Abstract:
:Platelet release products and purified platelet-derived growth factor stimulated the phosphorylation of ribosomal protein S6 in cultured mouse Balb/c 3T3 fibroblasts. The post-nuclear fraction of the stimulated cells was enriched in S6 kinase activity specific for sites resembling those phosphorylated within intact cells in response to PDGF as determined by tryptic peptide mapping. 3T3-S6 sites closely resembled those phosphorylated in S6 of rat hepatocytes stimulated with insulin and included sites for both cAMP-dependent and independent kinases.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Wettenhall RE,Chesterman CN,Walker T,Morgan FJdoi
10.1016/0014-5793(83)81072-2subject
Has Abstractpub_date
1983-10-03 00:00:00pages
171-6issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(83)81072-2journal_volume
162pub_type
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