RADIOIODINATED ESTROGEN DERIVATIVES

  • 1 January 1980
    • journal article
    • research article
    • Vol. 21  (2) , 142-146
Abstract
Monoiodohexestrol exhibits 10-15% specific binding to the 8S estrogen receptor while the remainder binds to nonreceptor 4S proteins. Reduction of nonreceptor binding with thyroxine or 8-anilino-1-naphthalene sulfonic acid was not quantitative. Thus no accurate determination of the concentration of receptor sites in the radioreceptor assay was possible by graphical analysis. 17.alpha.-[125I]iodoethynylestradiol and 17.alpha.-[125I]iodoethynyl-11.beta.-methoxy estradiol were synthesized at high specific activity. Although the iodoethynyl derivatives were stable under synthetic conditions, deiodination in the presence of proteins is too fast to allow in vivo or in vitro use. To make these compounds clinically useful, chemical modification to reduce nonreceptor binding and the rate of dehalogenation must be undertaken. [A radioiodinated tracer for the hormone estradiol may provide a scanning agent to visualize human estrogen-dependent tissues by binding to estrogen receptors, especially breast tumors.].

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