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Arfaptin 1 inhibits ADP‐ribosylation factor‐dependent matrix metalloproteinase‐9 secretion induced by phorbol ester in HT 1080 fibrosarcoma cells
Author(s) -
Ho Wan-Ting,
Exton John H.,
Williger Ben-Tsion
Publication year - 2003
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(03)00098-x
Subject(s) - secretion , phospholipase d , phorbol , matrix metalloproteinase , forskolin , cholera toxin , adp ribosylation factor , chemistry , adp ribosylation , in vitro , protein kinase c , microbiology and biotechnology , enzyme , endocrinology , biology , biochemistry , cell , golgi apparatus , nad+ kinase
Matrix metalloproteinase‐9 (MMP‐9) is a collagenolytic enzyme secreted by cancer cells and involved in invasiveness and metastasis. Its secretion from human fibrosarcoma HT 1080 cells is markedly enhanced by phorbol 12‐myristate 13‐acetate (PMA) and abolished by brefeldin A, an inhibitor of ADP‐ribosylation factor (ARF) activation. These results support a role for ARF in PMA‐stimulated MMP‐9 secretion. Overexpression of arfaptin 1, a 39 kDa ARF‐binding protein that inhibits in vitro activation of cholera toxin ADP‐ribosyltransferase and phospholipase D (PLD) by ARF, inhibited PMA‐stimulated MMP‐9 and PLD activation. These data are in agreement with previous results demonstrating a significant role for PLD in regulating MMP‐9 secretion.