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Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines
Author(s) -
Bottoni Arianna,
Vignali Cristina,
Piccin Daniela,
Tagliati Federico,
Luchin Andrea,
Zatelli Maria Chiara,
Uberti Ettore C. degli
Publication year - 2007
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.21083
Subject(s) - secretion , hela , proteasome , biology , cleavage (geology) , cell culture , cytokine , microbiology and biotechnology , monocyte , cancer cell , cell , protease , biochemistry , cancer , immunology , enzyme , genetics , paleontology , fracture (geology)
The aminoacyl t‐RNA synthetase interacting multifunctional protein (AIMP1) is the precursor of the multifunctional inflammatory cytokine endothelial monocyte‐activating polypeptide II (EMAP II). We previously demonstrated that AIMP1 secretion by pituitary adenomas is inversely correlated with tumor diameter and with RARS expression, suggesting that a high amount of RARS associated with AIMP1 might prevent the secretion of the latter cytokine. In this study, we investigated the role of RARS in modulating the secretion of AIMP1 in HeLa and MCF7 cell lines and investigated the possible role of the multicatalytic protease in the cleavage of AIMP1 to generate EMAP II. Our data show that RARS over‐expression impairs AIMP1 secretion by both HeLa and MCF7 cells. Moreover, proteasome inhibition impairs AIMP1 cleavage to produce EMAP II. These data indicate that RARS over‐expression associates with a reduced AIMP1 secretion and that the multicatalytic protease is involved in the generation of the mature cytokine, EMAP II. J. Cell. Physiol. 212: 293–297, 2007. © 2007 Wiley‐Liss, Inc.