Elucidation of a new activation regulation mechanism for the anti-viral factor interferon
Research Press Release | October 22, 2013
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| Key Points | – Jun activation domain-binding protein 1 (JAB1), which is responsible for proteolytic system, has been identified as a new binding partner for tyrosine kinase 2 (TYK2), a molecule involved in interferon (IFN) signal transduction.
– When a low-molecular-weight compound that inhibits the proteolytic system molecular group regulated by JAB1 was liberated, IFN receptor protein levels increased (indicating decreased degradation), and activation of downstream signal transduction and increased anti-viral activity / anti-proliferative activity due to IFN stimulation were observed. – JAB1 and its associated proteolytic system have the potential as new targets for the development of anti-viral and anti-cancer agents. |
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| Overview | Cells in vivo produce interferon (IFN) and other cytokines, which are humoral proteins, when they are invaded by viruses or other pathogens as well as in response to the proliferation of tumor cells. IFN is an anti-viral factor that not only inhibits viral proliferation and suppresses tumor cell proliferation, but also acts to regulate the immune system and inflammation, and is a particularly important molecule in the maintenance of bodily homeostasis. IFN is already widely used in clinical practice as an anti-viral and anti-cancer agent.
When cells are stimulated by IFN, its effect is limited by the degradation of IFN receptors. In this study, we discovered that a protein called JAB1, which regulates the proteolytic system, inhibits IFN receptor degradation. When a low-molecular-weight compound that inhibits the proteolytic system molecules regulated by JAB1 was liberated, IFN receptor protein levels increased (indicating decreased degradation), and activation of downstream signal transduction and increased anti-viral activity and anti-proliferative activity due to IFN stimulation were observed. The development of new drugs targeting JAB1 protein and its associated proteolytic system have the potential of being artificially manipulated and elevating the treatment results. |
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| Inquiries |
Ryuta Muromoto , Asst. Professor, Faculty of Pharmaceutical Sciences, Hokkaido University TEL: +81-11-706-3245 FAX:+81-11-706-4990 e-mail: muro@pharm.hokudai.ac.jp |
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Japanese Link |
http://www.hokudai.ac.jp/news/131009_pr_pharm.pdf | |
| Publications | Journal of Biological Chemistry (2013.9.16) | |
