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Related Concept Videos

Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
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.
As the injured blood vessel contracts, endothelial cells undergo contraction, revealing collagen fibers in the basement membrane and underlying connective tissue. Furthermore, the plasma membrane of endothelial cells becomes adhesive, preparing the site for platelet adhesion. Platelets...
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.
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
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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...
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GPCR Desensitization

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Related Experiment Video

Updated: Jun 16, 2026

Characterizing Modulators of Protease-Activated Receptors with a Calcium Mobilization Assay Using a Plate Reader
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Characterizing Modulators of Protease-Activated Receptors with a Calcium Mobilization Assay Using a Plate Reader

Published on: May 24, 2024

A new plasminogen receptor.

Dudley K Strickland1

  • 1University of Maryland School of Medicine, USA.

Blood
|February 20, 2010
PubMed
Summary

Researchers discovered Plg-R(KT), a novel cell surface receptor that binds plasminogen and enhances fibrinolytic pathway activation. This finding advances understanding of blood clot breakdown mechanisms.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • The fibrinolytic pathway is crucial for dissolving blood clots.
  • Efficient fibrinolysis depends on concentrating plasminogen and its activators on cell surfaces.
  • Identifying cell surface receptors for plasminogen has been a significant challenge.

Discussion:

  • Andronicos and colleagues utilized a proteomics approach to identify novel cell surface proteins.
  • A 17-kDa transmembrane receptor, designated Plg-R(KT), was identified.
  • Plg-R(KT) exhibits high-affinity binding to plasminogen.

Key Insights:

  • Plg-R(KT) acts as a specific receptor for plasminogen on the cell surface.
  • The interaction between Plg-R(KT) and plasminogen facilitates the activation of the fibrinolytic system.

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Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus
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Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus

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Related Experiment Videos

Last Updated: Jun 16, 2026

Characterizing Modulators of Protease-Activated Receptors with a Calcium Mobilization Assay Using a Plate Reader
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Characterizing Modulators of Protease-Activated Receptors with a Calcium Mobilization Assay Using a Plate Reader

Published on: May 24, 2024

The Nijmegen Hemostasis Assay: Simultaneous Fluorogenic Measurement of Thrombin and Plasmin Generation in a Single Well
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The Nijmegen Hemostasis Assay: Simultaneous Fluorogenic Measurement of Thrombin and Plasmin Generation in a Single Well

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Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus
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Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus

Published on: June 2, 2023

  • This discovery provides a molecular target for understanding and potentially modulating fibrinolysis.
  • Outlook:

    • Further research into Plg-R(KT) function could reveal therapeutic targets for thrombotic disorders.
    • Investigating the structural basis of Plg-R(KT)-plasminogen interaction is warranted.
    • Exploring the role of Plg-R(KT) in other physiological or pathological processes is a future direction.