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Research Interests
Signal Transduction
When
extracellular signals, such as neurotransmitters,
hormones, and growth factors, bind to their specific
receptors, phospholipids breakdown is one of the
immediate responses. The resulting breakdown products
become second messengers to amplify the extracelluar
signals, then the signals from the second messengers
are transcended to various effector molecules, which,
in turn, transduce their signals to next signaling
mediators, and so forth. The final effects of the
signal transduction would be one or more of the
many cellular phenomena, such as proliferation,
differentiation, or apoptosis.
The major research
goals of the Signal Transduction Laboratory is the
identification of the mechanism of signal transduction
pathway mediated by phospholipases. Based on the
substrate specificity and the produced second messengers,
the phospholipases are classified to A, C, and D.
Our lab has focused on the identification of the
regulatory mechanisms of and the discovery of new
molecular mediators for the signal transduction
of phospholipase C and D. These studies include
following studies. Purification of core signaling
molecules such as phospholipases and its kinetic
studies among various subtypes of the phospholipases;
identification of binding proteins and in vitro
molecular binding studies between phospholipases
and their putative effectors; establishing transient
and permanent cell lines expressing signal transduction-related
molecules for in vivo studies. The accumulations
of knowledges and experiences concerning the signal
transduction pathway for the last decade allow us
to expand our realm of research, not only in width
but in depth, to the molecular libraries, such as
synthetic peptides for the discovery of agonists
or antagonists, which ultimately lead to the developments
of new medicines. Recently, to provide valuable
informations for the basic researchers as well as
ideas for the industrial application in the field
of signal transduction, we are going to characterize
molecularly SMMC (signaling molecule multicomplex)
which composes of signal machinery by using PMT
(proteome molecular technology).
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Selected Publications
Bae, S.S., Lee, Y.H., Chang, J.S., Kim, Y.S.,
Ryu, S.H., and Suh, P.G. (1998) Src homology
domains of Phospholipase C-γ1 inhibits NGF-induced
differentiation of PC12 cells. J. Neurochem. 71,
178 - 185
Chang, J.S., Noh, D.Y., Park, I. A., Kim, M.J.,
Song, H., Ryu, S. H. and Suh, P. G. (1997) Overexpression
of Phospholipase C-r1 in Rat 3Y1 Fibroblast Cells
Leads to Malignant Transformatiom. Cancer. Res.
57, 5465 - 5468
Kim, M.J., Min, D.S., Ryu, S.H., and Suh, P.G.
(1998) A cytosolic, Gqα- and -βγ insensitive,
splice variant of phospholipase C-β4. J. Biol.
Chem. 273(6), 3618 - 3624
Bae, S.S., Perry, D.K., Lee, S.D., Chung, C.,
Oh, Y.S., Lee, H.T., Choi, J.H., Galadari, S.H.,
Ghayur, T., Ryu, S.H., Hannun, Y.A. and Suh, P.G.(2000)"
Proteolytic cleavage of phospholipase C-γ1 During
apoptosis" FASEB J. 14; 1083-1092
Hwang, J.I., Heo, K., Shin, K.J., Kim, E., Yun,
C.H., Ryu, S.H., Shin, H.S. and Suh, P.G. (2000)
" Regulation of phospholipase C-beta3 by Na+/H+
exchanger regulatory factor2" J. Biol. Chem.
275(22):16632-16637
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