Adhesion of menstrual endometrium to extracellular matrix: the possible role of integrin alpha(6)beta(1) and laminin interaction

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Menstrual endometrium expresses integrins, and its adhesion to laminin is significantly reduced by antibodies against integrin alpha(6)beta(1), suggesting this integrin mediates the interaction.

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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 alpha(4)beta(1). 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 beta(1) subunit, showed a significant reduction of adhesion (to approximately 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 alpha(6)beta(1) 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 beta(1) subunit resulted in greatest disruption to adhesion when layered on laminin, implying that the interaction was mediated by the alpha(6)beta(1) integrin. Since this adhesion was not completely blocked, other mechanisms are likely to be involved.

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Condition tags

endometriosis

MeSH descriptors

Cell Adhesion Endometrium Endometrium Extracellular Matrix Integrins Laminin Menstruation Adult Antibodies, Monoclonal Cell Adhesion Endometriosis Endometriosis Endometrium Extracellular Matrix Female Humans Immunohistochemistry Integrin alpha6beta1 Integrins Integrins

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Source provenance

europepmc
last seen: 2026-06-11T06:19:48.454388+00:00
pubmed
last seen: 2026-05-13T22:13:41.710148+00:00
unpaywall
last seen: 2026-05-14T19:30:52.867331+00:00
License: public-domain-us · commercial use OK · attribution required
Courtesy of the U.S. National Library of Medicine