Evidence for the Existence of Two Prolactin Isoforms in the Developing Pituitary Gland of the Goose (Anser cygnoides)

Abstract

Compared to Galliformes such as chicken and turkey, very little is known about the existence and expression of isoforms of prolactin (PRL) in the pituitary glands of Anseriformes. In this study, by generating a rabbit-anti-goose (Anser cygnoides) PRL polyclonal antibody, we analysed the expression patterns of goose PRL isoforms in the embryonic and post-hatch development of the pituitary gland. Our results showed that two immunoreactive bands with molecular weights of about 23 and 26 kDa were detected using the Western blot technique, corresponding to the non-glycosylated (NG-) and the glycosylated (G-) isoform of PRL, respectively. The protein levels of the total PRL in a goose increased gradually from the embryonic day (ED) 22 to the post-hatch day (PD) 28, with a non-significant decrease on PD6. Furthermore, the percentage of G-PRL in the pituitary gland of the goose fluctuated from about 30.3% to 54.7% throughout the embryonic and post-hatch development. At the mRNA level, the expression of PRL increased steadily during the development and reached the highest levels on PD12, but later showed a non-significant decrease on PD28. The inconsistent expression patterns between the PRL mRNA and protein during the stages from PD6 to PD28 indicated that the PRL gene expression involves both transcriptional and post-translational regulation. Taken together, our data unequivocally demonstrated the existence of NG- and G-PRL in the pituitary gland of a goose and that the expression of the total PRL as well as the percentage of G-PRL significantly changed during embryonic and post-hatch development, indicating that the versatile biological functions of PRL during the ontogenesis of a goose could be closely related to changes in both its total expression and the degree of glycosylation in the pituitary gland.