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Updated: Jul 28, 2025

Implantation of Fibrin Gel on Mouse Lung to Study Lung-specific Angiogenesis
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Fibrillin-1 regulates endothelial sprouting during angiogenesis.

Florian Alonso1,2, Yuechao Dong1,2, Ling Li3

  • 1Université de Bordeaux F-33000 Bordeaux, France.

Proceedings of the National Academy of Sciences of the United States of America
|May 30, 2023
PubMed
Summary

Fibrillin-1 is crucial for blood vessel formation (angiogenesis), and Marfan syndrome mutations impair this process. A specific fibrillin-1 fragment can correct these defects, offering potential therapeutic strategies.

Keywords:
Marfan Syndromeangiogenesisendothelial cellextracellular matrix proteinsfibrillin-1

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Area of Science:

  • Molecular Biology
  • Vascular Biology
  • Extracellular Matrix Biology

Background:

  • Fibrillin-1 is an extracellular matrix protein essential for microfibril assembly and tissue integrity, particularly in blood vessels.
  • Mutations in the fibrillin-1 gene cause Marfan syndrome, leading to cardiovascular, ocular, and skeletal abnormalities.
  • The role of fibrillin-1 in angiogenesis, the formation of new blood vessels, is not fully understood.

Purpose of the Study:

  • To investigate the role of fibrillin-1 in angiogenesis and its potential compromise in Marfan syndrome.
  • To explore the molecular mechanisms by which fibrillin-1 regulates endothelial cell behavior during angiogenesis.
  • To assess the therapeutic potential of fibrillin-1 fragments in correcting Marfan syndrome-associated angiogenic defects.

Main Methods:

  • Utilized a mouse retina vascularization model and cell culture experiments.
  • Analyzed fibrillin-1 and MAGP1 localization and deposition in angiogenic tissues.
  • Investigated the impact of fibrillin-1 deficiency on VEGF-A/Notch and Smad signaling pathways.
  • Administered a recombinant C-terminal fibrillin-1 fragment to Marfan syndrome model mice.
  • Performed mass spectrometry to identify proteins interacting with the fibrillin-1 fragment, including ADAMTS1.

Main Results:

  • Fibrillin-1 is present at the angiogenic front, colocalizing with MAGP1.
  • Marfan syndrome model mice (Fbn1C1041G/+) exhibited reduced MAGP1, impaired endothelial sprouting, and altered tip cell identity.
  • Fibrillin-1 deficiency disrupted VEGF-A/Notch and Smad signaling, affecting endothelial cell phenotype acquisition.
  • Treatment with a fibrillin-1 fragment restored normal angiogenesis and corrected defects in Marfan syndrome model mice.
  • The fibrillin-1 fragment altered the expression of proteins, including the metalloprotease ADAMTS1.

Conclusions:

  • Fibrillin-1 acts as a dynamic signaling platform regulating endothelial cell specification and matrix remodeling during angiogenesis.
  • Mutant fibrillin-1 impairs angiogenesis through disrupted signaling pathways and matrix composition.
  • Pharmacological intervention using a C-terminal fibrillin-1 fragment can rescue angiogenic defects in Marfan syndrome models.
  • Fibrillin-1, MAGP1, and ADAMTS1 are key regulators of endothelial sprouting, with implications for Marfan syndrome understanding and treatment.