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Related Concept Videos

Anticoagulant Drugs: Low-Molecular-Weight Heparins01:30

Anticoagulant Drugs: Low-Molecular-Weight Heparins

Hemostasis is a crucial process that prevents excessive blood loss from damaged blood vessels. It involves various mechanisms such as vasoconstriction, platelet adhesion and activation, and fibrin formation. The importance of each mechanism depends on the type of vessel injury. In contrast, thrombosis is the abnormal formation of a blood clot within the blood vessels, leading to potential complications if the clot obstructs blood flow. Thrombosis can be caused by increased coagulability of the...
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.
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...
Formation of the Platelet Plug01:22

Formation of the Platelet Plug

The platelet phase, the second stage of hemostasis, commences around 15-20 seconds after an injury. It follows and overlaps with the vascular phase, during which blood vessels constrict to minimize blood loss.
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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...
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...

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Thrombin induces endothelial arginase through AP-1 activation.

Weifei Zhu1, Unni M Chandrasekharan, Smarajit Bandyopadhyay

  • 1Department of Cell Biology, The Cleveland Clinic Foundation, 9500 Euclid Ave., Cleveland, OH 44195, USA.

American Journal of Physiology. Cell Physiology
|December 25, 2009
PubMed
Summary

Thrombin upregulates arginase I in endothelial cells via the activating protein-1 (AP-1) site, involving c-Jun and ATF-2. This reveals a mechanism for arterial thrombosis-related endothelial dysfunction, suggesting arginase inhibition as a therapy.

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RNA-seq Analysis of Transcriptomes in Thrombin-treated and Control Human Pulmonary Microvascular Endothelial Cells
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Published on: February 13, 2013

Area of Science:

  • Molecular Biology
  • Cardiovascular Research
  • Endothelial Cell Biology

Background:

  • Arterial thrombosis causes severe ischemia and endothelial dysfunction.
  • L-arginine or arginase blockade can rescue endothelial dysfunction in animal models.
  • Thrombin exposure increases arginase I in rat aortic endothelial cells (RAECs).

Purpose of the Study:

  • To investigate the molecular mechanism of thrombin-induced arginase changes in endothelial cells.
  • To identify the specific regulatory elements and transcription factors involved in arginase I gene expression.

Main Methods:

  • Primary cultured RAECs were stimulated with thrombin.
  • Reporter gene assays with promoter deletions and point mutations identified the thrombin-responsive element.
  • Electrophoretic mobility shift assays (EMSA) and chromatin immunoprecipitation (ChIP) assays confirmed transcription factor binding.
  • Small interfering RNA (siRNA) was used for loss-of-function studies.
  • Western blotting assessed protein phosphorylation.

Main Results:

  • Thrombin significantly increased arginase I promoter and enzyme activity in RAECs.
  • An activating protein-1 (AP-1) consensus site at -3,157 bp was identified as a key thrombin-responsive element.
  • Thrombin stimulation led to the binding of c-Jun and activating transcription factor-2 (ATF-2) to the AP-1 site.
  • siRNA-mediated knockdown of c-Jun and ATF-2 blocked thrombin-induced arginase upregulation.
  • Thrombin induced the phosphorylation of stress-activated protein kinase/c-Jun-NH(2)-terminal kinase (SAPK/JNK) and p38 MAPK, leading to c-Jun and ATF-2 phosphorylation.

Conclusions:

  • The study elucidates the molecular basis for thrombin induction of endothelial arginase I.
  • The findings highlight the critical role of the AP-1 transcription factor complex (c-Jun/ATF-2) in this process.
  • Arginase inhibition presents a potential therapeutic strategy for arterial thrombosis and associated endothelial dysfunction.