Abstract
Catecholamines bound covalently to glass beads have been found to have biological activity in several systems. Experimental evidence has been found that immobilized epinephrine and isoproterenol accelerate the heart rate in dogs, chick embryo, and chick heart cells grown in culture, whereas immobilized propranolol results in a decrease in heart rate. Isoproterenol bound to glass beads has also been shown to markedly increase the level of adenosine 3′:5′-cyclic monophosphoric acid in glial cells. The effects of the immobilized catecholamines are of longer duration than when the compounds are administered in solution. The present data indicate that the compounds are exerting their action when bound to the beads.
Keywords: cyclic AMP, tissue culture, immobilized catecholamines, canine hearts
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- Benda P., Lightbody J., Sato G., Levine L., Sweet W. Differentiated rat glial cell strain in tissue culture. Science. 1968 Jul 26;161(3839):370–371. doi: 10.1126/science.161.3839.370. [DOI] [PubMed] [Google Scholar]
- DeHann R. L. Regulation of spontaneous activity and growth of embryonic chick heart cells in tissue culture. Dev Biol. 1967 Sep;16(3):216–249. doi: 10.1016/0012-1606(67)90025-5. [DOI] [PubMed] [Google Scholar]
- Gilman A. G., Nirenberg M. Effect of catecholamines on the adenosine 3':5'-cyclic monophosphate concentrations of clonal satellite cells of neurons. Proc Natl Acad Sci U S A. 1971 Sep;68(9):2165–2168. doi: 10.1073/pnas.68.9.2165. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Halle W., Wollenberger A. Differentiation and behavior of isolated embryonic and neonatal heart cells in a chemically defined medium. Am J Cardiol. 1970 Mar;25(3):292–299. doi: 10.1016/s0002-9149(70)80006-6. [DOI] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Oka T., Topper Y. J. Insulin-sepharose and the dynamics of insulin action. Proc Natl Acad Sci U S A. 1971 Sep;68(9):2066–2068. doi: 10.1073/pnas.68.9.2066. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Renaud D., Le Douarin G. Sensibilité à l'adrénaline du tissu myocardique différencié in vitro à partir du mésoderme précardiaque. Annee Biol. 1970 May-Jun;9(5):325–334. [PubMed] [Google Scholar]
- Schimmer B. P., Ueda K., Sato G. H. Site of action of adrenocorticotropic hormone (ACTH) in adrenal cell cultures. Biochem Biophys Res Commun. 1968 Sep 6;32(5):806–810. doi: 10.1016/0006-291x(68)90312-4. [DOI] [PubMed] [Google Scholar]
- Wastila W. B., Stull J. T., Mayer S. E., Walsh D. A. Measurement of cyclic 3',5'-denosine monophosphate by the activation of skeletal muscle protein kinase. J Biol Chem. 1971 Apr 10;246(7):1996–2003. [PubMed] [Google Scholar]
- Weetall H. H. Trypsin and papain covalently coupled to porous glass: preparation and characterization. Science. 1969 Oct 31;166(3905):615–617. doi: 10.1126/science.166.3905.615. [DOI] [PubMed] [Google Scholar]
- Weibel M. K., Weetall H. H., Bright H. J. Insolubilized coenzymes: the covalent coupling of enzymatically active NAD to glass surfaces. Biochem Biophys Res Commun. 1971 Jul 16;44(2):347–352. doi: 10.1016/0006-291x(71)90606-1. [DOI] [PubMed] [Google Scholar]