Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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...
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...
Antiplatelet Drugs: Prostaglandin Synthesis, P2Y12 and Glycoprotein IIb/IIIa Inhibitors01:20

Antiplatelet Drugs: Prostaglandin Synthesis, P2Y12 and Glycoprotein IIb/IIIa Inhibitors

Antiplatelet drugs emerge as frontline defenders against the insidious threat of thromboembolic diseases, where abnormal clots obstruct vital blood vessels. These drugs stand as bulwarks, inhibiting platelet aggregation and clot formation, thereby mitigating the risk of life-threatening conditions like myocardial infarction, coronary artery disease, and thrombotic strokes.
Prostaglandin synthesis inhibitors, exemplified by the widely known aspirin, wield their power by irreversibly acetylating...
Structure and Function of Platelets01:18

Structure and Function of Platelets

The cell fragments known as platelets are disc-shaped, with an average diameter of about 3 μm and a thickness of roughly 1 μm. They play a crucial role in the body's vascular clotting system, which also involves plasma proteins, blood cells, and blood vessel tissues.
Platelets are continually replenished, circulating in the bloodstream for 9-12 days before being removed by phagocytes, primarily in the spleen. A microliter of circulating blood contains between 150,000 and 450,000 platelets, with...
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.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Structure and Function of Platelet Glycocalicin.

Thrombosis and haemostasis·2019
Same author

Thrombin binding to platelets defines functional receptors: inhibition of thrombin-induced platelet activation by catalytically-inactivated thrombin.

Platelets·2010
Same author

A note on external otitis.

British medical journal·2010
Same author

A Note on External Otitis.

British medical journal·2010
Same author

Low serum prostate-specific antigen levels in elderly rural African men at very low risk of prostate cancer.

European journal of cancer prevention : the official journal of the European Cancer Prevention Organisation (ECP)·2002
Same author

Both the high affinity thrombin receptor (GPIb-IX-V) and GPIIb/IIIa are implicated in expression of thrombin-induced platelet procoagulant activity.

Thrombosis and haemostasis·2001

Related Experiment Video

Updated: Jun 19, 2026

Platelet Adhesion and Aggregation Under Flow using Microfluidic Flow Cells
10:10

Platelet Adhesion and Aggregation Under Flow using Microfluidic Flow Cells

Published on: October 27, 2009

Reduced thrombin binding and aggregation in Bernard-Soulier platelets.

G A Jamieson, T Okumura

    The Journal of Clinical Investigation
    |March 1, 1978
    PubMed
    Summary
    This summary is machine-generated.

    Platelets from Bernard-Soulier disease patients exhibit reduced thrombin binding and aggregation, potentially explaining their bleeding issues. This study quantifies these binding differences in Bernard-Soulier platelets versus normal controls.

    More Related Videos

    Ferric Chloride-induced Murine Thrombosis Models
    10:37

    Ferric Chloride-induced Murine Thrombosis Models

    Published on: September 5, 2016

    Microfluidics in Assessing Platelet Function
    06:47

    Microfluidics in Assessing Platelet Function

    Published on: November 8, 2024

    Related Experiment Videos

    Last Updated: Jun 19, 2026

    Platelet Adhesion and Aggregation Under Flow using Microfluidic Flow Cells
    10:10

    Platelet Adhesion and Aggregation Under Flow using Microfluidic Flow Cells

    Published on: October 27, 2009

    Ferric Chloride-induced Murine Thrombosis Models
    10:37

    Ferric Chloride-induced Murine Thrombosis Models

    Published on: September 5, 2016

    Microfluidics in Assessing Platelet Function
    06:47

    Microfluidics in Assessing Platelet Function

    Published on: November 8, 2024

    Area of Science:

    • Hematology
    • Platelet Biology
    • Hemostasis

    Background:

    • Bernard-Soulier disease is a rare inherited bleeding disorder.
    • Platelets play a crucial role in hemostasis, and their interaction with thrombin is vital.

    Purpose of the Study:

    • To investigate thrombin binding and aggregation in platelets from Bernard-Soulier disease patients.
    • To compare thrombin binding characteristics between Bernard-Soulier platelets and normal controls.

    Main Methods:

    • Thrombin binding assays were performed on platelets from two Bernard-Soulier patients and normal controls.
    • High and low affinity binding sites and dissociation constants (Kd) were determined.
    • Platelet aggregation rates induced by various thrombin concentrations were measured.

    Main Results:

    • Bernard-Soulier platelets showed significantly fewer high-affinity (1,500 vs. 4,000 sites) and low-affinity (8,800 vs. 24,000 sites) thrombin binding sites compared to controls.
    • The dissociation constant (Kd) for thrombin binding was identical in both high (4.4 nM) and low (37 nM) affinity ranges for patients and controls.
    • Platelets from Bernard-Soulier patients exhibited a decreased rate of thrombin-induced aggregation at both optimal and suboptimal thrombin concentrations.

    Conclusions:

    • Reduced thrombin binding and impaired thrombin-induced aggregation in Bernard-Soulier platelets may contribute to the hemostatic defect.
    • The findings suggest a single class of thrombin binding sites on the platelet surface with consistent affinity in both normal and Bernard-Soulier platelets.