Springer Protocols: Abstract: Biochemical Methods for Detection and Measurement of Cyclic AMP and Adenylyl Cyclase Activity

Biochemical Methods for Detection and Measurement of Cyclic AMP and Adenylyl Cyclase Activity

By: Steven R. Post², Rennolds S. Ostrom², Paul A. Insel²

Abstract

Full Text

Download PDF (106K)

Many drugs and hormones interact with plasma membrane receptors to induce changes in the production of intracellular second messengers. The first such messenger to be identified was adenosine-3′,5′ cyclic monophosphate (cAMP), discovered by Sutherland and Rall in the late 1950s (1). Changes in cellular cAMP levels can occur from increases or decreases in its biosynthesis (which results from the catalytic conversion of ATP to cAMP by the enzyme adenylyl cyclase) or by altering its degradation (which results from hydrolysis of the cyclic phosphodiester bond by cyclic nucleotide or cAMP phosphodiesterases).

Affiliation(s): (2) Department of Pharmacology, University of California, San Diego, CA

Book Title: Adrenergic Receptor Protocols

Series: Methods in Molecular Biology | Volume: 126 | Pub. Date: Nov-05-1999 | Page Range: 363-374 | DOI: 10.1385/1-59259-684-3:363

Subject: Neuroscience

References

Download References

1.	Sutherland, E. W. and Rall, T. W. (1958) Fractionation and characterization of a cyclic adenine ribonucleotide formed by tissue particles. J. Biol. Chem. 232, 1077–1091.

2.	Taussig, R. and Gilman, A. G. (1995) Mammalian membrane-bound adenylyl cyclases. J. Biol. Chem. 270, 1–4.

3.	Tang, W. J. and Hurley, J. H. (1998) Catalytic mechanism and regulation of mammalian adenylyl cyclases. Mol. Pharmacol. 54(2), 231–240.

4.	Taussig, R., Iniguez, L. J., and Gilman, A. G (1993) Inhibition of adenylyl cyclase by Gi alpha. Science 261, 218–221.

5.	Taussig, R., Tang, W. J., Hepler, J. R., and Gilman, A. G. (1994) Distinct patterns of bidirectional regulation of mammalian adenylyl cyclases. J. Biol. Chem. 269, 6093–6100.

6.	Sunahara, R. K., Dessauer, C. W., and Gilman, A. G (1996) Complexity and diversity of mammalian adenylyl cyclases. Annu. Rev. Pharmacol. Toxicol. 36, 461–480.

7.	Salomon, Y., Londos, C., and Rodbell, M. (1974) A highly sensitive adenylate cyclase assay. Anal. Biochem. 58, 541–548.

8.	Gilman, A. G. (1970) A protein binding assay for adenosine 3′∶5′-cyclic monophosphate. Proc. Natl. Acad. Sci. USA 67, 305–312.

9.	Nordstedt, C. and Fredholm, B. B. (1990) A modification of a protein-binding method for rapid quantification of cAMP in cell-culture supernatants and body fluid. Anal. Biochem. 189, 231–244.

10.	Steiner, A. L., Kipnis, D. M., Utiger, R., and Parker C. (1969) Radioimmunoassay for the measurement of adenosine 3′,5′-cyclic phosphate. Proc. Natl. Acad. Sci. USA 64, 367–373.

11.	Steiner, A. L., Parker, C. W., and Kipnis, D. M. (1972) Radioimmunoassay for cyclic nucleotides. I. Preparation of antibodies and iodinated cyclic nucleotides. J. Biol. Chem. 247, 1106–1113.

12.	Harper, J. F. and Brooker, G. (1975) Femtomole sensitive radioimmunoassay for cyclic AMP and cyclic GMP after 2′0 acetylation by acetic anhydride in aqueous solution. J. Cyclic Nucleotide Res 1, 207–218.

13.	Brooker, G., Harper, J. F., Terasaki, W. L., and Moylan, R. D. (1979) Radioimmunoassay of cyclic AMP and cyclic GMP. Adv. Cyclic Nucleotide Res. 10, 1–33.

Comments (Loading...)

Post comment/View all comments