Sequential activation and production of matrix metalloproteinase-2 during breast cancer progression

Kyong Sik Lee, SunYoung Rha, Sea Joong Kim, Joo Hang Kim, Jae Kyung Roh, Byung Soo Kim, Hyuncheol Chung

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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 (72kD) 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.

Original languageEnglish
Pages (from-to)512-519
Number of pages8
JournalClinical and Experimental Metastasis
Volume14
Issue number6
DOIs
Publication statusPublished - 1996 Dec 1

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Matrix Metalloproteinase 2
Breast Neoplasms
Carcinoma, Intraductal, Noninfiltrating
Neoplasms
Breast Diseases
Biological Therapy
Serine Proteases
Gelatin
Matrix Metalloproteinases
Genetic Therapy
Breast
Gels
Neoplasm Metastasis
Therapeutics

All Science Journal Classification (ASJC) codes

  • Cancer Research

Cite this

Lee, Kyong Sik ; Rha, SunYoung ; Kim, Sea Joong ; Kim, Joo Hang ; Roh, Jae Kyung ; Kim, Byung Soo ; Chung, Hyuncheol. / Sequential activation and production of matrix metalloproteinase-2 during breast cancer progression. In: Clinical and Experimental Metastasis. 1996 ; Vol. 14, No. 6. pp. 512-519.
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title = "Sequential activation and production of matrix metalloproteinase-2 during breast cancer progression",
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 (72kD) 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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Sequential activation and production of matrix metalloproteinase-2 during breast cancer progression. / Lee, Kyong Sik; Rha, SunYoung; Kim, Sea Joong; Kim, Joo Hang; Roh, Jae Kyung; Kim, Byung Soo; Chung, Hyuncheol.

In: Clinical and Experimental Metastasis, Vol. 14, No. 6, 01.12.1996, p. 512-519.

Research output: Contribution to journalArticle

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AU - Lee, Kyong Sik

AU - Rha, SunYoung

AU - Kim, Sea Joong

AU - Kim, Joo Hang

AU - Roh, Jae Kyung

AU - Kim, Byung Soo

AU - Chung, Hyuncheol

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N2 - 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 (72kD) 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.

AB - 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 (72kD) 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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