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Interactions between galectin-3 and integrinß3 in regulating endometrial cell proliferation and adhesion
Oleh:
Cai-Xia, Lei
;
Wei, Zhang
;
Jian-Ping, Zhou
;
Yin-Kun, Liu
Jenis:
Article from Journal - ilmiah internasional
Dalam koleksi:
Human Reproduction vol. 24 no. 11 (Nov. 2009)
,
page 2879-2889 .
Topik:
galectin-3
;
integrin
;
endometrial receptivity
;
proliferation
;
adhesion
Ketersediaan
Perpustakaan FK
Nomor Panggil:
H07.K.2009.04
Non-tandon:
1 (dapat dipinjam: 0)
Tandon:
tidak ada
Lihat Detail Induk
Isi artikel
BACKGROUND Galectin-3 (gal-3) is a ß-galactoside-binding protein which can be detected in endometrium. The study was designed to investigate synergism of gal-3 and integrinß3 in endometrial cell proliferation and adhesion in an in vitro model of endometrial receptivity. METHODS The RL95-2 cell line was employed as an in vitro model for receptive endometrium. Cells transfected with gal-3 siRNA or treated with exogenous gal-3 were incubated with or without function-blocking integrinß1/3 antibody for evaluating synergism of gal-3 and integrins on cell proliferation and adhesion. Proliferation was measured by BrdU incorporation, and adhesion to fibronectin (FN) was determined by an adhesion assay. Integrin expression was analyzed by Flow Cytometry and western blots. Bewo spheroids were co-cultured with the RL95-2 monolayer to mimic the blastocyst–endometrial interaction, and colocalization of gal-3, integrinß3 and FN at the interface was observed by confocal microscopy. RESULTS The knock-down of gal-3 inhibited RL95-2 cell proliferation and adhesion. However, a reduction of proliferation and adhesion was also observed in presence of exogenous gal-3, and this was further reduced by a functional block to integrinß3. Moreover, gal-3 knock-down significantly increased integrinß3 expression, however, the colocalization of integrinß3 and FN was not increased. As expected, the colocalization of integrinß3 was decreased with the knock-down of gal-3. CONCLUSIONS This study has provided an in vitro model for the complex interactions between gal-3 and integrinß3 in the regulation of endometrial cell proliferation and adhesion.
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