LINC00607 facilitates endothelial VEGF-A receptor FLT1 splicing
- Mol Ther. 2026 Jul 1;34(7):4323-4338. doi: 10.1016/j.ymthe.2026.03.038.
- 1. Goethe University, Institute for Cardiovascular Physiology, Frankfurt, Germany; German Center of Cardiovascular Research (DZHK), Partner Site RheinMain, Frankfurt, Germany.
- 2. Goethe University, Institute for Cardiovascular Physiology, Frankfurt, Germany.
- 3. Goethe University, University Hospital Frankfurt, Division of Obstetrics and Prenatal Medicine, Frankfurt, Germany.
- 4. Technical University of Munich, Department of Cardiology, German Heart Centre Munich, School of Medicine and Health, Munich, Germany; DZHK, Partner Site Munich Heart Alliance, Munich, Germany.
- 5. Charité - Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Berlin, Germany; DZHK, Berlin, Germany.
- 6. Charité - Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Berlin, Germany; DZHK, Berlin, Germany; HELIOS Klinikum Berlin-Buch, Department of Cardiology and Nephrology, Berlin, Germany.
- 7. Goethe University, University Hospital Frankfurt, Department of Cardiovascular Surgery, Frankfurt, Germany.
- 8. German Center of Cardiovascular Research (DZHK), Partner Site RheinMain, Frankfurt, Germany; Goethe University, Institute for Cardiovascular Regeneration, Centre for Molecular Medicine, Frankfurt, Germany; Department of Physiology, Amsterdam Cardiovascular Sciences, VU Medical Center, Amsterdam UMC, Amsterdam, the Netherlands.
- 9. Institute for Neuroscience and Cardiovascular Research, University of Edinburgh, Edinburgh, Scotland; CARIM Institute, University of Maastricht, Maastricht, the Netherlands.
- 10. Max Planck Institute for Heart and Lung Research, Bad Nauheim, Germany.
- 11. Goethe University Frankfurt, Institute for Molecular Biosciences, Frankfurt, Germany; Max Planck Institute for Biophysics, Frankfurt, Germany.
- 12. Goethe University, Institute for Cardiovascular Physiology, Frankfurt, Germany; German Center of Cardiovascular Research (DZHK), Partner Site RheinMain, Frankfurt, Germany. Electronic address: [email protected].
Angiogenesis is a key function of vascular endothelial cells and becomes aberrant in pathologies such as preeclampsia. An important mediator of angiogenesis is vascular endothelial growth factor (VEGF) receptor FLT1; however, alternative splicing of FLT1 can generate soluble FLT1 (sFLT1), a decoy receptor that inhibits VEGF signaling. While some long non-coding RNAs (lncRNAs) are known to regulate splicing, their roles in endothelial biology remain poorly defined. Here, we identify lncRNA LINC00607 as a critical regulator of FLT1 alternative splicing. Loss of LINC00607 increased the formation of the anti-angiogenic sFLT1. CRISPR-mediated knockout of LINC00607 promoted exon 15 inclusion in FLT1, elevating sFLT1 levels and blunting VEGF-driven angiogenesis-a defect reversed by sFLT1-neutralizing antibodies. LINC00607 interacted with U2 small nuclear RNA (snRNA) to regulate exon 15 inclusion in FLT1, an interaction dependent on the chromatin-remodeler BRG1. A splice-blocking morpholino targeting the FLT1 intron14/exon15 junction specifically inhibited sFLT1 production by interacting with LINC00607 and U2 snRNA, and its application increased VEGF-A-mediated sprouting. LINC00607 expression inversely correlated with sFLT1 levels in vascular diseases. In preeclampsia, a multisystem pregnancy disorder involving hypertension and proteinuria, LINC00607 was downregulated in early and late-stage preeclampsia compared with healthy pregnancies. LINC00607 therefore fine-tunes VEGF signaling and might contribute to the pathophysiology of preeclampsia.
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Cat. No.Product NameDescriptionTargetResearch Area
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Research Areas: Cancer