Reconstitution of 5-hydroxytryptamine transport from cholate-disrupted platelet plasma membrane vesicles

Abstract
The bile acid cholate disrupted [human] platelet plasma membrane vesicles and inactivated 5-hydroxytryptamine transport activity. The transporter appeared not to be solubilized by this procedure, but remained associated with a high MW aggregate. Merely removing cholate did not restore the vesicular structure or transport activity, but in the presence of added soybean phospholipids, cholate removal generated proteoliposomes which accumulated 5-hydroxytryptamine. This reconstituted transport activity was similar in its ionic requirements and inhibitor sensitivity to transport in native membrane vesicles and intact platelets.