Abstract
The role of adenosine 3′:5′-cyclic monophosphate in the cortisol-mediated induction of HeLa 65 alkaline phosphatase was investigated. Although growth of these cells with 0.5-1.0 mm N6,O2′-dibutyryl adenosine 3′:5′-cyclic monophosphate induces a 5- to 8-fold increase in cellular phosphatase activity after 72 hr, neither cAMP nor theophylline induce at concentrations up to 1 mm. Sodium butyrate induces the enzyme as well as dibutyryl cAMP. Moreover, induction kinetics show sodium butyrate to be a more efficient inducer than dibutyryl cAMP, inducing activity as quickly as cortisol. This suggests that the butyric acid cleaved from dibutyryl cAMP by HeLa cells is the mediator of induction when the cyclic nucleotide derivative is used.
Original language | English (US) |
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Pages (from-to) | 619-623 |
Number of pages | 5 |
Journal | Archives of Biochemistry and Biophysics |
Volume | 164 |
Issue number | 2 |
DOIs | |
State | Published - Oct 1974 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology