help button home button Endocrine Society Endocrinology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Request Copyright Permission
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Galton, V. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Galton, V. A.

Endocrinology, Vol 106, 859-866, Copyright © 1980 by Endocrine Society


ARTICLES

Binding of thyroid hormones in vivo by hepatic nuclei of Rana catesbeiana tadpoles

VA Galton

Thyroid hormone is essential for amphibian metamorphosis, and tadpoles develop responsiveness to exogenous T4 and T3 during the premetamorphic stage of development. The present studies were performed to investigate the receptors concerned with the initiation of this response. Premetamorphic tadpoles (stages VII-XV of Taylor and Kollros) were injected ip with [125I]T3 or [125I]T4 (0.001-10 nmol/tadpole). Twenty- four hours later, liver and serum were obtained, and organic 125I in liver nuclei and serum (shown to be unchanged hormone) was measured. Saturable binding sites for both T3 and T4 were present in the liver nuclei. Analysis of binding data indicated for T3 a mean value for Kd of 1.6 x 10(-12) M (moles of free T3 per liter plasma) and a mean value for maximum binding capacity of 0.1 ng/mg DNA. For T4, the mean Kd was 3.9 x 10(-15 M, and the mean maximum binding capacity was 0.5 ng/mg DNA. It was estimated that a significant fraction of these sites was not normally occupied by endogenous hormone. Properties of the T3- binding sites were similar in tadpoles at stages X and XV. Stable T4 and the acetic and propionic acid analogs of T3 competed with [125I]T3 for the sites almost as readily as did stable T3. The acetic acid analog of T4, D-T4, 3,5-diiodothyronine, and rT3, less active analogs, were relatively poor competitors. Binding of T3 to saturable but not to non-saturable nuclear binding sites was reduced in tadpoles kept at 4 C. On the basis of these findings, it is suggested that these nuclear binding sites are thyroid hormone receptors.


This article has been cited by other articles:


Home page
EndocrinologyHome page
T. Murata and K. Yamauchi
Low-Temperature Arrest of the Triiodothyronine-Dependent Transcription in Rana catesbeiana Red Blood Cells
Endocrinology, January 1, 2005; 146(1): 256 - 264.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Endocrinology Endocrine Reviews J. Clin. End. & Metab.
Molecular Endocrinology Recent Prog. Horm. Res. All Endocrine Journals
Copyright © 1980 by The Endocrine Society