Antibodies to Xenopus egg S6 kinase II recognize S6 kinase from progesterone- and insulin-stimulated Xenopus oocytes and from proliferating chicken embryo fibroblasts

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Published inMolecular and Cellular Biology Vol. 7; no. 9; pp. 3147 - 3155
Main Authors Erikson, E, Stefanovic, D, Blenis, J, Erikson, R L, Maller, J L
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.09.1987
Subjects
Online AccessGet full text
ISSN0270-7306
1098-5549
DOI10.1128/MCB.7.9.3147

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Abstract Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
AbstractList Ribosomal protein S6 becomes highly phosphorylated during progesterone- or insulin-induced maturation of Xenopus laevis oocytes. We have previously purified an Mr 92,000 protein as one of the major S6 kinases from Xenopus unfertilized eggs. In this paper we confirm by renaturation of activity from a sodium dodecyl sulfate-polyacrylamide gel that this protein is an S6 kinase. This enzyme, termed S6 kinase II (S6 K II), was used for the preparation of polyclonal antiserum. Immunocomplexes formed with the antiserum and purified S6 K II were able to express kinase activity with the same substrate specificity as that of the purified enzyme, including autophosphorylation of S6 K II itself. The antiserum did not react with S6 kinase I, another major S6 kinase present in Xenopus eggs, which is chromatographically distinct from S6 K II. The administration of progesterone to oocytes resulted in a 20- to 25-fold increase in S6 kinase activity in extracts of these cells. Immunocomplex kinase assays done on extracts revealed that anti-S6 K II serum reacted with S6 kinase from progesterone-treated oocytes. This antiserum also reacted with the activated S6 kinase from insulin-stimulated oocytes. In addition, anti-S6 K II serum reacted with activated S6 kinase from chicken embryo fibroblasts stimulated with serum or transformed by Rous sarcoma virus. These results indicate that S6 K II or an antigenically related S6 kinase(s) is subject to regulation by mitogenic stimuli in various cell types.
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Author J L Maller
J Blenis
D Stefanovic
R L Erikson
E Erikson
AuthorAffiliation Department of Pharmacology, University of Colorado School of Medicine, Denver 80262
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Issue 9
Keywords Regulation(control)
Non fertilized ovum
Enzyme
Protein kinase
Ribosomal protein
Immunological method
Language English
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Snippet Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
Ribosomal protein S6 becomes highly phosphorylated during progesterone- or insulin-induced maturation of Xenopus laevis oocytes. We have previously purified an...
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StartPage 3147
SubjectTerms Animals
Antibody Specificity
Biological and medical sciences
Cell Division
Cell Transformation, Viral
Chemical Precipitation
Chick Embryo
Fundamental and applied biological sciences. Psychology
Immunologic Techniques
Insulin - pharmacology
Molecular and cellular biology
Molecular genetics
Molecular Weight
Oocytes - enzymology
Phosphoproteins - metabolism
Progesterone - pharmacology
Protein Kinases - immunology
Protein Kinases - metabolism
Ribosomal Protein S6
Ribosomal Proteins - metabolism
Translation. Translation factors. Protein processing
Xenopus laevis
Title Antibodies to Xenopus egg S6 kinase II recognize S6 kinase from progesterone- and insulin-stimulated Xenopus oocytes and from proliferating chicken embryo fibroblasts
URI http://mcb.asm.org/content/7/9/3147.abstract
https://www.ncbi.nlm.nih.gov/pubmed/3313008
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Volume 7
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