Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 498302
Title Effect of Glucuronidation on the Potential of Kaempferol to Inhibit Serine/Threonine Protein Kinases
Author(s) Beekmann, Karsten; Haan, Laura H.J. De; Actis-Goretta, Lucas; Bladeren, Peter J. Van; Rietjens, Ivonne M.C.M.
Source Journal of Agricultural and Food Chemistry 64 (2016)6. - ISSN 0021-8561 - p. 1256 - 1263.
DOI https://doi.org/10.1021/acs.jafc.5b05456
Department(s) Sub-department of Toxicology
VLAG
WIMEK
Publication type Refereed Article in a scientific journal
Publication year 2016
Keyword(s) conjugation - flavonoid - glucuronidation - serine/threonine protein kinases - substrate microarray
Abstract

To study the effect of metabolic conjugation of flavonoids on the potential to inhibit protein kinase activity, the inhibitory effects of the dietary flavonol kaempferol and its major plasma conjugate kaempferol-3-O-glucuronide on protein kinases were studied. To this end, the inhibition of the phosphorylation activity of recombinant protein kinase A (PKA) and of cell lysate from the hepatocellular carcinoma cell line HepG2 on 141 putative serine/threonine phosphorylation sites derived from human proteins was assessed. Glucuronidation reduced the inhibitory potency of kaempferol on the phosphorylation activity of PKA and HepG2 lysate on average about 16 and 3.5 times, respectively, but did not appear to affect the target selectivity for kinases present in the lysate. The data demonstrate that, upon glucuronidation, kaempferol retains part of its intrinsic kinase inhibition potential, which implies that K3G does not necessarily need to be deconjugated to the aglycone for a potential inhibitory effect on protein kinases.

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