Abstract:
:Extracellular calcium addition transiently stimulated two S6 peptide kinase activities in isolated rat hepatocytes. Mono Q chromatography revealed that the activities eluting at 0.15 M NaCl and 0.18 M NaCl were stimulated 4-fold and 2-fold, respectively. The kinase stimulated by calcium was a 40000-Mr S6 peptide kinase, as demonstrated by partial purification from whole liver. The protein kinase did not crossreact with antibodies directed against the N- or C-terminal part of p70 ribosomal S6 kinase (p70(S6K)) and the C-terminal part of p90 ribosomal S6 kinase (p90(rsk)). Following digestion of 40000-Mr S6 peptide kinase with trypsin, six peptides were sequenced. There was no similarity with the sequences of p70(S6K) and p90(rsk). Moreover, the obtained sequences could not be identified in the SwissProt or EMBL-genebank databases, suggesting that 40000-Mr S6 peptide kinase probably represents a novel protein kinase.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Harlin JC,Tredano M,Rider MH,Bollen M,Chédeville A,Lavoinne Adoi
10.1006/bbrc.1997.7175subject
Has Abstractpub_date
1997-10-20 00:00:00pages
451-6issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(97)97175-8journal_volume
239pub_type
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