Publications by authors named "Kwangbae Kim"

Although islands in South Korea have been significantly impacted by human activities, marine ecological studies focusing on island coasts have been limited. Due to their distinct characteristics, macrobenthos is extensively utilized to assess the impact of anthropogenic influences on the marine environment. In August 2010, August 2011, and September 2012, samples of macrobenthic communities, bottom water, and sediment were collected from the subtidal zones around southern Jindo and northern Jeju islands in South Korea.

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Background: Jeju Island is a world-renowned tourist destination. However, with the increasing intensity of anthropogenic activities, the coastal marine environment of Jeju Island has been negatively affected.

Methods And Results: Our study used five benthic indices to assess the ecological quality of the subtidal zone in northern Jeju Island.

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Previously, we demonstrated that the homeoprotein Msx1 interaction with p53 inhibited tumor growth by inducing apoptosis. However, Msx1 can exert its tumor suppressive effect through the inhibition of angiogenesis since growth of the tumor relies on sufficient blood supply from the existing vessels to provide oxygen and nutrients for tumor growth. We hypothesized that the inhibition of tumor growth by Msx1 might be due to the inhibition of angiogenesis.

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During carcinogenesis, NF-gammaB mediates processes associated with deregulation of the normal control of proliferation, angiogenesis, and metastasis. Thus, suppression of NF-gammaB has been linked with chemoprevention of cancer. Accumulating findings reveal that heat shock protein 90 (HSP90) is a molecular chaperone and a component of the IgammaB kinase (IKK) complex that plays a central role in NF-gammaB activation.

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The stability of wild-type p53 is critical for its apoptotic function. In some cancers, wild-type p53 is inactivated by interaction with viral and cellular proteins, and restoration of its activity has therapeutic potential. Here, we identify homeobox Msx1 as a p53-interacting protein and show its novel function as a p53 regulator.

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