Open AccessUbiquitin-Specific Peptidase 5, a Target Molecule of Vialinin A, Is a Key Molecule of TNF-α Production in RBL-2H3 Cells
Author(s) -
Yasukiyo Yoshioka,
Yue Qi Ye,
Kiyoshi Okada,
Kayoko Taniguchi,
Ayaka Yoshida,
Kimio Sugaya,
Junichi Onose,
Hiroyuki Koshino,
Shigetoshi Takahashi,
Arata Yajima,
Seishi Yajima,
Naoki Abe
Publication year - 2013
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0080931
Subject(s) - proinflammatory cytokine , deubiquitinating enzyme , tumor necrosis factor alpha , ubiquitin , microbiology and biotechnology , chemistry , gene knockdown , biochemistry , biology , inflammation , gene , immunology
Tumor necrosis factor alpha (TNF-α), a central mediator of the inflammatory response, is released from basophilic cells and other cells in response to a variety of proinflammatory stimuli. Vialinin A is a potent inhibitor of TNF-α production and is released from RBL-2H3 cells. Ubiquitin-specific peptidase 5 (USP5), a deubiquitinating enzyme, was identified as a target molecule of vialinin A and its enzymatic activity was inhibited by vialinin A. Here we report production of TNF-α is decreased in USP5 siRNA-knockdown RBL-2H3 cells, compared with control cells. The finding of the present study strongly suggests that USP5 is one of the essential molecules for the production of TNF-α in RBL-2H3.