis.Breast cancer research : BCR · 2006Article
- Matrix metalloproteinase-2 (MMP-2) is associated with survival in breast carcinoma.British journal of cancer · 2003Article
- Blockage of heregulin expression inhibits tumorigenicity and metastasis of breast cancer.Oncogene · 2003Article
- Angiogenesis, thrombospondin, and ductal carcinoma in situ of the breast.Journal of clinical pathology · 2002Review
- Matrix metalloproteinase biology applied to vitreoretinal disorders.The British journal of ophthalmology · 2000Review
- Expression of gelatinases A and B, stromelysin-3 and matrilysin genes in breast carcinomas: clinico-pathological correlations.Clinical & experimental metastasis · 1998Article
- Assay of matrix metalloproteinases types 1, 2, 3 and 9 in breast cancer.British journal of cancer · 1998Article
- Elevated cyclic AMP suppresses ConA-induced MT1-MMP expression in MDA-MB-231 human breast cancer cells.Clinical & experimental metastasis · 1998Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proteolytic processes are thought to be the critical point in tumor invasion and metastasis, mainly by matrix metalloproteinases (MMPs) and serine proteases. We measured the activity of MMP-2 from 28 normal, 12 benign and 126 breast cancer tissues using gelatin zymography. Inactive MMP-2 (72 kD) was expressed in 53.6% of the normal and 66.6% of the cancer tissues, respectively (P = 0.77), while active MMP-2 (62 kD) was expressed in 28.6% and 73.0%, respectively (P = 0.003). The enzymatic activity of active MMP-2 (62 kD) measured in the gel band area was 4.0 +/- 7.2 mm2 in normal breasts, 7.7 +/- 9.8 mm2 in benign breast diseases, 9.5 +/- 8.5 mm2 in ductal carcinoma in situ (DCIS), and 12.0 +/- 13.7 mm2 in invasive cancers. The MMP-2 activation ratio (62 kD/62 kD + 72 kD) was 0.12 +/- 0.18 in normal tissues, 0.10 +/- 0.20 in benign diseases, 0.61 +/- 0.22 in DCIS, and 0.50 +/- 0.28 in invasive cancers. In conclusion, MMP-2 activation was the main cause of the increased 62 kD MMP-2 activity during the early phase of breast cancer, while production of MMP-2 supplemented the increased 62 kD activity in the late phase. We suggest, therefore, that these differential expressions of MMP-2 activation and production during the different stages of breast cancer progression are potential therapeutic targets for biological or gene therapy under the concept of stage-oriented cancer treatment.
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