Demonstration of specific "high affinity" binding sites for [3H] imipramine on human platelets

Steven M. Paul, Moshe Rehavi, Phil Skolnick, Frederick K. Goodwin

Research output: Contribution to journalArticlepeer-review

202 Scopus citations


High affinity and saturable binding sites for [3H] imipramine have been demonstrated on human platelet membranes. These binding sites appear to be specific for tricyclic antidepressants and their pharmacologically-active metabolites. In contrast, inactive tricyclic compounds such as the parent iminodibenzyl and iminostilbenes do not inhibit [3H] imipramine binding. The binding of [3H] imipramine to human platelets is of high affinity (Kd {reversed tilde equals} 1.4nM), saturable (Bmax {reversed tilde equals} 625 fmols/mg prot), and sensitive to proteolytic degradation. The effects of various drugs and neurotransmitter agonists and antagonists suggests that these binding sites are pharmacologically distinct from the previously reported binding of tricyclic antidepressants to alpha-adrenergic, muscarinic-cholinergic, and histaminergic receptors. The binding characteristics of [3H] imipramine to platelets is similar to that in rat and human brain and may thus serve as a useful model in elucidating the pharmacological and physiological significance of these binding sites.

Original languageEnglish
Pages (from-to)953-959
Number of pages7
JournalLife Sciences
Issue number12
StatePublished - Mar 24 1980


Dive into the research topics of 'Demonstration of specific "high affinity" binding sites for [3H] imipramine on human platelets'. Together they form a unique fingerprint.

Cite this