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Venous Thrombosis I: Introduction01:30

Venous Thrombosis I: Introduction

Venous thrombosis, the most common disorder of the veins, involves the formation of a thrombus or blood clot associated with vein inflammation. It can be classified as either superficial vein thrombosis or deep vein thrombosis.Superficial Vein Thrombosis: This involves the formation of a thrombus in a superficial vein, usually the greater or lesser saphenous vein. Though less severe than deep vein thrombosis (DVT), SVT can lead to complications if untreated.Deep Vein Thrombosis (DVT): This...
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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.
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Updated: May 31, 2026

Subcutaneous Angiotensin II Infusion using Osmotic Pumps Induces Aortic Aneurysms in Mice
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An unexpected link between angiotensinogen and thrombin.

Yunjie Wang1, Hermann Ragg

  • 1Department of Biotechnology, Faculty of Technology, Bielefeld University, Bielefeld, Germany.

FEBS Letters
|July 5, 2011
PubMed
Summary

Lamprey angiotensinogen effectively inhibits human alpha-thrombin, an activity enhanced by heparin. This discovery reveals an ancient role for angiotensinogen in regulating blood coagulation.

Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Hematology

Background:

  • Angiotensinogen is primarily known as the precursor to vasoactive hormones.
  • The distinct biochemical functions of angiotensinogen remain largely uncharacterized.
  • Lamprey angiotensinogen (L. fluviatilis) represents an opportunity to study an early-diverged vertebrate system.

Purpose of the Study:

  • To investigate the biochemical activity of angiotensinogen from the primitive vertebrate Lampetra fluviatilis.
  • To determine if lamprey angiotensinogen possesses inhibitory properties against thrombin.
  • To explore the evolutionary origins of thrombin regulation.

Main Methods:

  • Recombinant production of lamprey angiotensinogen.
  • Biochemical assays to measure alpha-thrombin inhibition.

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  • Analysis of kinetic parameters, including rate constants and stoichiometry of inhibition (SI).
  • Genomic and protein sequence analysis to infer evolutionary relationships.

    • Main Results:

    • Recombinant lamprey angiotensinogen demonstrated progressive inhibitory activity against human alpha-thrombin.
    • The second-order rate constant for inhibition was determined to be 2.6×10(4) M(-1) min(-1).
    • Heparin significantly enhanced this inhibitory activity (>800-fold) with a bell-shaped dose-response curve and an SI of 1.3.
    • Genomic and sequence data suggest a common ancestor for angiotensinogen and heparin cofactor II (HCII).

    Conclusions:

    • Lamprey angiotensinogen functions as an effective inhibitor of human alpha-thrombin.
    • Heparin potentiates the anticoagulant activity of lamprey angiotensinogen.
    • These findings suggest an ancient role for angiotensinogen in thrombin regulation, predating its role in the renin-angiotensin system.
    • Angiotensinogen and heparin cofactor II likely evolved from a shared ancestral thrombin antagonist.