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 language | English |
|---|---|
| Pages (from-to) | 512-519 |
| Number of pages | 8 |
| Journal | Clinical and Experimental Metastasis |
| Volume | 14 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 1996 Dec 1 |
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All Science Journal Classification (ASJC) codes
- Cancer Research
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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 journal › Article
TY - JOUR
T1 - Sequential activation and production of matrix metalloproteinase-2 during breast cancer progression
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
PY - 1996/12/1
Y1 - 1996/12/1
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.
UR - http://www.scopus.com/inward/record.url?scp=0030472720&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030472720&partnerID=8YFLogxK
U2 - 10.1007/BF00115111
DO - 10.1007/BF00115111
M3 - Article
C2 - 8970581
AN - SCOPUS:0030472720
VL - 14
SP - 512
EP - 519
JO - Clinical and Experimental Metastasis
JF - Clinical and Experimental Metastasis
SN - 0262-0898
IS - 6
ER -