ArticleTranslational oncology2026
Soluble N-terminal EphA2 fragment as a diagnostic biomarker and functional mediator of tumor progression in triple-negative breast cancer.
Article in Translational oncology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Triple-negative breast cancer (TNBC) lacks reliable biomarkers for early detection and remains a highly aggressive disease. Ephrin type-A receptor 2 (EphA2), a receptor tyrosine kinase frequently overexpressed in advanced cancers, undergoes MMP14-mediated cleavage that releases soluble N-terminal fragments. Here, we investigated the diagnostic and functional significance of this fragment in TNBC. Immunohistochemical analysis of clinical specimens revealed elevated EphA2 expression in TNBC tissues, with a trend toward higher levels in tumors of advanced stage and grade. To enable non-invasive detection, we established a dual-epitope sandwich ELISA targeting spatially distinct regions of the EphA2 extracellular domain. The assay showed concentration-dependent detection of recombinant EphA2 (EC₅₀, 48 ng/mL) and detected soluble EphA2 in TNBC cell-conditioned media. Serum analysis showed significantly higher EphA2 levels in TNBC patients compared with healthy controls (median 93.3 vs 25.6 ng/mL). In this exploratory cohort, ROC analysis yielded an AUC of 0.912 (95% CI, 0.862-0.962), with a sensitivity of 95.0% (95% CI, 86.3-98.6%) and a specificity of 78.3% (95% CI, 66.4-86.9%), and higher levels were associated with lymph node metastasis and higher histological grade. Functionally, recombinant EphA2-P328 promoted TNBC-cell migration and induced cell context-dependent changes in EMT-associated markers in vitro. Collectively, these findings support the soluble N-terminal EphA2 fragment as a candidate serum biomarker and an in vitro modulator of TNBC cell migration, warranting validation in larger independent cohorts and further mechanistic investigation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.