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TPA‐enhanced invasion of matrigel associated with augmentation of cell motility but not metalloproteinase activity in a highly metastatic variant (L‐10) of human rectal adenocarcinoma cell line RCM‐1
Author(s) -
Nabeshima Kazuki,
Komada Naoto,
Kishi JunIchi,
Koita Hiroyuki,
Inoue Teruhiko,
Hayakawa Taro,
Koono Masashi
Publication year - 1993
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910550617
Subject(s) - matrigel , motility , matrix metalloproteinase , cell culture , matrix metalloproteinase inhibitor , cell , biology , cancer research , chemistry , microbiology and biotechnology , pathology , medicine , biochemistry , genetics
We previously found that the enhanced activity to invade Matrigel upon stimulation with 12‐O‐tetradecanoylphorbol‐13‐acetate (TPA) was one of the major properties of a highly metastatic variant (L‐10) of a human rectal adenocarcinoma cell line RCM‐1. To clarify the mechanism of this enhancement, we examined the effect of TPA on 2 major biological factors involved in tumor cell invasion: cell motility and matrix‐degrading metalloproteinase activity. The enhanced invasiveness was inhibited by protein‐kinase‐C inhibitors. TPA markedly enhanced both haptotactic response to type‐IV collagen and motility on tissue‐culture glass substrate of L‐10 cells in a dose‐response manner quite similar to that of TPA‐enhanced invasion of Matrigel. On the other hand, TPA showed little enhancement of metalloproteinase production, which was assessed by gelatin‐ and casein‐zymography, and of type‐IV collagenolytic activity. Addition of TIMP (tissue inhibitors of metalloproteinase)‐1 inhibited TPA‐enhanced invasion of Matrigel by only up to 13%. Thus, TPA treatment of L‐10 cells enhanced invasion of Matrigel in association with augmentation of cell motility but did not enhance metalloproteinase activity.