Galectin-7 acts as an adhesion molecule during implantation and increased expression is associated with miscarriage

Menkhorst, Ellen; Gamage, Thilini; Cuman, Carly; Kaitu’u-Lino, Tu’uhevaha J; Tong, Stephen

doi:10.1016/j.placenta.2014.01.004

Cited by 29 publications

(31 citation statements)

References 39 publications

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“…To mimic the rising levels of galectin-7 determined in EC, EC cell lines were treated with recombinant galectin-7 for the in vitro functional assays. The concentration used (1 µg/ml) was determined from the manufacturer's protocols and dose-response trials in previous studies (14,15), but it is notable that extracellular galectin-7 remains to be identified in EC. Galectin-7 could not be detected in the endometrial epithelial EC cell line conditioned media (data not shown).…”

Section: Discussionmentioning

confidence: 99%

“…no. ELH-Galectin7-001; RayBiotech, Inc., Norcross, GA, USA), according to the manufacturer's protocols (15,23). For the cell lines, cells were cultured in serum-free media for 48 h prior to cell lysate being collected for the ELISA.…”

Section: Methodsmentioning

confidence: 99%

“…Additionally, it accelerates the re-epithelialization of corneal wounds more efficiently than the majority of known growth factors (12,13). In the uterus, galectin-7 promotes wound repair following menstruation (14) and elevated endometrial epithelial galectin-7 is associated with miscarriage, possibly due to its role as an anti-adhesion molecule during implantation (15).…”

Section: Introductionmentioning

confidence: 99%

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Galectin‑7 is elevated in endometrioid (type I) endometrial cancer and promotes cell migration

et al. 2018

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Endometrial cancer (EC) is the most commonly diagnosed gynecological malignancy in Australian women. Notably, its incidence and mortality rate is increasing. Despite this, there are limited treatment options for EC. Galectin-7 regulates tumorigenesis in numerous epithelial cancer types, but the role of galectin-7 has not been investigated in EC. It was hypothesized that galectin-7 expression would be altered in EC and contribute to the development of EC. Galectin-7 levels in EC and benign endometrium were quantified by reverse transcription-quantitative polymerase chain reaction (RT-qPCR) and ELISA. The effect of recombinant galectin-7 (1 µg/ml) on cell adhesion, proliferation, apoptosis (xCELLigence and flow cytometry), migration (wound healing assay) and gene expression (RT-qPCR) was investigated using three human EC cell lines (Ishikawa, HEC1A and AN3CA). Galectin-7 gene and protein expression was significantly elevated in Grade 3 EC, compared with benign tissues. Galectin-7 was almost undetectable in Ishikawa and AN3CA cells, but highly expressed by HEC1A cells. Recombinant galectin-7 had no significant effect on cell proliferation or apoptosis in any cell line, but significantly reduced cell adhesion in Ishikawa (at 4 and 6 h) and AN3CA (at 2, 3, 4 and 6 h). Galectin-7 significantly promoted Ishikawa migration and significantly elevated collagen type IV α 1 chain and intercellular adhesion molecule 1 (ICAM1) gene expression during wound healing. The present study demonstrated that galectin-7 production increased in EC with increasing cancer grade; therefore, galectin-7 may promote the metastasis of EC by reducing cell-cell adhesion and enhancing cell migration.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Galectin‑7 is elevated in endometrioid (type I) endometrial cancer and promotes cell migration

et al. 2018

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“…It can be found in female reproductive system (35) and its expression changes in some cancers of the reproductive tract, including that of the ovary and uterus. Endometrial epithelium can produce galectin-7 and women with a history of miscarriage have abnormally elevated levels of galectin-7 in the endometrium (42). GalNAc-T6 is one of the members of the UDP-N-acetylalpha-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase family of enzymes.…”

Section: Discussionmentioning

confidence: 99%

A Human Lectin Microarray for Sperm Surface Glycosylation Analysis

Sun

Cheng

et al. 2016

Molecular & Cellular Proteomics

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Glycosylation is one of the most abundant and functionally important protein post-translational modifications. As such, technology for efficient glycosylation analysis is in high demand. Lectin microarrays are a powerful tool for such investigations and have been successfully applied for a variety of glycobiological studies. However, most of the current lectin microarrays are primarily constructed from plant lectins, which are not well suited for studies of human glycosylation because of the extreme complexity of human glycans. Herein, we constructed a human lectin microarray with 60 human lectin and lectin-like proteins. All of the lectins and lectin-like proteins were purified from yeast, and most showed binding to human glycans. To demonstrate the applicability of the human lectin microarray, human sperm were probed on the microarray and strong bindings were observed for several lectins, including galectin-1, 7, 8, GalNAc-T6, and ERGIC-53 (LMAN1). These bindings were validated by flow cytometry and fluorescence immunostaining. Further, mass spectrometry analysis showed that galectin-1 binds several membrane-associated proteins including heat shock protein 90. Finally, functional assays showed that binding of galectin-8 could significantly enhance the acrosome reaction within human sperms. To our knowledge, this is the first construction of a human lectin microarray, and we anticipate it will find wide use for a range of human or mammalian studies, alone or in combination with plant lectin microarrays. Molecular & Cellular

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“…In addition, elevated galectin-7 expression is associated with uterine repair after menstruation (Evans et al 2014 ), miscarriage (Menkhorst et al 2014b ), and preeclampsia (Menkhorst et al 2014a ). Many of these observations relate to the proposed role for galectin-7 in reepithelialization associated with wound repair (Panjwani 2014 ).…”

Section: Galectinsmentioning

confidence: 99%

Regulation of Implantation and Establishment of Pregnancy in Mammals

Geisert¹,

Bazer²

2015

Advances in Anatomy, Embryology and Cell Biology

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Advances in Anatomy, Embryology and Cell Biology publishes critical reviews and state-of-the-art surveys on all aspects of anatomy and of developmental, cellular and molecular biology, with a special emphasis on biomedical and translational topics.The series publishes volumes in two different formats:• Contributed volumes, each collecting 5 to 15 focused reviews written by leading experts • Single-authored or multi-authored monographs, providing a comprehensive overview of their topic of research

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Galectin-7 acts as an adhesion molecule during implantation and increased expression is associated with miscarriage

Cited by 29 publications

References 39 publications

Galectin‑7 is elevated in endometrioid (type I) endometrial cancer and promotes cell migration

Galectin‑7 is elevated in endometrioid (type I) endometrial cancer and promotes cell migration

A Human Lectin Microarray for Sperm Surface Glycosylation Analysis

Regulation of Implantation and Establishment of Pregnancy in Mammals

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