Glycosylation selectively alters the biological activity of prolactin.
We have undertaken studies to determine the effect of glycosylation on the lactogenic activity of ovine PRL (oPRL). Measuring casein production in the in vitro mouse mammary gland explant assay, we found that glycosylated oPRL had 80% of the activity of oPRL. In competitive binding studies using lactogen receptors from mammary glands of lactating rabbits, glycosylated oPRL had only 20% the potency of oPRL. In the Nb2 assay also, glycosylated oPRL was approximately 24% as potent as oPRL in stimulating mitogenic activity. Thus, these studies show that the glycosylated variant of PRL has less biological activity than the major PRL form and that the alteration of an activity by glycosylation is selective.
Markoff
E
E
Lutcher Brown Department of Biochemistry, Whittier Institute for Diabetes and Endocrinology, La Jolla, California 92037.
Sigel
M B
MB
Lacour
N
N
Seavey
B K
BK
Friesen
H G
HG
Lewis
U J
UJ
D000818:Animals; D001667:Binding, Competitive; D002364:Caseins / Q000096:biosynthesis*; D005260:Female; D007700:Kinetics; D008321:Mammary Glands, Animal / Q000187:drug effects / Q000502:physiology*; D051379:Mice; D009924:Organ Culture Techniques; D011388:Prolactin / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology*; D011817:Rabbits; D011981:Receptors, Prolactin / Q000378:metabolism*; D012756:Sheep
D002364:Caseins; D011981:Receptors, Prolactin; C043928:prolactin, glycosylated; D011388:Prolactin