Major objective of biochemistry is the complete understanding of all of the chemical processes associated with living cells at the molecular level. The knowledge of biochemistry and molecular biology are giving an ever-increasing impact on clinical medicine in prevention, diagnosis, and treatment of disease.
In our laboratory, we are focusing on the study of stress proteins, especially on mammalian HSP105 family proteins, which are an evolutionarily highly conserved class of proteins expressed in organisms from yeast to human in response to various stresses and pathophysiological conditions. Hsp105 plays important roles in normal cellular functions as molecular chaperone. The protein prevents the aggregation of thermally denatured proteins, and negatively regulates the Hsp70 chaperone activity by inhibiting the ATPase activity of Hsp70. Hsp105 has opposite effects on stress-induced apoptosis depending on cell types; a pro-apoptotic effect in embryonic cells and an anti-apoptotic effect in neuronal cells. Furthermore, it is suggested an important role for Hsp105 in preventing neurodegenerative diseases associated with polyglutamine expansions. We are also interested in applied studies of stress proteins for therapeutic usage against diseases such as neurodegerative disorders, and are trying to find compounds which selectively modulate the expression of stress proteins to use for medicinal applications.

Localization of Hsp105 in mammalian cells

Life of Proteins is escorted by molecular chaperone: : Molecular chaperone mediates the folding of nascent proteins (1) and the association (2), transport (3) and degradation (4) of proteins in cells.