The hormonal control of protein N-glycosylation in the developing rabbit mammary gland and its effect upon transferrin synthesis and secretion.
Pregnant rabbit mammary gland explants cultured with insulin, prolactin and cortisol, synthesise and secrete transferrin radiolabelled with [3H]leucine or [3H]mannose. Omission of prolactin from the culture medium inhibited the incorporation of [3H]leucine into casein but not transferrin. Total transferrin secreted under these conditions was approx. 75% of the control (+prolactin) value measured by rocket immunoelectrophoresis. Little incorporation of [3H]mannose into transferrin was seen in the absence of prolactin suggesting a lack of glycosylation of the protein. Dual label experiments with [3H]mannose and [14C]leucine confirmed this. The decreased incorporation of [3H]mannose into dolichol linked intermediates suggests a general effect on protein N-glycosylation in the absence of prolactin. Thus, while the synthesis of the polypeptide backbone of transferrin does not require prolactin its glycosylation does.
D000818:Animals; D005260:Female; D006020:Glycopeptides / Q000032:analysis; D006023:Glycoproteins / Q000096:biosynthesis*; D006728:Hormones / Q000494:pharmacology*; D006854:Hydrocortisone / Q000494:pharmacology; D007328:Insulin / Q000494:pharmacology; D007930:Leucine / Q000378:metabolism; D008321:Mammary Glands, Animal / Q000378:metabolism*; D008358:Mannose / Q000378:metabolism; D008894:Milk Proteins / Q000096:biosynthesis*; D011388:Prolactin / Q000494:pharmacology; D011499:Protein Processing, Post-Translational; D011817:Rabbits; D014168:Transferrin / Q000096:biosynthesis* / Q000378:metabolism
D006020:Glycopeptides; D006023:Glycoproteins; D006728:Hormones; D007328:Insulin; D008894:Milk Proteins; D014168:Transferrin; D011388:Prolactin; D007930:Leucine; D008358:Mannose; D006854:Hydrocortisone