Elsevier

Life Sciences

Volume 21, Issue 9, 1 November 1977, Pages 1343-1349
Life Sciences

Coronary vasoactivity of adenosine covalently linked to polylysine

https://doi.org/10.1016/0024-3205(77)90017-0Get rights and content

Abstract

Adenosine was covalently linke to polylysine nonapeptide by reacting adenosine-5-carboxaldehyde with polylysine at pH 9.5, then reducing the Schiff base with NaBH4. The product (PLADO), which contained an average of two adenosine residues per molecule, did not penetrate cell membranes. When administered to two conscious instrumented dogs PLADO caused maximum coronary vasodilation at a concentration of 4 μM in coronary plasma water. This coronary vasodilatory effect was antagonized by aminophylline. Thus, after the administration of this methylxanthine coronary conductance increased by only 46% of maximum at a PLADO concentration of 6.9 μM. This result confirms earlier work using adenosine coupled to oxidized oligosaccharides that indicates the possibility of adenosine receptors on the surface of coronary myocytes.

References (12)

  • E. Layne
  • R.M. Berne

    Am. J. Physiol.

    (1963)
  • J. Scholtholt et al.

    Arzniem.-Forsch.

    (1972)
  • L.B. Corbin et al.

    Brit. J. Pharmacol.

    (1974)
  • R.A. Olsson et al.

    Prog. Molec. Subcell. Biol.

    (1976)
  • R.A. Olsson et al.

    Circ. Res.

    (1976)
There are more references available in the full text version of this article.

Cited by (15)

  • Photoaffinity labels as pharmacological tools

    1984, Biochemical Pharmacology
View all citing articles on Scopus

In conducting the research described in this report, the investigators adhered to the “Guide for Laboratory Animal Facilities and Care,” as promulgated by the Committee on the Guide for Laboratory Animal Facilities and Care of the Institute of Laboratory Animal Resources, National Academy of Sciences - National Research Council.

View full text