Changes in post-translational modifications of prolactin during development and reproductive cycles in the chicken

Abstract Changes in proportion of glycosylated prolactin in the anterior pituitary glands of chickens were assessed using one- and two-dimensional western blotting analysis during the perihatch stage of embryos and reproductive cycles. Multiple isoforms of prolactin were detected by one-dimensional...

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Bibliographic Details
Published in:General and comparative endocrinology 2009-04, Vol.161 (2), p.238-245
Main Authors: Hiyama, Gen, Kansaku, Norio, Kinoshita, Mihoko, Sasanami, Tomohiro, Nakamura, Akihiro, Noda, Kenji, Tsukada, Akira, Shimada, Kiyoshi, Zadworny, David
Format: Article
Language:English
Subjects:
Animals
Blotting, Western
Chick Embryo
Chicken
Chickens - growth & development
Chickens - physiology
Electrophoresis, Gel, Two-Dimensional
Endocrinology & Metabolism
Female
Glycosylation
Isoform
Pituitary Gland, Anterior - metabolism
Prolactin
Prolactin - analogs & derivatives
Prolactin - metabolism
Protein Isoforms - metabolism
Protein Processing, Post-Translational - physiology
Radioimmunoassay
Sialylation
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Summary:Abstract Changes in proportion of glycosylated prolactin in the anterior pituitary glands of chickens were assessed using one- and two-dimensional western blotting analysis during the perihatch stage of embryos and reproductive cycles. Multiple isoforms of prolactin were detected by one-dimensional analysis and glycosylated (G) and non-glycosylated (NG) isoforms were identified by N -glycosidase and neuraminidase treatment. Increases of ratio of G to NG isoforms were observed in both embryonic stages and reproductive cycles by the one-dimensional analysis. Although a similar tendency of increase of proportion of G prolactin was obtained, different values of proportion were observed between one-dimensional and two-dimensional analysis. Since two-dimensional analysis may better resolve isoforms differing slightly in molecular size of G prolactin, the results from two-dimensional analysis may reflect the actual proportion of prolactin isoforms. Furthermore, isoforms differing in isoelectric points were detected after N -glycosidase and neuraminidase treatment. These results indicate that prolactin may also be additionally post-translationally modified such as by phosphorylation. Thus function and biological activity of prolactin were, at least in part, regulated by post-translational modification in the various physiological stages.
ISSN:0016-6480
1095-6840
DOI:10.1016/j.ygcen.2009.01.007