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Development of In Situ Zymography to Localize Active Matrix Metalloproteinase-7 (Matrilysin-1)

Ryoichi Nemori, Masayoshi Yamamoto, Fumio Kataoka, Gakuji Hashimoto, Hiroshi Arakatsu, Takayuki Shiomi and Yasunori Okada

Advanced Core Technology Laboratories, Fuji Photo Film Co., Ltd., Kanagawa, Japan (RN,MY,HA) and Department of Pathology, School of Medicine, Keio University, Tokyo, Japan (FK,GH,TS,YO)

Correspondence to: Yasunori Okada, MD, PhD, Department of Pathology, School of Medicine, Keio University, 35 Shinanomachi, Shinjuku-ku, Tokyo 160-0016, Japan. E-mail: okada{at}sc.itc.keio.ac.jp

Matrix metalloproteinase-7 (MMP-7) is upregulated during carcinogenesis and its expression correlates with metastasis of human endometrial and gastrointestinal carcinomas. In the present study, we have developed a new method to localize the activity of MMP-7 within tissues. Polyethylene terephthalate films were uniformly coated with crosslinked carboxymethylated transferrin (CCm-Tf) as a substrate and incubated with frozen tissue sections mounted on the films. CCm-Tf on the films was degraded selectively by MMP-7, but showed little or no susceptibility to MMP-1, -2, -3, -9, or -13; MT1-MMP; MT3-MMP; or ADAMTS4. Although some serine proteinases such as elastase also digested CCm-Tf, CCm-Tf films impregnated with serine proteinase inhibitors prevented the digestion. When frozen sections of human endometrial carcinoma and lung carcinoma tissues were incubated on CCm-Tf films or those treated with proteinase inhibitors, the activity was detected in the carcinoma cell nests, where MMP-7 was immunolocalized. The present in situ zymography using CCm-Tf may be a useful method to analyze the functions of MMP-7 in pathophysiological conditions. (J Histochem Cytochem 53:1227–1234, 2005)

Key Words: matrix metalloproteinase-7 • Matrilysin-1 • in situ zymography • proteolytic activity • tissue localization • carcinoma invasion

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