KAMADA, Shinji, Ph.D.

Professor, Division of Biosignal Transduction, Laboratory of Gene Function

Research Interests

 Organisms, including humans, are living in the environments that involve many stresses inducing DNA damages. Cells containing damaged DNA quickly respond to arrest the cell cycle, leading to DNA repair, apoptosis, or senescence. Apoptosis usually offers advantages during the life cycle of a multicellular organism. If damages are too severe to repair, cells die by apoptosis and are engulfed by surrounding cells, leading to quick removal of the dead cells to prevent inflammation. In addition, defects in apoptotic processes have been implicated in a variety of diseases. Excessive apoptosis causes atrophy such as neurodegenerative disorders, whereas an insufficient amount of apoptosis results in uncontrolled cell proliferation such as cancer. On the other hand, another form of cellular response to DNA damages is senescence. Senescence was first mentioned as a state of irreversible growth arrest of normal human fibroblasts, and induced by a variety of stimuli including DNA damages. Recently, it was suggested that senescence functions as an effective tumor suppression mechanism by preventing cell proliferation. DNA damages can induce both apoptosis and senescence. However, the molecule mechanisms of cell fate decision between apoptosis and senescence have been under investigation. Our main Research Interest is to clarify how cells are destined for apoptosis or senescence by the same DNA damages.

Research Focus

1. The regulation of apoptosis and cell cycle progression by caspases.

2. Molecular mechanisms of apoptosis and senescence induced by DNA damages.

Recent Publication

  • Nakano, M., Nakashima A., Nagano, T., Ishikawa, S., Kikkawa, U., and Kamada, S. (2013)
    Branched-chain amino acids enhance premature senescence through mammalian target of rapamycin complex I-mediated up regulation of p21 protein.
    PLoS ONE 8, e80411.
  • Nagano, T., Hashimoto, T., Nakashima, A., Hisanaga, S., Kikkawa, U., and Kamada, S. (2013)
    Cyclin I is involved in the regulation of cell cycle progression.
    Cell Cycle 12, 2617-2624.
  • Kamada, S. (2013)
    Inhibitor of apoptosis proteins as E3 ligases for ubiquitin and NEDD8. (review)
    Biomol. Concepts 4, 161-171.
  • Nagano, T., Hashimoto, T., Nakashima, A., Kikkawa, U., and Kamada, S. (2012)
    X-linked inhibitor of apoptosis protein mediates neddylation by itself but does not function as a NEDD8-E3 ligase for caspase-7.
    FEBS Lett. 586, 1612-1616.
  • Hashimoto, T., Juso, K., Nakano, M., Nagano, T., Kambayashi, S., Nakashima, A., Kikkawa, U., and Kamada, S. (2012)
    Preferential Fas-mediated apoptotic execution at G1 phase: the resistance of mitotic cells to the cell death.
    Cell Death Dis. 3, e313.
  • Hashimoto, T., Kikkawa, U., and Kamada, S. (2011)
    Contribution of caspase(s) to the cell cycle regulation at mitotic phase.
    PLoS ONE 6 (3), e18449.
  • Hashimoto, T., Yamauchi, L., Hunter, T., Kikkawa, U., and Kamada, S. (2008)
    Possible involvement of caspase-7 in cell cycle progression at mitosis.
    Genes Cells 13, 609-621.
  • Kamada, S., Kikkawa, U., Tsujimoto, Y., and Hunter, T. (2005)
    A-kinase-anchoring protein 95 functions as a potential carrier for the nuclear translocation of active caspase 3 through an enzyme-substrate-like association.
    Mol. Cell. Biol. 25, 9469-9477.
  • Kamada, S., Kikkawa, U., Tsujimoto, Y., and Hunter, T. (2005)
    Nuclear translocation of caspase-3 is dependent on its proteolytic activation and recognition of a substrate-like protein(s).
    J. Biol. Chem. 280, 857-860.

Contact

Office: Research Center for Environmental Genomics 4F

Tel&Fax: +81-78-803-5959

Fax: +81-78-803-5951

E-mail: skamada@kobe-u.ac.jp