Ubiquitin-specific peptidase 5, a target molecule of vialinin A, is a key molecule of TNF-α production in RBL-2H3 cells

• Published in: PloS one Vol. 8; no. 12; p. e80931
• Main Authors: Yoshioka, Yasukiyo, Ye, Yue Qi, Okada, Kiyoshi, Taniguchi, Kayoko, Yoshida, Ayaka, Sugaya, Kouichi, Onose, Jun-ichi, Koshino, Hiroyuki, Takahashi, Shunya, Yajima, Arata, Yajima, Shunsuke, Abe, Naoki
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 04.12.2013; Public Library of Science (PLoS)
• Subjects: Animals; Antigens; Blotting, Western; Cell culture; Cell Line; Crohns disease; Cytokines; Endopeptidases - metabolism; Enzymatic activity; Enzymes; Experiments; Gene expression; Inflammation; Inflammatory response; Interleukin-4 - metabolism; Leukemia; Peptidase; Proteins; Rats; Reverse Transcriptase Polymerase Chain Reaction; Rheumatoid arthritis; RNA, Small Interfering; Science; siRNA; Stem cells; Target recognition; Terphenyl Compounds - metabolism; Tumor Necrosis Factor-alpha - metabolism; Tumor necrosis factor-TNF; Tumor necrosis factor-α; Ubiquitin; Japan
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0080931

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.