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Related Concept Videos

What are Second Messengers?01:12

What are Second Messengers?

Because many receptor binding ligands are hydrophilic, they do not cross the cell membrane and thus their message must be relayed to a second messenger on the inside. There are several second messenger pathways, each with their own way of relaying information. G-protein coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol path is active when the receptor induces phospholipase C to hydrolyze the phospholipid,...
Intracellular Signaling Cascades01:24

Intracellular Signaling Cascades

Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...
Amplifying Signals via Second Messengers01:15

Amplifying Signals via Second Messengers

Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
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...
Secondary Messengers in Hormone Action01:26

Secondary Messengers in Hormone Action

Water-soluble hormones cannot cross the plasma membrane, so they rely on protein receptors that span the membrane to trigger intracellular signaling pathways. These pathways then activate second messengers inside the cell, including cAMP or calcium ions.
Many hormones bind to transmembrane G protein-coupled receptors that connect to regulatory G proteins. These G proteins can then activate enzymes such as adenylyl cyclase or phospholipase C. Adenylyl cyclase converts ATP to cAMP, activating...
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Acute Inflammation II: Cellular Phase

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Related Experiment Video

Updated: Jun 7, 2026

Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells
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Cellular activation by thromboxane A2 and other eicosanoids

M Reilly1, G A Fitzgerald

  • 1Department of Medicine and Experimental Therapeutics, University College Dublin, Ireland.

European Heart Journal
|December 1, 1993
PubMed
Summary
This summary is machine-generated.

Thromboxane A2 (TXA2) is a key molecule in platelet activation and blood vessel constriction. Its complex biosynthesis and signaling pathways, involving G-protein coupled receptors, are crucial for cellular responses, particularly in cardiovascular health.

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Last Updated: Jun 7, 2026

Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells
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Characterizing Modulators of Protease-Activated Receptors with a Calcium Mobilization Assay Using a Plate Reader

Published on: May 24, 2024

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cardiovascular Physiology

Background:

  • Thromboxane A2 (TXA2), a cyclooxygenase (COX) product of arachidonic acid (AA), is vital for platelet activation and vasoconstriction, especially in acute coronary syndromes.
  • TXA2 biosynthesis regulation is complex, involving COX-2 and product-based inactivation, challenging the traditional view of AA liberation as the sole rate-limiting step.

Purpose of the Study:

  • To elucidate the intricate regulatory mechanisms of TXA2 formation and signaling.
  • To explore the molecular basis of TXA2 receptor heterogeneity and its associated G-protein signaling pathways.
  • To understand the desensitization processes of TXA2, PGI2, and PGE receptors.

Main Methods:

  • Analysis of cyclooxygenase (COX) gene regulation, including COX-2.
  • Investigation of thromboxane synthase activity and product inhibition.
  • Pharmacological characterization of G-protein coupled receptors (GPCRs) for TXA2, PGI2, and PGE.
  • Biochemical studies on G-protein coupling (Gq, Gs) and signaling cascades (PLC, adenylate cyclase).

Main Results:

  • Evidence suggests complex regulation of TXA2 biosynthesis beyond AA liberation, involving COX-2 and feedback inhibition.
  • TXA2 signaling is mediated by a Gq-linked receptor, potentially involving dual signaling mechanisms via G-protein alpha and beta-gamma subunits.
  • Receptor heterogeneity for TXA2 and prostacyclin (PGI2) is suggested, with distinct signaling pathways (PLC vs. adenylate cyclase).
  • Desensitization mechanisms for TXA2, PGI2, and PGE receptors involve potential COOH-terminal phosphorylation.

Conclusions:

  • TXA2 formation and signaling are tightly regulated through multiple complex pathways, including receptor-mediated G-protein activation.
  • The discovery of COX-2 and product inhibition highlights a sophisticated control of TXA2 biosynthesis.
  • Understanding these signaling pathways and receptor desensitization is critical for comprehending cardiovascular responses to eicosanoids.