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Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits.  Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl...
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The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
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Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
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The Glomerular Filtration Rate (GFR) is a measure of kidney function, reflecting the volume of filtrate formed per minute in the kidneys. On average, GFR is approximately 125 mL/min in males and 105 mL/min in females. Maintaining a relatively constant GFR is essential for the kidneys to effectively regulate body fluid homeostasis and maintain extracellular stability.
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Interrogating TGF-β Function and Regulation in Endothelial Cells.

J A Maring1, L A van Meeteren2, M J Goumans2

  • 1Department of Molecular Cell Biology, Cancer Genomics Centre Netherlands, Centre for Biomedical Genetics, Leiden University Medical Center, Postzone S-1-P, Postbus 9600, 2300 RC, Leiden, The Netherlands. j.a.maring@lumc.nl.

Methods in Molecular Biology (Clifton, N.J.)
|November 2, 2015
PubMed
Summary
This summary is machine-generated.

Transforming growth factor-β (TGF-β) is crucial for blood vessel formation (angiogenesis). This study details methods to analyze TGF-β

Keywords:
AngiogenesisEndothelial cellTGF-βVEGF

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Developmental Biology

Background:

  • Transforming growth factor-β (TGF-β) is a key cytokine regulating embryogenesis and tissue homeostasis.
  • TGF-β isoforms (TGF-β1, -β2, -β3) signal through receptor complexes involving serine/threonine kinases and Smad transcription factors.
  • Endothelial cell signaling diverges, with TGF-β activating ALK5 and ALK1, mediating opposing cellular responses.

Purpose of the Study:

  • To introduce methods for studying TGF-β function and regulation in angiogenesis.
  • To investigate the role of TGF-β signaling pathways in endothelial cells.
  • To provide techniques for analyzing TGF-β in both in vitro and ex vivo models.

Main Methods:

  • Utilizing in vitro assays with cultured endothelial cells.
  • Employing ex vivo metatarsal explant models.
  • Examining TGF-β receptor-mediated signaling pathways, including ALK1, ALK5, and the co-receptor endoglin.

Main Results:

  • TGF-β signaling is essential for angiogenesis, as evidenced by embryonic lethality in mice lacking TGF-β receptors.
  • Endoglin modulates TGF-β signaling by facilitating ALK1 and inhibiting ALK5 pathways.
  • Distinct type I receptors (ALK1 and ALK5) mediate opposing TGF-β effects in endothelial cells.

Conclusions:

  • TGF-β plays a pivotal role in angiogenesis through distinct receptor-mediated signaling pathways.
  • Understanding TGF-β regulation in endothelial cells is critical for developmental processes.
  • The presented methods allow for detailed functional and regulatory analysis of TGF-β in angiogenesis.