The Loss of Luteal Progesterone Production in Women Is Associated With a Galectin Switch via alpha 2,6-Sialylation of Glycoconjugates

• Nio-Kobayashi, Junko

• Boswell, Lyndsey

• Amano, Maho

• Iwanaga, Toshihiko

• Duncan, W. Colin

抄録

Context: Luteal progesterone is fundamental for reproduction, but the molecular regulation of the corpus luteum (CL) in women remains unclear. Galectin-1 and galectin-3 bind to the sugar chains on cells to control key biological processes including cell function and fate. Methods: The expression and localization of LGALS1 and LGALS3 were analyzed by quantitative PCR and histochemical analysis, with special reference to alpha 2,6-sialylation of glycoconjugates in carefully dated human CL collected across the menstrual cycle and after exposure to human chorionic gonadotrophin (hCG) in vivo. The effects of hCG and prostaglandin E-2 on the expression of galectins and an alpha 2,6-sialyltransferase 1 (ST6GAL1) in granulosa lutein cells were analyzed in vitro. Results: Galectin-1 was predominantly localized to healthy granulosa lutein cells and galectin-3 was localized to macrophages and regressing granulosa lutein cells. Acute exposure to luteotrophic hormones (hCG and prostaglandin E2) up-regulated LGALS1 expression (P < .001). ST6GAL1, which catalyzes alpha 2,6-sialylation to block galectin-1 binding, increased during luteolysis (P < .05) as did LGALS3 (P < .05). Luteotrophic hormones reduced ST6GAL1 and LGALS3 in vivo (P < .05) and in vitro (P < .001). There was an inverse correlation between the expression of ST6GAL1 and HSD3B1 (P < .01) and a distinct cellular relationship among alpha 2,6-sialylation, 3 beta-hydroxysteroid dehydrogenase, and galectin expression. Conclusions: Galectin-1 is a luteotrophic factor whose binding is inhibited by alpha 2,6-sialylation in the human CL during luteolysis. ST6GAL1 and galectin-3 expression is increased during luteolysis and associated with a loss of progesterone synthesis. Luteotrophic hormones differentially regulate galectin-1 and galectin-3/alpha 2,6-sialylation in granulosa lutein cells, suggesting a novel galectin switch regulated by luteotrophic stimuli during luteolysis and luteal rescue.

収録刊行物

• Journal of clinical endocrinology & metabolism

  Journal of clinical endocrinology & metabolism 99 (12), 4616-4624, 2014-12

  Endocrine Society

詳細情報

• CRID: 1050001339018024704
• NII論文ID: 120005553690
• HANDLE: 2115/58031
• ISSN: 0021972X
• 本文言語コード: en
• 資料種別: journal article
• データソース種別:
  • IRDB
  • CiNii Articles