Format

Send to

Choose Destination
Zoolog Sci. 2012 Feb;29(2):79-82. doi: 10.2108/zsj.29.79.

Binding properties of thyroxine to nuclear extract from sea urchin larvae.

Author information

1
Graduate School of Science and Engineering, Saitama University, Saitama, Japan.

Abstract

We previously reported that thyroid hormones are involved in the formation of the adult rudiment and adult-type skeleton in sea urchin larvae, as well as in the resorption of larval tissues. In the present study, to search for the presence of thyroid hormone receptor in sea urchin larvae, we performed a ligand-binding assay between radiolabeled thyroid hormones and nuclear extracts from the larvae of the sea urchin Hemicentrotus pulcherrimus. The presence of binding sites with a high affinity to thyroxine (T4) was detected in the nuclear extract, but not in the cytoplasmic fraction. The dissociation constants for the T4 binding to the nuclear extracts were estimated to be about 18 pM from the mesenchyme-blastula stage to the four-armed pluteus stage. The quantity of T4 binding sites in the nuclear extracts increased during larval development. These results suggest that the binding affinity to T4 in the nuclear extracts was caused by a putative nuclear thyroid hormone receptor in sea urchin larvae.

PMID:
22303847
DOI:
10.2108/zsj.29.79
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for BioOne
Loading ...
Support Center