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Journal of Clinical Endocrinology & Metabolism Vol. 44, No. 1 62-68
doi:10.1210/jcem-44-1-62
Copyright © 1977 by the Endocrine Society.
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Observations Concerning the Binding of L-Triiodothyronine in the Human Polymorphonuclear Leukocyte

KENNETH A. WOEBER and BETTY A. MADDUX, Technical Assistant

Department of Medicine, Mount Zion Hospital and Medical Center and University of California San Francisco, California 94120

To examine the subcellular locus of L-triiodothyronine (T3) binding in the human polymorphonuclear leukocyte, intact leukocytes (>90% polymorphonuclear) were incubated with small tracer concentrations of [125I]T3 with or without an excess of non-radioactive T3. Measurement of the [125I]T3 content of several subcellular fractions revealed that the non-radioactive T3 had led to significant displacement of [125I]T3 from the nuclear fraction alone. After correction for degradation and non-specific binding of the added T3 in intact leukocytes from hypothyroid patients in which the endogenous T3 concentration would be minimal, the T3-nuclear binding interaction was found to have an equilibrium dissociation constant of 1.1 x 10-I0M and a binding capacity of 4.3 fmol/1 x 107 cells. Pre-incubation of intact cells with non-radioactive T3 did not increase the subsequent specific binding of [125I]T3 by the nuclei isolated therefrom. The data indicate that: 1) the human polymorphonuclear leukocyte possesses saturable nuclear binding sites for T3, and 2) the sites appear to bind T3 without the intermediation of a cytosol receptor.

Supported in part by research grants AM-17825 and AM-19081 from the National Institutes of Health, Bethesda, Maryland.

Received August 14, 1975.






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Copyright © 1977 by The Endocrine Society