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. 1973 Apr;70(4):1099–1103. doi: 10.1073/pnas.70.4.1099

Adenosine 3′:5′-Cyclic Monophosphate in Chlamydomonas reinhardtii: Isolation and Characterization

Nikolaus Amrhein 1,*, Philip Filner 1
PMCID: PMC433434  PMID: 16592076

Abstract

Chlamydomonas reinhardtii contains a factor that can replace adenosine 3′:5′-cyclic monophosphate (cAMP) in the stimulation of rabbit-muscle protein kinase. The factor cochromatographs and coelectrophoreses with authentic cAMP, and is inactivated by beef heart cyclic nucleotide phosphodiesterase. When C. reinhardtii is exposed to aminophylline (theophylline2 ethylenediamine), the concentration of the factor in the cells increases within 1 hr, from about 25 pmol of cAMP equivalents per g dry weight to more than 250 pmol. Cyclic nucleotide phosphodiesterase activity is present in crude extract of C. reinhardtii and is inhibited by theophylline. We conclude that cAMP occurs in C. reinhardtii and that the endogenous concentration is governed at least in part by a theophylline-sensitive cyclic nucleotide phosphodiesterase. These findings provide a sound basis for attributing the effects of methylxanthines on flagellar function and regeneration in C. reinhardtii to the resultant elevation of endogenous cAMP.

Keywords: protein kinase assay, aminophylline, cyclic nucleotide phosphodiesterase

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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