Galectin-1 binds mucin in human trophoblast

Mucins are multifunctional highly glycosylated proteins expressed by the female reproductive tract. Differential expression of MUC1 and MUC15 has been shown in trophoblast. This study was undertaken to establish the distribution of mucin(s) in cytotrophoblast cell cultures using anti-bovine submaxil...

Full description

Saved in:
Bibliographic Details
Published in:Histochemistry and cell biology 2014-11, Vol.142 (5), p.541-553
Main Authors: Bojic-trbojevic, Anka, Jovanovic Krivokuca, Milica, Kolundzic, Nikola, Petronijevic, Milos, Vrzic-petronijevic, Svetlana, Golubovic, Snezana, Vicovac, Ljiljana
Format: Article
Language:English
Subjects:
Binding sites
Biochemistry
Biomedical and Life Sciences
Biomedicine
Cell Biology
Cell culture
Cells, Cultured
Cellular biology
Developmental Biology
Galectin 1 - chemistry
Galectin 1 - metabolism
Humans
Immunohistochemistry
Mucins - chemistry
Mucins - metabolism
Original Paper
Protein Binding
Proteins
Trophoblasts - cytology
Trophoblasts - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Mucins are multifunctional highly glycosylated proteins expressed by the female reproductive tract. Differential expression of MUC1 and MUC15 has been shown in trophoblast. This study was undertaken to establish the distribution of mucin(s) in cytotrophoblast cell cultures using anti-bovine submaxillary mucin (BSM) and to investigate the possibility of MUC1/mucin(s) being a binding partner of trophoblast galectin-1. MUC1 is demonstrated here using immunocytochemistry on isolated cytotrophoblast and the HTR-8/SVneo extravillous trophoblast cell line but detection of additional trophoblast mucins cannot be excluded. Western blot analysis showed similar bands ranging from 30 to >200 kDa with anti-BSM and the well-known mucin antibodies HMFG1 and B72.3. Immunocytochemistry and cell-based ELISA data were found to support that all of the antibodies used are reactive with BSM, suggesting the presence of shared epitopes between BSM and trophoblast mucin(s). Binding of galectin-1 to trophoblast MUC1/mucin(s) was analyzed using a solid-phase assay and co-immunoprecipitation. Recombinant galectin-1 binding to isolated trophoblast mucin in solid-phase assay was sensitive to lactose, a carbohydrate inhibitor of galectin binding. In whole HTR-8/SVneo lysates, ~200 kDa mucin was detected in galectin-1 immunoprecipitates, while endogenous galectin-1 was present in BSM-immunoprecipitates. Furthermore, double fluorescence immunocytochemistry showed overlap of galectin-1 and trophoblast mucins at the plasma membrane of HTR-8/SVneo cells. These results suggest that trophoblast mucin(s) could act as binding partners of galectin-1, in a carbohydrate-dependent manner.
ISSN:0948-6143
1432-119X
DOI:10.1007/s00418-014-1229-7