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Osteoactivin fragments produced by ectodomain shedding induce MMP‐3 expression via ERK pathway in mouse NIH‐3T3 fibroblasts
Author(s) -
Furochi Harumi,
Tamura Seiko,
Mameoka Mai,
Yamada Chiharu,
Ogawa Takayuki,
Hirasaka Katsuya,
Okumura Yuushi,
Imagawa Takahito,
Oguri Sachiko,
Ishidoh Kazumi,
Kishi Kyoichi,
Higashiyama Shigeki,
Nikawa Takeshi
Publication year - 2007
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/j.febslet.2007.11.036
Subject(s) - ectodomain , mapk/erk pathway , extracellular , extracellular matrix , microbiology and biotechnology , chemistry , matrix metalloproteinase , kinase , 3t3 cells , protein kinase a , metalloproteinase , biology , biochemistry , transfection , receptor , gene
Intact osteoactivin, a novel type I membrane glycoprotein, were shed at a dibasic motif in the juxtamembrane region in C2C12 myoblasts. Extracellular fragments were secreted into the culture media by a putative metalloprotease. Extracellular fragments of osteoactivin, but not control protein, induced matrix metalloprotease‐3 (MMP‐3) expression in NIH‐3T3 fibroblasts. Epidermal growth factor (ERK) kinase inhibitors inhibited the osteoactivin‐mediated MMP‐3 expression, whereas the extracellular fragment of osteoactivin activated ERK1/2 and p38 in the mitogen‐activated protein kinase pathway. Our results suggest that the extracellular fragments of osteoactivin produced by shedding act as a growth factor to induce MMP‐3 expression via the ERK pathway in fibroblasts.