Identification of a novel Ca2+-stimulated S6-kinase in rat liver.

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.

authors

Harlin JC,Tredano M,Rider MH,Bollen M,Chédeville A,Lavoinne A

doi

10.1006/bbrc.1997.7175

subject

Has Abstract

pub_date

1997-10-20 00:00:00

pages

451-6

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(97)97175-8

journal_volume

239

pub_type

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