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Activation of matrix metalloproteinase‐2 in human breast cancer cells overexpressing cyclooxygenase‐1 or ‐2
Author(s) -
Takahashi Yoshitaka,
Kawahara Futoshi,
Noguchi Masakuni,
Miwa Koichi,
Sato Hiroshi,
Seiki Motoharu,
Inoue Hiroyasu,
Tanabe Tadashi,
Yoshimoto Tanihiro
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01328-9
Subject(s) - cyclooxygenase , matrix metalloproteinase , transfection , cell culture , metalloproteinase , chemistry , cancer cell , microbiology and biotechnology , blot , matrix metalloproteinase inhibitor , cancer research , cancer , biology , biochemistry , medicine , enzyme , gene , genetics
Human breast cancer cell line Hs578T was stably transfected with cDNA for cyclooxygenase‐1 or ‐2. When the cells overexpressing cyclooxygenase‐1 or ‐2 were stimulated with concanavalin A, the processing of matrix metalloproteinase‐2 was observed with the aid of gelatin zymography. This processing was not seen in mock‐transfected and original cells which did not express detectable cyclooxygenase activity. Furthermore, Northern blotting showed 8–13 fold induction of membrane‐type 1 matrix metalloproteinase which processed matrix metalloproteinase‐2 in the cells expressing cyclooxygenases. These findings suggest that both isoforms of cyclooxygenase mediate the processing of matrix metalloproteinase‐2 through induction of membrane‐type 1 metalloproteinase in breast cancer cells.