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Faculty
 Chi-Kuang
Huang
Associate Professor of Immunology
huangchi@neuron.uchc.edu
Areas of Interest:
Protein phosphorylation is an essential part of the activating and
regulatory processes in the functioning and responses for a variety of
cells. Attention has been paid to protein phosphorylation in neutrophils
because of the importance of this leukocyte in defense against infection
and in a number of allergic and non-allergic tissue-damaging
inflammatory reactions. The ultimate purpose of the proposed
investigation is to identify, isolate and characterize those proteins
which are phosphorylated when neutrophils are stimulated by chemotactic
factors, cytokines and crosslinking of Fc receptors and the respective
protein kinases for which they are responsible. Attempts will be made to
identify the function of phosphorylated proteins, the role that
phosphorylation plays in these respective functions and what role the
proteins and their phosphorylation play in neutrophil stimulus-response
coupling. For these purposes, the following studies are being pursued:
(1) To define the varieties of neutrophil protein kinases (tyrosine
protein kinases, mitogen-activated protein kinase (MAP kinase), MAP
kinase-activated protein kinase 2, calcium/calmodulin-dependent protein
kinase, histone H4 protein kinase, protein kinase C and others); the
regulation and the mechanism of activation of these kinases and their
respective substrates in various subcellular fractions of neutrophils.
(2) To define the phosphoproteins, the phosphorylation levels of
which are regulated by chemotactic factors (fMet-Leu-Phe), cytokines,
crosslinking of Fc receptors, calcium ionophores and phorbol esters in
intact neutrophils. Attempts will be made to identify and characterize
the molecular components (protein kinases and their substrates) of the
physiologically important phosphorylation system in neutrophils.
Publications
Selected Publications:
Wu, Y., Hannigan, M., Kotlyarov, A., Gaestel, M., Wu, D., Huang, C-K.
(2004) A requirement of MAPKAPK2 in the uropod localization of PTGN
during fMLP-induced neutrophil chemotaxis. Biochem. Biophys. Res. Commun.
316:666-672.
Li, Z., Hannigan, M., Mo, Z., Liu, B., Lu, W., Smrcka, A..V., Wu, G.,
Liu, M., Huang, C-K. and Wu, D. (2003) Directional sensing requires
G__-mediated PAK1 and PIX_-dependent activation of cdc42. Cell
114:215-227.
Hannigan, M.O., Huang, C-K., and Wu, D.(2003) Roles of PI3K in
neutrophil function. Curr. Topics in Microbiology and Immunology
282:166-175.
Hannigan, M., Zhan, L., Zhong Li, Ai. Y., Wu, D. and Huang, C-K.
(2002) Neutrophils lacking phosphoinositide 3-kinase g show loss of
directionality during N-formyl-Met-Leu-Phe-induced chemotaxis. Proc.
Natl. Acad. Sci. 99:3603-3608.
Mathews, E.E., Dunn, B. D., Hannigan, M.O., Huang, C-K., and Lester,
E.H. (2002) Genetic control of neutrophil superoxide burst activity in
diabetes resistant Alr/Lt mice Free Radical Biol and Medicine
32:744-751.
Hannigan M.O., Zhan, L., Ai, Y., Kotlyarov, A., Gaestel, M. and
Huang, C-K. (2001) Abnormal migration phenotype of MAPKAP kinase 2-/-
neutrophils in Zigmond chambers containing fMLP gradients. J. Immunol.
167:3953-3961.
Cochrane, R., Clark, R.B., Huang, C-K., Cone, R.E. (2001)
Differential regulation of T cell receptor-mediated Th1 cell IFN-g
production and proliferation by divergent cAMP-mediation redox pathway.
J. Interferon and Cytokine Research 21:797-807.
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