8-N3-cAMP - CAS 31966-52-6
Catalog number: 31966-52-6
Category: Nucleotides
Molecular Formula:
C10H10N8O6P · Na
Molecular Weight:
Cyclic Nucleotides
8-N3-cAMP is an analogue of cAMP binding proteins used for photoaffinity labelling.
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≥ 95% by HPLC
8- Azidoadenosine- 3', 5'-cyclic monophosphate, sodium salt
1.cAMP-binding proteins in medullary tubules from rat kidney: effect of ADH.
Gapstur SM1, Homma S, Dousa TP. Am J Physiol. 1988 Aug;255(2 Pt 2):F292-300.
Little is known of the regulatory steps in the cellular action of vasopressin (AVP) on the renal epithelium, subsequent to the cAMP generation. We studied cAMP-binding proteins in the medullary collecting tubule (MCT) and the thick ascending limb of Henle's loop (MTAL) microdissected from the rat kidney by use of photoaffinity labeling. Microdissected tubules were homogenized and photoaffinity labeled by incubation with 1 microM 32P-labeled 8-azido-adenosine 3',5'-cyclic monophosphate (N3-8-[32P]-cAMP); the incorporated 32P was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography. Both in MCT and MTAL preparations, the analyses showed incorporation of N3-8-[32P]cAMP into two bands (Mr = 49,000 and Mr = 55,000) that comigrated with standards of the cAMP-dependent protein kinase regulatory subunits RI and RII. In MCT, most of the 32P (80%) was incorporated into RI, whereas in MTAL the 32P incorporated into RI and RII was equivalent.
2.Characterization of soluble cyclic adenosine monophosphate-dependent protein kinase isozymes in murine embryonic palatal tissue.
Greene RM1, Linask KK, Pisano MM, Lloyd MR. J Craniofac Genet Dev Biol. 1989;9(2):207-22.
Certain hormonal primary messengers identified in the mammalian palate during its ontogeny transmit information to the interior of the cell via transmembrane signaling systems that control the production of the secondary messenger cyclic adenosine monophosphate. The singular role of intracellular cyclic AMP is to activate cAMP-dependent protein kinases (cAMP-dPK). cAMP-dPK were thus identified and characterized in the developing murine embryonic palate. Incubation of cytosolic fractions of embryonic palatal tissue with cAMP resulted in a dose-dependent increase in the cAMP-dPK activity ratio. A transient elevation of basal cAMP-dPK was seen during the period of palatal ontogeny that corresponded temporally with a previously demonstrated transient elevation of palatal basal cAMP levels. Fractions of embryonic palatal tissue cytosols derived by diethylaminoethyl (DEAE)-Sephacel chromatography were analyzed for phosphotransferase activity and for [3H]-cAMP binding to the regulatory (R) subunits of cAMP-dPK.
3.Inhibition of the self-renewal capacity of blast progenitors from acute myeloblastic leukemia patients by site-selective 8-chloroadenosine 3',5'-cyclic monophosphate.
Pinto A1, Aldinucci D, Gattei V, Zagonel V, Tortora G, Budillon A, Cho-Chung YS. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):8884-8.
The physiologic balance between the two regulatory subunit isoforms, RI and RII, of cAMP-dependent protein kinase is disrupted in cancer cells; growth arrest and differentiation of malignant cells can be achieved when the normal ratio of these intracellular signal transducers of cAMP is restored by the use of site-selective cAMP analogs. In this study we evaluated the effects of the site-selective cAMP analog 8-chloroadenosine 3',5'-cyclic monophosphate (8-Cl-cAMP) on clonogenic growth of blast progenitors from 15 patients with acute myeloblastic leukemia and 3 patients affected by advanced myelodysplastic syndrome. Leukemic blast progenitors undergo terminal divisions, giving rise to colonies in methylcellulose. The self-renewal capacity of blast progenitors is conversely reflected in a secondary methylcellulose assay after exponential growth of clonogenic cells in suspension cultures. In all the samples tested, 8-Cl-cAMP, at micromolar concentrations (0.
4.Isoproterenol-induced amylase release in rabbit parotid acini: relation of protein phosphorylation, cyclic AMP and related kinase activity to changes in secretory rate.
Horio B, Dowd F, Watson E, Mednieks M, Warren J. J Pharmacol Exp Ther. 1984 May;229(2):608-14.
Isoproterenol-induced amylase release from rabbit parotid acini was examined in relation to cyclic AMP (cAMP) concentrations, cAMP-dependent protein kinase (cAMP-PK) activity ratios and protein phosphorylation. Initial stimulation of amylase release by isoproterenol was preceded by increases in cAMP, cAMP-PK activity ratios and phosphorylation of a 34,000 MW (major) and a 30,000 MW (minor) protein in the microsomal fraction. When propranolol was added, decreases in cAMP concentrations and cAMP-PK activity ratios preceded the reduction in amylase release. Detailed analysis was performed on the 34,000 MW protein. The relation of dephosphorylation of protein 34 and reduction in amylase release was complex. Slight dephosphorylation occurred before or concurrently with the decrease in amylase release; however, maximal dephosphorylation was preceded by maximal inhibition of amylase release. When secretion of amylase was reinstituted by isoproterenol or forskolin, increases in cAMP and cAMP-PK activity ratios occurred before or in concert with amylase release but rephosphorylation of protein 34 occurred after the start of amylase release.
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Chemical Structure

CAS 31966-52-6 8-N3-cAMP

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