Molecular Human Reproduction, Vol. 6, No. 2, 170-177,
February 2000
© 2000 European Society of Human Reproduction and Embryology
Uterus and pregnancy |
Adhesion of menstrual endometrium to extracellular matrix: the possible role of integrin 
6ß1 and laminin interaction
1 Research Institute GROW, 2 Department of Obstetrics & Gynaecology, 3 Department of Pathology, Academisch Ziekenhuis Maastricht and Maastricht University, Maastricht, The Netherlands
Abstract
Previous in-vitro studies have shown that the endometrium preferentially adheres to the extracellular matrix (ECM) of the amnion and peritoneum. This interaction probably involves adhesion molecules, e.g. integrins. We evaluated the expression of integrins in naturally shed menstrual endometrium and the adhesion pattern of this tissue to different components of the ECM. To identify integrins and matrix components involved, blocking studies were performed. Most of the 15 menstrual tissue samples showed positive staining for each of the integrins investigated, except 
4ß1. Compared with binding to collagen IV, which was set at 100%, adhesion to collagen I was 93% (not significant), to fibronectin 87% (P < 0.05), and to laminin 74% (P < 0.05). Scanning electron micoscopy showed that endometrium adhered to laminin but hardly spread, whereas spreading was observed when layered on the other coatings. Compared with the control (which was set at 100%), incubation with 4B4, a monoclonal antibody against the integrin ß1 subunit, showed a significant reduction of adhesion (to ~50%; P < 0.05) when layered on laminin and a smaller reduction (to 82–86%; P < 0.05) when layered on the other three coatings. Incubation with antibody GOH3 against integrin 6ß1 resulted in a similar reduction in adhesion to laminin. Incubation with an RGD peptide significantly reduced adhesion (to 84%; P < 0.05) when plated on fibronectin. In conclusion, antegradely shed menstrual endometrium expresses various integrins. It shows preferential attachment to collagen IV and collagen I, when compared with fibronectin and laminin. Blockage of the integrin ß1 subunit resulted in greatest disruption to adhesion when layered on laminin, implying that the interaction was mediated by the 6ß1 integrin. Since this adhesion was not completely blocked, other mechanisms are likely to be involved.
blocking antibodies/cell culture/ectopic endometrium/menstruation/RGD peptide
Notes
4 To whom correspondence should be addressed at: Department of Obstetrics and Gynaecology, St Joseph Ziekenhuis, P.O Box 7777, 5500 MB, Veldhoven, The Netherlands
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