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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Extrinsic and Intrinsic Pathways of Hemostasis01:20

Extrinsic and Intrinsic Pathways of Hemostasis

Blood clotting or coagulation involves extrinsic and intrinsic pathways, which ultimately merge into the common pathway, forming a fibrin clot.
The Extrinsic Pathway
The extrinsic pathway of coagulation is typically initiated by tissue damage that exposes blood to tissue factor (TF), a protein released by the damaged tissue cells outside the blood vessels—this interaction with TF triggers biochemical reactions involving specific clotting factors. The key player here is Factor VII, which forms a...
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

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 are of three kinds RI, RII, and RIII. The RI...
Regulation of Angiogenesis and Blood Supply01:24

Regulation of Angiogenesis and Blood Supply

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 hydroxylase and factor...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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.
Some...
Clot Retraction and Fibrinolysis01:16

Clot Retraction and Fibrinolysis

After a fibrin clot is formed, the next step is clot retraction, a vital process facilitated by platelet contractile proteins, such as actin and myosin. These proteins pull the fibrin strands closer together and condense the clot. This action reduces the size of the clot, creating a smaller, denser structure that effectively seals off the damaged vessel. Clot retraction consolidates the clot and helps with wound healing by bringing the edges of the damaged blood vessel closer together.

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Related Experiment Video

Updated: May 26, 2026

Extracellular Vesicle Tissue Factor Activity Assay
03:53

Extracellular Vesicle Tissue Factor Activity Assay

Published on: December 29, 2023

Posttranslational modifications of tissue factor.

Saulius Butenas1, Jolanta Amblo-Krudysz, Kenneth G Mann

  • 1Department of Biochemistry, College of Medicine, University of Vermont, Burlington, VT 05446, USA. sbutenas@uvm.edu

Frontiers in Bioscience (Elite Edition)
|December 29, 2011
PubMed
Summary
This summary is machine-generated.

Posttranslational modifications impact tissue factor (TF) activity. Glycosylation enhances TF

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Extracellular Vesicle Tissue Factor Activity Assay
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Published on: December 29, 2023

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Published on: October 13, 2022

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Hematology

Background:

  • Tissue factor (TF) initiates blood coagulation in vivo.
  • TF is a membrane protein with critical roles in hemostasis.

Purpose of the Study:

  • To review the effects of posttranslational modifications on TF activity and properties.
  • To clarify the influence of specific modifications like glycosylation and disulfide bond formation.

Main Methods:

  • Literature review of published studies on TF posttranslational modifications.
  • Analysis of experimental data regarding TF activity and substrate interactions.

Main Results:

  • Glycosylation of TF's extracellular domain influences extrinsic FXase activity by increasing FX proteolysis rate.
  • TF glycosylation does not affect the FVIIa/TF complex activity with synthetic substrates, suggesting no impact on FVIIa interaction.
  • Evidence for direct influence of phosphorylation or palmitoylation on TF procoagulant activity is lacking.
  • The role of the Cys¹⁸⁶-Cys²⁰⁹ disulfide bond in TF activity remains debated.

Conclusions:

  • Specific TF modifications, particularly glycosylation, significantly affect its procoagulant activity, signaling, and trafficking.
  • The precise role of certain modifications, like the Cys¹⁸⁶-Cys²⁰⁹ disulfide bond, requires further investigation.