O-079 In vitro human Implantation modelling reveals the role of lysophosphatidic acid and Rho-ROCK pathway in driving cell-in-cell mechanisms during the initial embryo-endometrial interactions during implantation Article Swipe
Andrea Palomar
,
Alicia Quiñonero
,
Irene Zorzan
,
Roberto Yagüe-Serrano
,
Elizabeth Morales Salinas
,
J Garrido
,
Amparo Mercader
,
Pilar Alamá
,
José Remohı́
,
Peter J. Rugg‐Gunn
,
M.Leonard Mole
,
Francisco Domı́nguez
·
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1093/humrep/deaf097.079
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1093/humrep/deaf097.079
Study question To decipher the mechanisms that control cell-in-cell (CIC) interactions between trophoblast and endometrial cells and contribute to the clearance of epithelial lining during human implantation. Summary answer CIC facilitates epithelial barrier clearance during implantation by internalizing epithelial cells into trophoblast, driven by lysophosphatidic acid (LPA) and active Rho-ROCK signalling at embryo-endometrial interface. What is known already During human embryo implantation, epithelial barrier rupture is essential to facilitate later stromal invasion. CIC role in this internalization process remains unexplored. Murine models suggest that LPA, generated by autotaxin (ATX) from LPC, activates Rho-ROCK signalling, promoting CIC internalization. This study characterizes CIC regulators in vitro and examines the impact of inhibiting ROCK and upstream regulators like ATX. Using a cell-engineered receptive endometrial scaffold technology (CREST) co-cultured with GFP-expressing human blastoids, we investigate LPC-LPA interplay in embryo-endometrial crosstalk. This live-imaging model precisely tracks CIC events, identifies different interacting embryo cell lineages, and assess how pathway disruptions affect implantation dynamics. Study design, size, duration ATX and LPA receptor (LPA3) were localized in vitro in hormone-stimulated primary human endometrial epithelial cells (hEnEC). Advanced 3D co-culture models were established using hormone-responsive CREST, integrating primary hEnEC and stromal (hEnSC) cells from healthy donors to recapitulate human endometrial cytoarchitecture. ROCK and ATX were selectively inhibited in endometrial compartments of CREST systems. Control, ROCK- and ATX-inhibited CREST models were co-cultured with human GFP-blastoids, and LPC-LPA levels were quantified at the blastoid-endometrial interface during implantation. Participants/materials, setting, methods ATX and LPA3 were localized by immunofluorescence in hormone-stimulated hEnEC (n = 5). To evaluate LPA-induced ROCK activation, LPA3, RhoA, and ROCK protein levels were quantified by western-blot in LPA-treated (10 µM,48h) and untreated hormone-stimulated hEnEC (n = 5/group). Specific immunoassays quantified LPC/LPA levels in control and ROCK/ATX-inhibited CREST (n = 5/group) before/after blastoid introduction (72h). CIC events and trophoblast adhesion were assessed via immunofluorescence, confocal microscopy, GFP signal tracking, and β-hCG quantifications throughout co-culture. Statistics:One- and two-way ANOVA(p < 0.05 significance threshold). Main results and the role of chance ATX and LPA3 were expressed in hormone-stimulated hEnEC. LPA treatment significantly increased RhoA and ROCK protein levels (2.5- and 3.8-fold, respectively; p<0.05) compared to controls. Basal LPC and LPA levels were detected in CREST before blastoid introduction. ATX inhibition in CREST led to LPC accumulation and reduced LPA secretion (p<0.01) when compared to control and ROCK-inhibited CREST. GFP-blastoids induced a substantial >10-fold increase in LPC secretion across all co-cultures (p<0.01). In control and ROCK-inhibited models, LPC levels subsequently decreased (p < 0.01), while LPA progressively increased after 48h (p < 0.05), indicating normal ATX-mediated LPC-to-LPA conversion. In contrast, ATX inhibition led to progressive LPC accumulation (p<0.01) and reduced LPA release (p<0.05), confirming impaired ATX activity. Confocal 3D-imaging confirmed hEnEC internalization by GATA3+ trophoblast cells, which was significantly reduced in ATX-inhibited CREST (p<0.05) leading to a 40% decrease in blastoid adhesion (p<0.05). While ROCK inhibition did not impair ATX, it resulted in a 50% reduction in blastoid adhesion (p < 0.05). Live-imaging confirmed GFP+ blastoid internalization of hEnEC under control conditions, whereas ROCK and ATX inhibition led to reduced CIC internalization, lower blastoid-associated GFP signal (p < 0.01), and progressive β-hCG decline (p < 0.05) over 72 hours, indicating impaired implantation. Limitations, reasons for caution This in vitro study would benefit from further validation of the mechanistic pathway in a larger sample size to strengthen the findings and assess reproducibility. Wider implications of the findings LPC-LPA interplay and active ROCK signaling at embryo-endometrial interface contribute to CIC-driven epithelial barrier rupture during blastocyst implantation. This research provides valuable insights into the existing knowledge gap in embryo implantation. A deeper understanding of this process may help identify underlying causes of implantation failure and inform potential therapeutic strategies. Trial registration number No
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Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1093/humrep/deaf097.079
- https://academic.oup.com/humrep/article-pdf/40/Supplement_1/deaf097.079/63539831/deaf097.079.pdf
- OA Status
- bronze
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4411746832
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- OpenAlex ID
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https://openalex.org/W4411746832Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1093/humrep/deaf097.079Digital Object Identifier
- Title
-
O-079 In vitro human Implantation modelling reveals the role of lysophosphatidic acid and Rho-ROCK pathway in driving cell-in-cell mechanisms during the initial embryo-endometrial interactions during implantationWork title
- Type
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articleOpenAlex work type
- Language
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enPrimary language
- Publication year
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2025Year of publication
- Publication date
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2025-06-01Full publication date if available
- Authors
-
Andrea Palomar, Alicia Quiñonero, Irene Zorzan, Roberto Yagüe-Serrano, Elizabeth Morales Salinas, J Garrido, Amparo Mercader, Pilar Alamá, José Remohı́, Peter J. Rugg‐Gunn, M.Leonard Mole, Francisco Domı́nguezList of authors in order
- Landing page
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https://doi.org/10.1093/humrep/deaf097.079Publisher landing page
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https://academic.oup.com/humrep/article-pdf/40/Supplement_1/deaf097.079/63539831/deaf097.079.pdfDirect link to full text PDF
- Open access
-
YesWhether a free full text is available
- OA status
-
bronzeOpen access status per OpenAlex
- OA URL
-
https://academic.oup.com/humrep/article-pdf/40/Supplement_1/deaf097.079/63539831/deaf097.079.pdfDirect OA link when available
- Concepts
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Lysophosphatidic acid, Embryo, In vitro, Cell biology, Cell, Andrology, Biology, Medicine, Internal medicine, Genetics, ReceptorTop concepts (fields/topics) attached by OpenAlex
- Cited by
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0Total citation count in OpenAlex
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10Other works algorithmically related by OpenAlex
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| abstract_inverted_index.implantation. | 27, 236, 529, 581, 594 |
| abstract_inverted_index.internalizing | 38 |
| abstract_inverted_index.introduction. | 366 |
| abstract_inverted_index.progressively | 414 |
| abstract_inverted_index.respectively; | 350 |
| abstract_inverted_index.significantly | 340, 456 |
| abstract_inverted_index.understanding | 597 |
| abstract_inverted_index.GFP-blastoids, | 225 |
| abstract_inverted_index.GFP-expressing | 127 |
| abstract_inverted_index.ROCK-inhibited | 385, 403 |
| abstract_inverted_index.p&lt;0.05) | 351 |
| abstract_inverted_index.&gt;10-fold | 391 |
| abstract_inverted_index.(p&lt;0.01) | 379, 435 |
| abstract_inverted_index.(p&lt;0.05) | 461 |
| abstract_inverted_index.Statistics:One- | 315 |
| abstract_inverted_index.cell-engineered | 119 |
| abstract_inverted_index.internalization | 77, 449, 494 |
| abstract_inverted_index.quantifications | 312 |
| abstract_inverted_index.(p&lt;0.01). | 399 |
| abstract_inverted_index.(p&lt;0.05), | 440 |
| abstract_inverted_index.(p&lt;0.05). | 470 |
| abstract_inverted_index.internalization, | 509 |
| abstract_inverted_index.internalization. | 97 |
| abstract_inverted_index.lysophosphatidic | 45 |
| abstract_inverted_index.reproducibility. | 558 |
| abstract_inverted_index.cytoarchitecture. | 202 |
| abstract_inverted_index.ROCK/ATX-inhibited | 287 |
| abstract_inverted_index.embryo-endometrial | 53, 135, 571 |
| abstract_inverted_index.hormone-responsive | 186 |
| abstract_inverted_index.hormone-stimulated | 172, 248, 274, 336 |
| abstract_inverted_index.immunofluorescence | 246 |
| abstract_inverted_index.blastoid-associated | 511 |
| abstract_inverted_index.immunofluorescence, | 304 |
| abstract_inverted_index.blastoid-endometrial | 233 |
| abstract_inverted_index.Participants/materials, | 237 |
| cited_by_percentile_year | |
| countries_distinct_count | 3 |
| institutions_distinct_count | 12 |
| citation_normalized_percentile.value | 0.29294054 |
| citation_normalized_percentile.is_in_top_1_percent | False |
| citation_normalized_percentile.is_in_top_10_percent | False |