Abstract:
:The physiological correlation between casein kinase I (CK-I) and an isoform eta of protein kinase C (C-kinase eta) was investigated in vitro, since it has been reported that (i) cholesterol-3-sulfate (CH-3S) effectively activates C-kinase eta rather than the other isoforms (C-kinase epsilon and C-kinase delta) in vitro; and (ii) CK-I efficiently phosphorylates CH-3S-binding proteins, such as high mobility group protein 1 (HMG1), in the presence of CH-3S in vitro. We found that (i) CK-I phosphorylated Thr in preference to Ser on recombinant human C-kinase isoform eta (rhC-kinase eta) in the presence of CH-3S; (ii) this phosphorylation was selectively inhibited by CK-I-7 (a CK-I inhibitor); and (iii) the activity (phosphorylation of protamine sulfate) of rhC-kinase eta was approx. 3.2-fold stimulated by its full phosphorylation by CK-I in the presence of 3 microM CH-3S. These results suggest that CK-I is a protein kinase responsible for the activation of rhC-kinase eta in the presence of CH-3S in vitro.
journal_name
Biol Pharm Bulljournal_title
Biological & pharmaceutical bulletinauthors
Okano M,Yokoyama T,Miyanaga T,Ohtsuki Kdoi
10.1248/bpb.27.109subject
Has Abstractpub_date
2004-01-01 00:00:00pages
109-12issue
1eissn
0918-6158issn
1347-5215journal_volume
27pub_type
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更新日期:2008-11-01 00:00:00
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journal_title:Biological & pharmaceutical bulletin
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