Abstract
The incorporation of 32PO4 into cytosol and ribosomal proteins was measured after cAMP and ACTH treatment of functional adrenal tumor cell cultures. Although small changes in total 32PO4 uptake occurred after ACTH treatment a marked increase in 32PO4 incorporation into cytosol and ribosomal proteins was observed. Changes in phosphate uptake and pool size previously observed after cAMP treatment were eliminated by the use of preincubated adrenal cell cultures. In the absence of such changes, selective increases in the incorporation of 32PO4 into cytosol and ribosomal protein were observed after cAMP treatment. This is the first report that cAMP increases the phosphorylation of both cytosol and ribosomal proteins. These results support the concept that ACTH regulates adrenal cell function via cAMP dependent phosphorylation of adrenal cell proteins.
| Original language | English |
|---|---|
| Pages (from-to) | 1287-1293 |
| Number of pages | 7 |
| Journal | Endocrinology |
| Volume | 93 |
| Issue number | 6 |
| State | Published - Dec 1 1973 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Endocrinology
- Endocrinology, Diabetes and Metabolism
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ACTH and cAMP stimulation of adrenal ribosomal protein phosphorylation. / Roos, B. A.
In: Endocrinology, Vol. 93, No. 6, 01.12.1973, p. 1287-1293.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - ACTH and cAMP stimulation of adrenal ribosomal protein phosphorylation
AU - Roos, B. A.
PY - 1973/12/1
Y1 - 1973/12/1
N2 - The incorporation of 32PO4 into cytosol and ribosomal proteins was measured after cAMP and ACTH treatment of functional adrenal tumor cell cultures. Although small changes in total 32PO4 uptake occurred after ACTH treatment a marked increase in 32PO4 incorporation into cytosol and ribosomal proteins was observed. Changes in phosphate uptake and pool size previously observed after cAMP treatment were eliminated by the use of preincubated adrenal cell cultures. In the absence of such changes, selective increases in the incorporation of 32PO4 into cytosol and ribosomal protein were observed after cAMP treatment. This is the first report that cAMP increases the phosphorylation of both cytosol and ribosomal proteins. These results support the concept that ACTH regulates adrenal cell function via cAMP dependent phosphorylation of adrenal cell proteins.
AB - The incorporation of 32PO4 into cytosol and ribosomal proteins was measured after cAMP and ACTH treatment of functional adrenal tumor cell cultures. Although small changes in total 32PO4 uptake occurred after ACTH treatment a marked increase in 32PO4 incorporation into cytosol and ribosomal proteins was observed. Changes in phosphate uptake and pool size previously observed after cAMP treatment were eliminated by the use of preincubated adrenal cell cultures. In the absence of such changes, selective increases in the incorporation of 32PO4 into cytosol and ribosomal protein were observed after cAMP treatment. This is the first report that cAMP increases the phosphorylation of both cytosol and ribosomal proteins. These results support the concept that ACTH regulates adrenal cell function via cAMP dependent phosphorylation of adrenal cell proteins.
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UR - http://www.scopus.com/inward/citedby.url?scp=0015765543&partnerID=8YFLogxK
M3 - Article
C2 - 4356611
AN - SCOPUS:0015765543
VL - 93
SP - 1287
EP - 1293
JO - Endocrinology
JF - Endocrinology
SN - 0013-7227
IS - 6
ER -