Selective activation of the N-glycosylation apparatus in uteri by estrogen

Daniel D. Carson, J. David Farrar, Jana Laidlaw, David A. Wright

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Abstract

Estrogen rapidly, preferentially and markedly enhances the rate of N-linked glycoprotein synthesis in mouse uteri. In contrast, the rate of glycoprotein turnover is unaffected by the hormone. Estrogen's effect on the expression of mRNA coding for glycoproteins was studied using an in vitro translation-glycosylation system as well as by Northern/slot blot analyses. Both approaches indicated that estrogen did not have a preferential stimulatory effect on the general expression of glycoprotein mRNA. Neither was there a significant change in the relative levels of specific mRNA coding for several N-linked glycoproteins, i.e. laminin B1 and B2, fibronectin, and uvomorulin, as a function of estrogen treatment. Immunoprecipitation studies also demonstrated no change in the relative rates of synthesis of the corresponding core proteins for laminin or fibronectin. Taken together, these results suggested that estrogen primarily stimulated glycoprotein synthesis by stimulating the glycosylation apparatus, and not by increasing synthesis of protein acceptors. Previous studies have indicated that of a variety of potential regulatory points in the pathway of N-linked glycoprotein assembly, only expression of mannosylphosphoryldolichol synthase (MPDS) increases sufficiently to account for the increase in glycoprotein expression observed in response to estrogen. Consistent with these observations, it was found that injection of uterine poly(A+) RNA from estrogen-treated uteri into Xenopus oocytes markedly stimulated MPDS activity in the oocytes. In contrast, injection of RNA from non-estrogen-treated uteri did not stimulate MPDS activity in oocytes. Collectively, these results indicate that steroid hormones can modulate glycoprotein expression by preferentially stimulating the glycosylation apparatus. Nonetheless, one of estrogen's effects on the glycosylation apparatus, induction of MPDS activity, appears to occur at a transcriptional level.

Original languageEnglish (US)
Pages (from-to)2947-2955
Number of pages9
JournalJournal of Biological Chemistry
Volume265
Issue number5
StatePublished - 1990

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Glycosylation
Uterus
Glycoproteins
Estrogens
Chemical activation
Oocytes
Messenger RNA
Laminin
Fibronectins
Steroid hormones
Hormones
Injections
Cadherins
Xenopus
Immunoprecipitation
Northern Blotting
Proteins
Steroids
RNA

ASJC Scopus subject areas

  • Biochemistry

Cite this

Selective activation of the N-glycosylation apparatus in uteri by estrogen. / Carson, Daniel D.; David Farrar, J.; Laidlaw, Jana; Wright, David A.

In: Journal of Biological Chemistry, Vol. 265, No. 5, 1990, p. 2947-2955.

Research output: Contribution to journalArticle

Carson, Daniel D. ; David Farrar, J. ; Laidlaw, Jana ; Wright, David A. / Selective activation of the N-glycosylation apparatus in uteri by estrogen. In: Journal of Biological Chemistry. 1990 ; Vol. 265, No. 5. pp. 2947-2955.
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