title: Differential regulation of messenger ribonucleic acids for specific subunits of cyclic adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase by cAMP in rat Sertoli cells.
abstract: In the present study we have examined the effects of FSH, forskolin, and (Bu)2cAMP on messenger RNA (mRNA) levels for all known subunits of cAMP-dependent protein kinase in rat Sertoli cells, using newly developed complementary DNA (cDNA) probes. mRNAs for the three regulatory subunits [RI alpha, RII51, (RII beta), and RII54 (RII alpha)] and the catalytic subunit C alpha were shown to be present in cultured rat Sertoli cells, whereas mRNAs for the subunits designated RI beta and C beta were below the level of detection. A high-levelled, concentration-dependent increase in a 3.2 kilobase mRNA for RII51 was observed when cultured immature Sertoli cells were incubated with increasing concentrations of (Bu)2cAMP (10(-6) to 5 X 10(-3) M) for 16 h. Densitometric scanning indicated a maximal stimulation by (Bu)2cAMP of 30- to 40-fold. Incubation with forskolin (100 microM) and FSH (200 ng/ml) gave rise to a smaller but significant increase in mRNA for RII51. When cultured Sertoli cells were incubated in the presence of 10(-4) M (Bu)2cAMP for varying time periods, there was a biphasic regulation of mRNA for RII51. (Bu)2cAMP caused an initial increase in mRNA for RII51 with maximal levels obtained after 10-16 h, after which a time-dependent decrease was observed. For the other three subunits present in Sertoli cells (RI alpha, RII54, and C alpha) a smaller but significant stimulation by (Bu)2cAMP and forskolin (2-4 fold) was seen. The functional implications of these changes in mRNA levels for the different subunits of cAMP-dependent protein kinase have not yet been revealed. However, our data clearly demonstrate differential regulation of the various subunits of cAMP-dependent protein kinase in Sertoli cells. Furthermore, these results document the presence of distinct adaptational changes taking place at the level of cAMP-dependent protein kinase in response to long term elevation of cAMP.
authors.affiliation: Institute of Pathology, Rikshospitalet, Oslo, Norway.
authors.forename: O
authors.initials: O
authors.lastname: Oyen
authors.forename: M
authors.initials: M
authors.lastname: Sandberg
authors.forename: W
authors.initials: W
authors.lastname: Eskild
authors.forename: F O
authors.initials: FO
authors.lastname: Levy
authors.forename: G
authors.initials: G
authors.lastname: Knutsen
authors.forename: S
authors.initials: S
authors.lastname: Beebe
authors.forename: V
authors.initials: V
authors.lastname: Hansson
authors.forename: T
authors.initials: T
authors.lastname: Jahnsen
mesh_terms: D000818:Animals; D003994:Bucladesine / Q000494:pharmacology; D002478:Cells, Cultured; D005576:Colforsin / Q000494:pharmacology; D000242:Cyclic AMP / Q000494:pharmacology*; D004247:DNA; D005640:Follicle Stimulating Hormone / Q000494:pharmacology; D005786:Gene Expression Regulation / Q000187:drug effects*; D007700:Kinetics; D008297:Male; D011494:Protein Kinases / Q000235:genetics*; D012333:RNA, Messenger / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D012708:Sertoli Cells / Q000187:drug effects / Q000201:enzymology*
chemical_list: D012333:RNA, Messenger; D005576:Colforsin; D003994:Bucladesine; D005640:Follicle Stimulating Hormone; D004247:DNA; D000242:Cyclic AMP; D011494:Protein Kinases