PMID: 2125005Dec 10, 1990Paper

Hormone glycosylation required for lutropin receptor recognition in sheep testis

FEBS Letters
M R SairamT A Yarney

Abstract

The high affinity binding sites for ovine pituitary lutropin (oLH) present in DLS-1 sheep testis recognized only the fully glycosylated ovine or bovine hormone (bLH) in receptor binding assays using 125I-labeled oLH. Chemically deglycosylated (DG-) oLH or bLH which were fully active with other lutropin receptors (rat/pig) were completely inert in the DLS-1 receptor assay. In the same membranes, the FSH (follitropin) receptor reacted well with both glycosylated FSH and DG-oFSH. In recombination studies, lutropin formed by glycosylated native alpha- and beta-subunits of the hormone was fully active but when one of the subunits was in the deglycosylated form, receptor binding activity was greatly reduced. The presence of glycosylated alpha-subunit in the recombined hormone gave rise to 5x more activity than DG-alpha + beta. All these preparations were fully active in the rat/pig receptor assays for LH. These results demonstrate that lutropin hormone glycosylation is essential for optimum receptor recognition in the sheep testis, further emphasizing the importance of correct glycosylation in oLH alpha hormone function.

References

May 1, 1990·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·M R SairamG N Bhargavi
Jul 9, 1990·Molecular and Cellular Endocrinology·M P BernardW R Moyle
Jan 2, 1990·Molecular and Cellular Endocrinology·F LibertG Vassart
Oct 1, 1989·Molecular and Cellular Endocrinology·L Lamarre, M R Sairam
Jun 1, 1989·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·M R Sairam
Oct 1, 1988·Canadian Journal of Physiology and Pharmacology·T A YarneyM R Sairam

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