Abstract：
:Types I and II cyclic adenosine 3':5'-monophosphate (cAMP)-dependent protein kinases were compared in extracts from untransformed rat 3Y1 cells and 3Y1 cells transformed by the highly oncogenic human adenovirus type 12. Analysis of the kinases through diethylaminoethyl Sepharose column chromatography showed a significantly increased activity of type I, but not of type II, cAMP-dependent protein kinase in two transformed cell clones tested. 8-Azidoadenosine 3':5'-monophosphate, a sensitive photoaffinity-labeling analogue of cAMP, was used to quantitate the regulatory subunits of the type I kinase. A 3- to 6-fold increase in the amount of incorporation of the photoaffinity label into the Mr 48,000 regulatory subunit of type I kinase was obtained in three transformants tested. The increased incorporation was attributed to an increase in the actual amount of the subunit rather than to an increase in the affinity of type I regulatory subunit for the photoaffinity label. These results suggest that type I cAMP-dependent protein kinase activity may be a biochemical marker for adenovirus transformation.
journal_name
Cancer Resjournal_title
Cancer researchauthors
Ledinko N,Chan IJsubject
Has Abstractpub_date
1984-06-01 00:00:00pages
2622-7issue
6eissn
0008-5472issn
1538-7445journal_volume
44pub_type
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