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Some pharmacological and biochemical interactions of the enantiomers of adenylyl 5′‐(β, γ‐methylene)‐diphosphonate with the guinea‐pig urinary bladder
Author(s) -
Cusack N.J.,
Hourani S.M.O.
Publication year - 1984
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1984.tb16453.x
Subject(s) - adenosine , guinea pig , adenosine triphosphate , chemistry , biochemistry , endocrinology , biology
1 Adenosine 5′‐triphosphate (ATP) and adenylyl 5′‐(β,γ methylene)‐diphosphonate (AMP‐PCP) both contracted the guinea‐pig urinary bladder, but the response to AMP‐PCP was much greater. We synthesized the enantiomer of AMP‐PCP, L‐adenylyl 5′‐(β,γ‐methylene)‐diphosphonate ( L ‐AMP‐PCP), and tested it on the guinea‐pig bladder. 2 L ‐AMP‐PCP contracted the guinea‐pig bladder, and was more potent than AMP‐PCP and much more potent than ATP. The potential breakdown product of L ‐AMP‐PCP, L ‐adenosine, unlike adenosine (the breakdown product of AMP‐PCP), did not inhibit contractions of the guinea‐pig bladder. 3 ATP and its enantiomer L ‐adenosine 5′‐triphosphate ( L ‐ATP) were rapidly degraded by the muscle, and AMP‐PCP was also degraded, but more slowly. L ‐AMP‐PCP, however, was completely resistant to degradation. 4 L ‐AMP‐PCP would appear to be a useful ATP analogue, as it is potent and resistant to degradation, and its potential breakdown product, L ‐adenosine, is inactive.