ABSTRACT
The specific binding of [3H]-dexamethasone to glucocoticoid receptor (GR) and activation of hormone-receptor (H-R) complexes from the liver of chicken at day 0, 5, 10, 30, 60 and 90 were investigated to find out GR regulation during postnatal development. Results showed that GR level (fmol/mg protein) reached a peak by day 5 of postnatal age and was significantly higher (+ 42%) than observed at day-0 (day of hatching), as evidenced also by protein blot experiments and Scatchard analysis of binding data. The GR concentration declined gradually up to day 30, and thereafter, no significant change was observed at day 60 and 90 of postnatal ages. The temperature and salt-dependent activation of GR showed no significant differences in 0 and 30-day old chicken, as determined by DNA-cellulose binding assay. However, nuclear binding of temperature and salt-activated GR complexes was significantly higher in 0-day old chicken. Cross-mixing experiments (wherein nuclei of day-0 were incubated with the H-R complexes of day-30 and vice-versa) revealed the role of nuclear specificity in higher binding of temperature and salt-activated H-R complexes at day-0 of postnatal age. DNase I extraction of nuclei bound to activated H-R complexes showed higher extractability at day-0 (70%), compared to day-30 (44%). Above findings suggested that changes in GR concentration as well as chromatin organization might play an important role in glucocorticoid-mediated responses during postnatal development of chicken.