z-logo
Premium
AN ACTION OF ERYTHROMYCIN IN THE INTESTINE THAT IS NOT MEDIATED VIA MOTILIN RECEPTORS
Author(s) -
Furness JB,
Clark MJ,
Wright T,
Bertrand PP,
Bornstein JC,
Verlinden M
Publication year - 1999
Publication title -
clinical and experimental pharmacology and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.752
H-Index - 103
eISSN - 1440-1681
pISSN - 0305-1870
DOI - 10.1046/j.1440-1681.1999.03002.x
Subject(s) - motilin , erythromycin , endocrinology , medicine , receptor , ileum , guinea pig , chemistry , jejunum , muscle contraction , biology , pharmacology , biochemistry , antibiotics
1. Erythromycin lactobionate caused a concentration‐ dependent inhibition of nerve‐mediated contractions of the longitudinal muscle of the guinea‐pig ileum, with a threshold for effect of 10–30 μmol/L. The non‐antibiotic derivative of erythromycin ABT‐229 had a similar effect, but was approximately 10‐fold less potent. At a greater concentration (1 mmol/L), erythromycin also depressed the direct contractile effect of 10 μmol/L carbachol on the muscle. 2. Human/porcine motilin (up to 100 μmol/L) did not reduce the nerve‐mediated contractions, although it did contract the muscle (threshold 30 μmol/L). Antagonists of motilin receptors (phe 3 leu 13 motilin, up to 1 μmol/L, and GM‐109, up to 3 μmol/L) did not reduce responses to erythromycin. 3. Erythromycin contracted the longitudinal muscle of the rabbit duodenum, with a threshold concentration of 0.1 μmol/L and ABT‐229 contracted this tissue at a threshold concentration of 0.01 μmol/L. Effects of both agonists were antagonized by the motilin receptor antagonists phe 3 leu 13 motilin (0.3 μmol/L) and GM‐109 (1 μmol/L). 4. It is concluded that the site(s) at which erythromycin acts in the guinea‐pig ileum is not a motilin receptor and that ABT‐229 is selective for the motilin receptor in comparison with non‐motilin erythromycin sites and is unlikely to act at the latter site in therapeutic doses.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here