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Fibulin-1 mediates platelet adhesion via a bridge of fibrinogen
S Godyna, M Diaz-Ricart and WS Argraves
Biochemistry Department, J.H. Holland Laboratory, American Red Cross,
Rockville, MD, USA.
Fibulin-1 is a component of the extracellular matrix that surrounds
vascular smooth muscle. This observation, along with the recent finding
that fibulin-1 can bind fibrinogen (J Biol Chem 270:19458, 1995), prompted
investigation into the potential role of fibulin-1 as a thrombogenic agent.
In perfusion chamber assays, platelets in whole blood under flow conditions
attached and spread on surfaces coated with fibulin-1. This adhesion was
completely blocked by fibulin-1 antibodies. Platelets free of plasma did
not attach to fibulin-1 coated surfaces; however, with the addition of
fibrinogen, platelet adhesion to fibulin-1 took place. When detergent
extracts of platelets were subjected to fibulin-1-Sepharose affinity
chromatography, the integrin alpha IIb beta 3 was selected. Solid phase
binding assays using purified components showed that integrin alpha IIb
beta 3 could not bind directly to fibulin-1 but in the presence of
fibrinogen the integrin bound to fibulin-1-coated surfaces. Monoclonal
alpha IIb beta 3 antibodies capable of blocking its interaction with
fibrinogen completely blocked platelet adhesion to fibulin-1 in both whole
blood perfusion and static adhesion assays. The results show that fibulin-1
can support platelet attachment via a bridge of fibrinogen to the platelet
integrin alpha IIb beta 3. When fibroblast monolayers containing
extracellular matrix-incorporated fibulin-1 were used as adhesion
substrates, platelet adhesion in the presence of fibrinogen could be
inhibited by 30% using antibodies to fibulin-1. Following vascular injury,
fibulin-1 present in the extracellular matrix of the vessel wall may
therefore interact with plasma fibrinogen and promote platelet adhesion,
leading to the formation of a platelet plug. Thus, fibulin-1 joins the list
of matrix proteins including collagens I and IV and fibronectin that
mediate platelet adhesion via a plasma protein bridge. This bridging
phenomenon may represent a general mechanism by which platelets interact
with exposed subendothelial matrices following vascular injury.
Volume 88,
Issue 7,
pp. 2569-2577,
10/01/1996
Copyright © 1996 by The American Society of Hematology
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