Polyphosphate colocalizes with factor XII on platelet-bound fibrin and augments its plasminogen activator activity-Reference-Cited by-同舟云学术

Polyphosphate colocalizes with factor XII on platelet-bound fibrin and augments its plasminogen activator activity

Published:2016-12-15 Issue:24 Volume:128 Page:2834-2845
ISSN:0006-4971
Container-title:Blood
language:en
Short-container-title:

Author:

Mitchell Joanne L.¹^ORCID,Lionikiene Ausra S.¹,Georgiev Georgi¹,Klemmer Anja¹,Brain Chelsea¹,Kim Paul Y.²,Mutch Nicola J.¹^ORCID

Affiliation:

1. Institute of Medical Sciences, School of Medicine, Medical Sciences, and Nutrition, University of Aberdeen, Aberdeen, United Kingdom; and

2. Thrombosis and Atherosclerosis Research Institute, Department of Medicine, McMaster University, Hamilton, ON, Canada

Abstract

Key PointsPolyP significantly augments the plasminogen activator capacity of FXIIa. Platelet-bound fibrin acts as a reservoir for plasminogen, FXII(a), and polyP.

Publisher

American Society of Hematology

Subject

Cell Biology,Hematology,Immunology,Biochemistry

Link

http://ashpublications.org/blood/article-pdf/128/24/2834/1358166/blood673285.pdf

Reference65 articles.

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3. Surface-independent acceleration of factor XII activation by zinc ions. II. Direct binding and fluorescence studies;Bernardo;J Biol Chem,1993

4. Surface-independent acceleration of factor XII activation by zinc ions. I. Kinetic characterization of the metal ion rate enhancement;Bernardo;J Biol Chem,1993

5. The inositol-phospholipid-accelerated activation of prekallikrein by activated factor XII at physiological ionic strength requires zinc ions and high-Mr kininogen;Schousboe;Eur J Biochem,1990

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