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Doxorubicin binds to un-phosphorylated form of hNopp140 and reduces protein kinase CK2-dependent phosphorylation of hNopp140

Title
Doxorubicin binds to un-phosphorylated form of hNopp140 and reduces protein kinase CK2-dependent phosphorylation of hNopp140
Authors
Kim Y.-K.Lee W.K.Jin Y.Lee K.-J.Jeon H.Yu Y.G.
Ewha Authors
이공주
SCOPUS Author ID
이공주scopus
Issue Date
2006
Journal Title
Journal of Biochemistry and Molecular Biology
ISSN
1225-8687JCR Link
Citation
vol. 39, no. 6, pp. 774 - 781
Indexed
SCOPUS WOS scopus
Abstract
Human nucleolar phosphoprotein p140 (hNopp140) is a nucleolar phosphoprotein that can bind to doxorubicin, an anti-cancer agent. We have examined the interaction between hNopp140 and doxorubicin as well as the folding property of hNopp140. Also, the effects of ATP and phosphorylation on the affinity of hNopp140 to doxorubicin are investigated by affinity dependent co-precipitation and surface plasmon resonance methods. Doxorubicin preferentially binds to un-phosphorylated form of hNopp140 with a KD value of 3.3 × 10-7 M. Furthermore, doxorubicin reduces the protein kinase CK2-dependent phosphorylation of hNoppl40, indicating that doxorubicin may perturb the cellular function of hNopp140 by reducing the protein kinase CK2-dependent phosphorylation of hNopp140. Low contents of the secondary structures of hNopp140 and the fast rate of proteolysis imply that hNoppl40 has a high percentage of flexible regions or extended loop structures.
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약학대학 > 약학과 > Journal papers
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