AI Article Synopsis

  • Angiogenesis is essential for processes like development and healing, relying on signals from vascular endothelial growth factors (VEGFs) that activate endothelial cells to form new blood vessels.
  • The heparan sulfate proteoglycan (HSPG) Tmem184a acts as a heparin receptor that may regulate interactions between VEGF and its receptor, Vegfr2, influencing angiogenesis.
  • Research in zebrafish embryos shows that Tmem184a is crucial for forming intact intersegmental vessels (ISVs), as its knockdown leads to fewer vessels and indicates it works alongside Vegfr2b to ensure proper vascular organization.

Article Abstract

Angiogenesis, the outgrowth of new blood vessels from existing vasculature, is critical during development, tissue formation, and wound healing. In response to vascular endothelial growth factors (VEGFs), endothelial cells are activated to proliferate and move towards the signal, extending the vessel. These events are directed by VEGF-VEGF receptor (Vegfr2) signal transduction, which in turn is modulated by heparan sulfate proteoglycans (HSPGs). HSPGs are glycoproteins covalently attached to HS glycosaminoglycan chains. Transmembrane protein 184a (Tmem184a) has been recently identified as a heparin receptor, which is believed to bind heparan sulfate chains . Therefore, Tmem184a has the potential to fine-tune interactions between VEGF and HS, modulating Vegfr2-dependent angiogenesis. The function of Tmem184a has been investigated in the regenerating zebrafish caudal fin, but its role has yet to be evaluated during developmental angiogenesis. Here we provide insights into how Tmem184a contributes to the proper formation of the vasculature in zebrafish embryos. First, we find that knockdown of Tmem184a causes a reduction in the number of intact intersegmental vessels (ISVs) in the zebrafish embryo. This phenotype mimics that of knockout mutants, which have previously been shown to exhibit severe defects in ISV development. We then test the importance of HS interactions by removing the binding domain within the Tmem184a protein, which has a negative effect on angiogenesis. Tmem184a is found to act synergistically with Vegfr2b, indicating that the two gene products function in a common pathway to modulate angiogenesis. Moreover, we find that knockdown of Tmem184a leads to an increase in endothelial cell proliferation but a decrease in the amount of VE-cadherin present. Together, these findings suggest that Tmem184a is necessary for ISVs to organize into mature, complete vessels.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9478037PMC
http://dx.doi.org/10.3389/fphys.2022.845407DOI Listing

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